PEPTIDE WITH MULTIPLE EPITOPES

Abstract

The present invention relates to peptides comprising multiple MHC Class II-binding T cell epitopes for tolerisation therapy.

Description

RELATED APPLICATIONS

[0001] This application is a continuation of U.S. patent application Ser. No. 12/673,386 (allowed), filed on Mar. 11, 2010, which is a national stage filing under 35 U.S.C. 371 of International Patent Application No. PCT/GB2008/002780, filed Aug. 15, 2008, which claims the benefit of British Patent Application No. 0715949.4, filed Aug. 15, 2007, British Patent Application No. 0716224.1, filed Aug. 20, 2007, and British Priority Application No. 0723337.2, filed Nov. 28, 2007.

FIELD OF THE INVENTION

[0002] The present invention relates to peptides comprising multiple MHC Class II-binding T cell epitopes for tolerisation therapy.

BACKGROUND OF THE INVENTION

[0003] T-cell antigen recognition requires antigen presenting cells (APCs) to present antigen fragments (peptides) on their cell surface in association with molecules of the major histocompatibility complex (MHC). T cells use their antigen specific T-cell receptors (TCRs) to recognise with high specificity the antigen fragments presented by the APC. Such recognition acts as a trigger to the immune system to generate a range of responses to eradicate the antigen which has been recognized.

[0004] Most of the specificity of T cell recognition of the antigen fragments is provided by a smaller subsequence of amino acids within the fragments. This subsequence is known as the T cell epitope. In the case of extracellular allergens and auto- or allo-antigens, the peptides are presented on MHC Class II molecules, which are recognized by CD4 T cells. Accordingly, interest in allergic and auto- or allo-immune disorders has focused on MHC Class II-binding T cell epitopes.

[0005] Given their role in the immune system, there is considerable interest in such epitopes for use as therapeutic agents to modulate the immune systems of subjects. For example, administration of peptide epitopes to subjects has been demonstrated to result in the induction of tolerance to the antigen from which the epitope derives. Therapeutic agents based on such an effect have great potential in the prevention and treatment of allergy, and auto- or allo-immune diseases where the down-regulation of an immune response is desirable.

SUMMARY OF THE INVENTION

[0006] The minimal amino acid sequence of a T cell epitope required for binding to MHC Class II-molecules can be precisely identified and generally comprises approximately nine amino acids. An epitope sequence typically binds specifically to a particular class of MHC Class II molecule, and does not bind to other MHC Class II molecules. Accordingly, the efficacy of a given epitope sequence varies greatly depending on the MHC Class II type of the individual to whom it is administered. To utilise an epitope for, e.g. the induction of tolerance, it is therefore necessary to undertake time-consuming and costly steps to identify the MHC Class II type of the individual to be tolerised.

[0007] The present inventors have made the finding that by incorporating multiple different epitope sequences, it is possible to produce a peptide which binds to multiple different classes of MHC Class II and is therefore effective when administered to a wider range of individuals, reducing the requirement to identify the MHC Class II type of an individual. Two or more epitope sequences may be combined in a peptide in an overlapping configuration, or as two independent sequences separated by amino acids which are not comprised in either epitope, without producing a peptide large enough to possess significant tertiary structure that would enable it to retain the conformation of an IgG or IgE-cross-linking epitope. Consequently the downstream immune responses to antigen caused by such cross-linking do not occur.

[0008] Accordingly, the present invention provides:

[0009] a peptide which has a length of 10 to 25 amino acids, the peptide comprising a region that comprises at least two different MHC class II-binding T cell epitope sequences, wherein the epitope sequences comprise at least 9 amino acids and derive from an antigenic protein, and wherein each epitope sequence binds to a different MHC class II molecule, and wherein the region is optionally flanked at the N and/or C terminus by additional amino acids which are not part of the epitope sequence. The peptide is typically suitable for use in tolerisation therapy. Polynucleotides, vectors and cells expressing the peptide of the invention, and methods of making the peptide of the invention are also provided.

DETAILED DESCRIPTION OF THE INVENTION

[0010] It is to be understood that references to inserting, deleting, replacing amino acids herein does not require the actual physical insertion, deletion or replacement of amino acids, and instead a peptide can be synthesized comprising sequence which represents (or is the end result of) the insertion, deletion or replacement having occurred.

Amino Acids

[0011] The table below shows the properties of amino acids.

TABLE-US-00001 Ala aliphatic, hydrophobic, neutral Met hydrophobic, neutral Cys polar, hydrophobic, neutral Asn polar, hydrophilic, neutral Asp polar, hydrophilic, charged (-) Pro hydrophobic, neutral Glu polar, hydrophilic, charged (-) Gln polar, hydrophilic, neutral Phe aromatic, hydrophobic, neutral Arg polar, hydrophilic, charged (+) Gly aliphatic, neutral Ser polar, hydrophilic, neutral His aromatic, polar, hydrophilic, Thr polar, hydrophilic, charged (+) neutral Ile aliphatic, hydrophobic, neutral Val aliphatic, hydrophobic, neutral Lys polar, hydrophilic, charged(+) Trp aromatic, hydrophobic, neutral Leu aliphatic, hydrophobic, neutral Tyr aromatic, polar, hydrophobic

MHC Class II-Binding T Cell Epitopes

[0012] The MHC Class II-binding T cell epitope comprised in the peptides of the invention is typically the minimal amino acid sequence that is capable of binding to Class II molecules and capable of stimulating T cells when presented in to T cells in association with Class II on the cell surface. The epitope is typically one that binds to a human MHC class II molecule.

[0013] An MHC Class II molecule consists of two proteins, .alpha. and .beta. each of which is encoded by a different gene. In humans, there are three clusters of genes encoding different .alpha. and .beta. proteins. These are the Human Leukocyte Antigen (HLA) clusters, DR, DQ and DP. Each cluster comprises multiple different A genes encoding different variant of the .alpha. protein and multiple different B genes encoding different variants of the .beta. protein. The resulting MHC Class II heterodimers are therefore extremely diverse, and correspondingly so are the T cell epitopes that they bind.

[0014] The binding site of MHC Class II molecules is composed of two separate proteins which form a cleft. The cleft is open-ended, which in theory allows a peptide of any length to bind. However, only 9 amino acids can occupy the cleft itself. The identities of the up to 9 amino acids which occupy the cleft define whether or not a given peptide will bind to a given MHC Class II molecule and be available for presentation to T cells. These up to 9 amino acids therefore represent the minimal sequence that is required for MHC Class II-binding. It is generally assumed that such a sequence will be capable of stimulating T cells when presented to T cells in association with Class II on the cell surface. However, this may be confirmed experimentally by methods standard in the art.

[0015] Such methods may typically comprise contacting the epitope with T cells in a sample taken from a subject, under conditions which allow the epitope and the T cells to interact; and then determining whether or not any of the T cells are stimulated. Determining whether or not the T cells are stimulated may be achieved by any suitable method, for example by detecting the production of cytokines by the T cells, wherein cytokine production indicates that T cells have been stimulated. Suitable cytokines include interferon gamma and interleukin 13. Cytokine production may be detected by any suitable method, for example an ELISA, ELISPOT assay or a flow cytometric assay. Particularly preferred methods include Multiplex bead array assays as described in, for example de Jager et al; Clinical and Diagnostic Laboratory Immunology, 2003, Vol 10(1) p. 133-139 The T cells in a sample from a subject are typically present in a population of peripheral blood mononuclear cells (PBMCs) isolated from a blood or serum sample taken from the subject.

[0016] The MHC Class II-binding T cell epitope of the invention typically consists of 8 or 9 amino acids, but may consist of 7, 10, 11, 12, 13, 14, 15 or 16 amino acids. The amino acid sequence of the epitope may be broadly defined by further reference to the binding site of MHC Class II molecules. This binding site has specific binding pockets, which corresponding to primary and secondary anchor positions in the sequence of the binding peptide epitope. The binding pockets are defined by amino acid positions in the sequence of the MHC Class II molecule, and are generally not absolutely discriminatory for a specific amino acid in the epitope. Therefore the peptide binding specificity of any given MHC molecule is relatively broad. Thus, peptides binding to the same MHC allotype exhibit some degree of similarity, but there is no requirement for identity.

[0017] For the most common human MHC Class II type, HLA-DR, the key anchor positions for binding to the binding pockets are at positions 1, 4, 6, 7 and 9 of the peptide epitope (counting from the most N terminal residue occupying the cleft to the most C terminal). Different HLA-DR alleles which have similar amino acids in their binding pockets therefore typically bind peptides with similar amino acids at positions 1, 4, 6, 7 and 9. Accordingly, the region containing an MHC Class II binding T cell epitope preferably has amino acids at positions corresponding to positions 1, 4, 6, 7 and 9 that allow binding to the widest range of HLA-DR alleles. Examples of characteristic binding properties of different HLA-DR alleles are set out below:

[0018] DR alleles with Glycine at position 86 of the .beta. chain show strong preferences for large hydrophobic side chains (Trp, Tyr, Phe) at peptide position 1, whereas Valine at position 86 restricts the pocket size and alters the preferences to small hydrophobic side chains (Val and Ala) at this position. Medium sized hydrophobic amino acids Leu and Be are well accepted in all DR alleles.

[0019] DR alleles with Gln at position 70, Lysine at position 71, and Arginine or Gln at position 74 of the .beta. chain have an overall positive charge within pocket 4, which requires negatively charged amino acids Asp and Glu at position 4 of the binding peptide (as in for example, DRB1*0301). DR alleles with this motif are associated with two autoimmune diseases: systematic lupus erythematosus and Hashimoto's thyroiditis.

[0020] DR alleles with Gln or Arg at position 70, Arg or Lys at position 71 and Glu or Ala at position 74 of the .beta. chain bind similar peptides to those directly above since the only significant difference is at position 74. However, when Ala is present at position 74, pocket 4 increases in size and can accommodate larger amino acids such as Phe, Trp, and Ile (as in for example DRB1*0401, 04, 05). Alleles bearing Glu at position 74 are expected to allow small polar residues, like Ser and Thr at position 4 of the binding peptide. DR alleles with this motif are associated with a susceptibility to rheumatoid arthritis.

[0021] DR alleles with Asp at position 70, Glu or Arg at position 71, and Leu or Ala at position 74 of the .beta. chain exclude peptides with negatively charged amino acids at peptide position 4 (for example DRB1*0402). This is due to the presence of Asp at position 70. DR alleles with this motif are associated with the autoimmune diseases Juvenile rheumatoid arthritis (JRA), pemphigus vulgaris, and allergic bronchopulmonary.

[0022] Polymorphisms at position 9 of the .beta. chain define the size of binding pocket 9 in all DR alleles. Alleles with Trp at this position accept only small amino acids in position 9 of the binding peptide, e.g. Ala, Val, Gly, Ser, Thr, Pro (as in for example DRB1*0101 and *1501). Glu at position 9, in combination with Asp at position 57, makes pocket 9 negatively charged, facilitating the accommodation of positively charged amino acids, such as Lys (as in for example DRB1*0401 and *0404) and Histine (as in for example DRB1*0402). In most MHC class II alleles, Asp at position 57 makes a salt-bridged hydrogen bond with Arg at position 76, allowing the pocket to also accommodate aliphatic and polar amino acids. In cases where Asp at position 57 is replaced by Ser (for example DRB1*0405) or Ala (DQ8), the hydrogen bonding network is destroyed and Arg at position 76 can strongly attract negatively charged amino acids such as Asp or Glu at position 9 of the binding peptide (as in for example DRB1*0405).

[0023] An example of a preferred sequence for an epitope therefore has Trp, Tyr, Phe, Val or Ala at position 1; Asp, Glu, Ser or Thr at position 4; and Ala, Val, Gly, Ser, Thr, Pro at position 9. A further example of a preferred sequence for an epitope has a large aromatic or hydrophobic amino acid at position 1, for example Tyr, Phe, Trp, Leu, Ile or Val, and a small, non-charged amino acid at position 6, for example Ser, Thr, Ala, Pro, Val, Ile or Met. Approximately 87.5% of peptides binding to all or a combination of the MHC Class II molecules encoded by the DRB1*0101, *0401 and *0701 alleles contain this motif. Furthermore, since T cell epitopes derived from allergens and autoimmune antigens do not typically contain a large number of repeats of a given amino acid or amino acids, preferred epitopes of the invention typically comprise at least 5, 6, 7 or 8 different amino acids.

[0024] The precise amino sequence of an epitope may be predicted by computer-based algorithms and confirmed by in vitro biochemical analysis. Suitable commercially available algorithms include the EpiMatrix algorithm (EpiVax Inc.). Other algorithms are available at, for example, the website at the ProPed MHC Class-II Binding Peptide Prediction Server. Analysis with these algorithms typically comprises parsing a larger polypeptide sequence into multiple overlapping small peptides. The sequences of these small peptides are then analysed using the algorithm to identify those which are predicted to bind MHC Class II molecules. The overlapping small peptides are typically 9-mers.

[0025] The candidate peptides which score most highly in this analysis are then assessed for the ability to bind a panel of MHC Class II molecules encoded by different Class II alleles in vitro using standard binding assays. For example a competitive MHC class II binding assay may be used, wherein each peptide is analysed for its ability to displace a known control binder from each of the human MHC class II allotypes investigated. In such an assay each peptide is assigned an IC.sub.50 value (the concentration at which 50% inhibition of control peptide binding is achieved). The lower the IC.sub.50 the higher the affinity of a peptide for a given MHC class II allotype.

[0026] The epitope or epitopes in a polypeptide are taken to be those peptides which show the highest binding affinity to MHC Class II molecules. Particularly preferred epitopes show high affinity binding to different Class II molecules encoded by more than one preferably two, more preferably three, four or five MHC Class II alleles.

[0027] It will be appreciated that biochemical assays for the identification of a T cell epitope are not typically able to precisely define the position of the minimal epitope sequence within a larger sequence more accurately than to within approximately 12 amino acids, and more typically 15, 20 or more amino acids. The reason for this is that a large sequence must be physically fragmented into smaller overlapping peptides, or smaller overlapping peptides must be manufactured de novo prior to in vitro assessment of the ability of these peptides to bind MHC Class II molecules. The skilled person will recognise that the smaller the overlapping peptide fragments used, the more time-consuming and labour intensive is the process of manufacture. Hence epitopes are often identified as being contained within a larger polypeptide region. It is envisaged that the epitopes of the invention may be defined as such a larger region.

[0028] In all cases, it is envisaged that the epitope sequences of the invention also comprise functional variants of the epitope sequences. A functional variant epitope sequence is any homologous epitope sequence which is able to stimulate a T cell that specifically recognise the native epitope sequence from which the variant derives, or which is able to induce tolerance to the native epitope sequence in an individual. Such a variant typically has at least 55%, preferably 60%, 65%, 70%, 75%, 80%, 85%, 90%, 95% or 99% homology to the native epitope sequence. Suitable methods for determining the stimulatory effect of a variant epitope are known in the art. For example, a sample of peripheral blood mononuclear cells (PBMCs) can be stimulated with the protein from which the native epitope derives at various cell densities. After one week of culture, the T cell cultures are restimulated with autologous antigen presenting cells pulsed with peptides consisting of the native epitope sequence, which produces T cell lines specific for the native epitope sequence. The resulting lines can then be tested to see if they are stimulated by any variant epitope sequence, with stimulation being correlated with, e.g. proliferation or production of cytokines, in particular interferon-gamma, interleukin-13 and interleukin-17.

Regions Containing at Least Two MHC Class II-Binding T Cell Epitopes

[0029] As set out above, the bioinformatic techniques used to identify epitopes may identify multiple epitopes in the same polypeptide. Each of these multiple epitopes typically binds to different types of MHC Class II molecule. That is, a first epitope may bind Class II molecules encoded by alleles w, x, and y, whereas a second epitope binds Class II molecules encoded by alleles x, y and z. Since the region of the invention comprises at least two different epitope sequences, the peptides of the invention are capable of binding to a large number of different MHC Class II molecules.

[0030] The multiple different epitope sequences may be comprised in a region as two or more overlapping epitopes. For example, in a sequence of 12 amino acids, one epitope corresponds to amino acids 1 to 9 and a second epitope corresponds to amino acids 4 to 12. A peptide region comprising amino acids 1 to 12 will therefore comprise two overlapping epitope sequences since both epitopes comprise the contiguous sequence of amino acids 4 to 9.

[0031] The overlap of sequence between any two epitopes may typically comprise a contiguous sequence of upto approximately 10%, 20%, 30%, 40%, 50%, 60%, 65%, 70%, 80% or 90% of the amino acids from the N or C terminus either epitope. Therefore, assuming an epitope length of 9 amino acids, a second epitope may comprise the contiguous sequence of 1, 2, 3, 4, 5, 6, 7 or 8 amino acids at the N terminal of a first epitope, with additional amino acids present at the N terminus of this sequence which are not comprised in the first epitope, or may comprise the contiguous sequence of 1, 2, 3, 4, 5, 6, 7 or 8 amino acids at the C terminal of a first epitope, with additional amino acids present at the C terminus of this sequence which are not comprised in the first epitope.

[0032] A preferred overlap of sequence between any two epitopes typically comprises a contiguous sequence of upto approximately 65% of the amino acids from the N or C terminus either epitope. For an epitope length of 9 amino acids, a second epitope may therefore comprise the contiguous sequence of 6 amino acids at the N terminal of a first epitope, with additional amino acids present at the N terminus of this sequence which are not comprised in the first epitope, or may comprise the contiguous sequence of 6 amino acids at the C terminal of a first epitope, with additional amino acids present at the C terminus of this sequence which are not comprised in the first epitope.

[0033] Alternatively, the multiple epitopes in the region may be two or more independent sequences. The independent sequences may be consecutive or may be separated by additional amino acids which are not comprised in an epitope. As an example of the former case, in a sequence of 18 amino acids, one epitope corresponds to amino acids 1 to 9 and a second epitope corresponds to amino acids 10 to 18. As an example of the latter case, in a sequence of 19 amino acids, one epitope corresponds to amino acids 1 to 9 and a second epitope corresponds to amino acids 11 to 19. In this example, amino acid 10 is not comprised in either epitope. In general terms, two independent epitope sequences may typically be separated by 1, 2, 3, 4, 5, 6 or 7 additional amino acids which are not comprised in either epitope.

[0034] The amino acid sequence separating the epitope sequences ("the additional amino acid(s)") may comprise any amino acid sequence. It is particularly preferred that the additional amino acid(s) comprise a high proportion of hydrophilic amino acids (typically>60%) and comprise no cysteine residues.

[0035] In one preferred embodiment, the sequence of the additional amino acid(s) is identical to or homogolous to the sequence of the amino acid(s) which separates the epitope sequences in the native sequence of the protein from which the epitopes derive. If the additional amino acid(s) are homolgous to the native sequence, homology of greater than 55%, 60%, 75%, 80%, 85%, 90% or 95% with the native sequence is preferred. In an alternative embodiment, the sequence of the additional amino acid(s) is not related to the sequence of the amino acid(s) which separates the epitope sequences in the native sequence of the protein from which the epitopes derive. That is, the region may comprise a fusion protein comprising a first epitope, a sequence of additional amino acids, and at least a second epitope.

[0036] Alternatively the multiple epitopes may be present in the region as a combination of overlapping or independent epitope sequences.

[0037] It will be appreciated that the region may therefore consist entirely of amino acids which are comprised in at least one epitope. Typically, the proportion of amino acids in a region which are comprised in at least one epitope is approximately 70%, 71%, 72%, 73%, 74%, 75%, 80%, 85%, 90% or 95%, or 99%. Preferably, at least 70% of the amino acids in a region are comprised in at least one epitope.

[0038] The region therefore typically has a length of approximately 18 amino acids, but may be 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24 or 25 amino acids in length.

Peptides

[0039] The peptides of the invention may consist entirely of the region as defined above. However, the peptides may optionally comprise additional amino acids flanking the N or C termini of the region. These amino acids are not comprised in an epitope. Typically, the proportion of amino acids in a peptide which are comprised in at least one epitope is approximately 70%, 71%, 72%, 73%, 74%, 75%, 80%, 85%, 90% or 95%, or 99%. Preferably, at least 70% of the amino acids in a peptide are comprised in at least one epitope.

[0040] The residues flanking the region typically result in the peptide having a solubility greater than 3.5 mg/ml in aqueous solution at pH 2.0 to 12.0, or pH 2.0 to 11.0, pH 2.0 to 10.0, pH 2.0 to 9.0, pH 2.0 to 8.0 or pH 2.0 to 7.0. The residues flanking the region are preferably:

[0041] at the N terminus, at least one, two, three, four, five or six contiguous amino acids corresponding to the at least one, two, three, four, five or six contiguous amino acids immediately N terminal to the region in the natural sequence of the protein from which the region derives; or

[0042] at the C terminus, at least one, two, three, four, five or six contiguous amino acids corresponding to the at least one, two, three, four, five or six contiguous amino acids immediately C terminal to the epitope sequence in the natural sequence of the protein from which the region derives; or

[0043] at both the N and C termini, at least one, preferably two, or three amino acids selected from arginine, lysine, histidine, glutamate and aspartate.

[0044] Further, the peptide may comprise the region as defined above, but incorporating modification of its native sequence. Particularly preferred modifications regions wherein:

[0045] any cysteine residues in the native sequence of the region are replaced with serine; and/or

[0046] any hydrophobic residues in the up to one, two, preferably three or four amino acids at the N or C terminus of the native sequence of the region which are not comprised in the epitope are deleted; and/or

[0047] any two consecutive amino acids comprising the sequence Asp-Gly in the up to three or preferably four amino acids at the N or C terminus of the native sequence of the region which are not comprised in the epitope are deleted.

[0048] The peptides of the invention typically contain from 10 to 25 amino acids, and may contain 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23 or 24 amino acids. Peptides longer than 25 amino acids are likely to possess sufficient tertiary structure to cross-link IgG or IgE on cell surfaces resulting in undesirable immune responses such as B cell activation or mast cell degranulation. Peptides shorter than 10 amino acids are unlikely to contain more than one epitope.

Peptide Synthesis

[0049] The peptides of the invention are derived in an intellectual sense from the polypeptide which comprises the epitopes and regions as defined above with additional flanking residues or residues to separate independent epitope sequences. This is done by making use of the amino acid sequence of the region or epitope and synthesising peptides based on the sequence. Peptides may be synthesised using methods well known in the art. Preferred methods include solid-phase peptide synthesis techniques and most preferably preferably an automated or semiautomated peptide synthesizer. Typically, using such techniques, an .alpha.-N-carbamoyl protected amino acid and an amino acid attached to the growing peptide chain on a resin are coupled at room temperature in an inert solvent such as dimethylformamide, N-methylpyrrolidinone or methylene chloride in the presence of coupling agents such as dicyclohexylcarbodiimide and 1-hydroxybenzotriazole in the presence of a base such as diisopropyl-ethylamine. The .alpha.-N-carbamoyl protecting group is removed from the resulting peptide-resin using a reagent such as trifluoroacetic acid or piperidine, and the coupling reaction repeated with the next desired N-protected amino acid to be added to the peptide chain. Suitable N-protecting groups are well known in the art, and include t-butyloxycarbonyl (tBoc) and fluorenylmethoxycarbonyl (Fmoc).

[0050] The term "peptide" includes not only molecules in which amino acid residues are joined by peptide (--CO--NH--) linkages but also molecules in which the peptide bond is reversed. Such retro-inverso peptidomimetics may be made using methods known in the art, for example such as those described in Meziere et al (1997) J. Immunol.159, 3230-3237. This approach involves making pseudopeptides containing changes involving the backbone, and not the orientation of side chains. Meziere et al (1997) show that, at least for MHC class II and T helper cell responses, these pseudopeptides are useful. Retro-inverse peptides, which contain NH--CO bonds instead of CO--NH peptide bonds, are much more resistant to proteolysis.

[0051] Similarly, the peptide bond may be dispensed with altogether provided that an appropriate linker moiety which retains the spacing between the carbon atoms of the amino acid residues is used; it is particularly preferred if the linker moiety has substantially the same charge distribution and substantially the same planarity as a peptide bond. It will also be appreciated that the peptide may conveniently be blocked at its N-or C-terminus so as to help reduce susceptibility to exoproteolytic digestion. For example, the N-terminal amino group of the peptides may be protected by reacting with a carboxylic acid and the C-terminal carboxyl group of the peptide may be protected by reacting with an amine. Other examples of modifications include glycosylation and phosphorylation. Another potential modification is that hydrogens on the side chain amines of R or K may be replaced with methylene groups (--NH.sub.2.fwdarw.-NH(Me) or --N(Me).sub.2).

[0052] Analogues of peptides according to the invention may also include peptide variants that increase or decrease the peptide's half-life in vivo. Examples of analogues capable of increasing the half-life of peptides used according to the invention include peptoid analogues of the peptides, D-amino acid derivatives of the peptides, and peptide-peptoid hybrids. A further embodiment of the variant polypeptides used according to the invention comprises D-amino acid forms of the polypeptide. The preparation of polypeptides using D-amino acids rather than L-amino acids greatly decreases any unwanted breakdown of such an agent by normal metabolic processes, decreasing the amounts of agent which needs to be administered, along with the frequency of its administration.

Polynucleotides, Vectors and Cells

[0053] The terms "nucleic acid molecule" and "polynucleotide" are used interchangeably herein and refer to a polymeric form of nucleotides of any length, either deoxyribonucleotides or ribonucleotides, or analogs thereof. Non-limiting examples of polynucleotides include a gene, a gene fragment, messenger RNA (mRNA), cDNA, recombinant polynucleotides, plasmids, vectors, isolated DNA of any sequence, isolated RNA of any sequence, nucleic acid probes, and primers. A polynucleotide of the invention may be provided in isolated or purified form. A nucleic acid sequence which "encodes" a selected polypeptide is a nucleic acid molecule which is transcribed (in the case of DNA) and translated (in the case of mRNA) into a polypeptide in vivo when placed under the control of appropriate regulatory sequences. The boundaries of the coding sequence are determined by a start codon at the 5' (amino) terminus and a translation stop codon at the 3' (carboxy) terminus. For the purposes of the invention, such nucleic acid sequences can include, but are not limited to, cDNA from viral, prokaryotic or eukaryotic mRNA, genomic sequences from viral or prokaryotic DNA or RNA, and even synthetic DNA sequences. A transcription termination sequence may be located 3' to the coding sequence.

[0054] Polynucleotides of the invention can be synthesised according to methods well known in the art, as described by way of example in Sambrook et al (1989, Molecular Cloning--a laboratory manual; Cold Spring Harbor Press).

[0055] The polynucleotide molecules of the present invention may be provided in the form of an expression cassette which includes control sequences operably linked to the inserted sequence, thus allowing for expression of the peptide of the invention in vivo in a targeted subject. These expression cassettes, in turn, are typically provided within vectors (e.g., plasmids or recombinant viral vectors) which are suitable for use as reagents for nucleic acid immunization. Such an expression cassette may be administered directly to a host subject. Alternatively, a vector comprising a polynucleotide of the invention may be administered to a host subject. Preferably the polynucleotide is prepared and/or administered using a genetic vector. A suitable vector may be any vector which is capable of carrying a sufficient amount of genetic information, and allowing expression of a peptide of the invention.

[0056] The present invention thus includes expression vectors that comprise such polynucleotide sequences. Thus, the present invention provides a vector for use in preventing or treating allergy by tolerisation comprising four or more polynucleotide sequences which encode different polypeptides of the invention and optionally one or more further polynucleotide sequences which encode different polypeptides as defined herein. The vector may comprise 4, 5, 6 or 7 polynucleotide sequences which encode different polypeptides of the invention.

[0057] Furthermore, it will be appreciated that the compositions and products of the invention may comprise a mixture of polypeptides and polynucleotides. Accordingly, the invention provides a composition or product as defined herein, wherein in place of any one of the polypeptide is a polynucleotide capable of expressing said polypeptide.

[0058] Expression vectors are routinely constructed in the art of molecular biology and may for example involve the use of plasmid DNA and appropriate initiators, promoters, enhancers and other elements, such as for example polyadenylation signals which may be necessary, and which are positioned in the correct orientation, in order to allow for expression of a peptide of the invention. Other suitable vectors would be apparent to persons skilled in the art. By way of further example in this regard we refer to Sambrook et al.

[0059] Thus, a polypeptide of the invention may be provided by delivering such a vector to a cell and allowing transcription from the vector to occur. Preferably, a polynucleotide of the invention or for use in the invention in a vector is operably linked to a control sequence which is capable of providing for the expression of the coding sequence by the host cell, i.e. the vector is an expression vector.

[0060] "Operably linked" refers to an arrangement of elements wherein the components so described are configured so as to perform their usual function. Thus, a given regulatory sequence, such as a promoter, operably linked to a nucleic acid sequence is capable of effecting the expression of that sequence when the proper enzymes are present. The promoter need not be contiguous with the sequence, so long as it functions to direct the expression thereof. Thus, for example, intervening untranslated yet transcribed sequences can be present between the promoter sequence and the nucleic acid sequence and the promoter sequence can still be considered "operably linked" to the coding sequence.

[0061] A number of expression systems have been described in the art, each of which typically consists of a vector containing a gene or nucleotide sequence of interest operably linked to expression control sequences. These control sequences include transcriptional promoter sequences and transcriptional start and termination sequences. The vectors of the invention may be for example, plasmid, virus or phage vectors provided with an origin of replication, optionally a promoter for the expression of the said polynucleotide and optionally a regulator of the promoter. A "plasmid" is a vector in the form of an extrachromosomal genetic element. The vectors may contain one or more selectable marker genes, for example an ampicillin resistence gene in the case of a bacterial plasmid or a resistance gene for a fungal vector. Vectors may be used in vitro, for example for the production of DNA or RNA or used to transfect or transform a host cell, for example, a mammalian host cell. The vectors may also be adapted to be used in vivo, for example to allow in vivo expression of the polypeptide.

[0062] A "promoter" is a nucleotide sequence which initiates and regulates transcription of a polypeptide-encoding polynucleotide. Promoters can include inducible promoters (where expression of a polynucleotide sequence operably linked to the promoter is induced by an analyte, cofactor, regulatory protein, etc.), repressible promoters (where expression of a polynucleotide sequence operably linked to the promoter is repressed by an analyte, cofactor, regulatory protein, etc.), and constitutive promoters. It is intended that the term "promoter" or "control element" includes full-length promoter regions and functional (e.g., controls transcription or translation) segments of these regions.

[0063] A polynucleotide, expression cassette or vector according to the present invention may additionally comprise a signal peptide sequence. The signal peptide sequence is generally inserted in operable linkage with the promoter such that the signal peptide is expressed and facilitates secretion of a polypeptide encoded by coding sequence also in operable linkage with the promoter.

[0064] Typically a signal peptide sequence encodes a peptide of 10 to 30 amino acids for example 15 to 20 amino acids. Often the amino acids are predominantly hydrophobic. In a typical situation, a signal peptide targets a growing polypeptide chain bearing the signal peptide to the endoplasmic reticulum of the expressing cell. The signal peptide is cleaved off in the endoplasmic reticulum, allowing for secretion of the polypeptide via the Golgi apparatus. Thus, a peptide of the invention may be provided to an individual by expression from cells within the individual, and secretion from those cells.

[0065] Alternatively, polynucleotides of the invention may be expressed in a suitable manner to allow presentation of a peptide of the invention by an MHC class II molecule at the surface of an antigen presenting cell. For example, a polynucleotide, expression cassette or vector of the invention may be targeted to antigen presenting cells, or the expression of encoded peptide may be preferentially stimulated or induced in such cells.

[0066] In some embodiments, the polynucleotide, expression cassette or vector will encode an adjuvant, or an adjuvant will otherwise be provided. As used herein, the term "adjuvant" refers to any material or composition capable of specifically or non-specifically altering, enhancing, directing, redirecting, potentiating or initiating an antigen-specific immune response.

[0067] Polynucleotides of interest may be used in vitro, ex vivo or in vivo in the production of a peptide of the invention. Such polynucleotides may be administered or used in the prevention or treatment of allergy by tolerisation.

[0068] Methods for gene delivery are known in the art. See, e.g., U.S. Pat. Nos. 5,399,346, 5,580,859 and 5,589,466. The nucleic acid molecule can be introduced directly into the recipient subject, such as by standard intramuscular or intradermal injection; transdermal particle delivery; inhalation; topically, or by oral, intranasal or mucosal modes of administration. The molecule alternatively can be introduced ex vivo into cells that have been removed from a subject. For example, a polynucleotide, expression cassette or vector of the invention may be introduced into APCs of an individual ex vivo. Cells containing the nucleic acid molecule of interest are re-introduced into the subject such that an immune response can be mounted against the peptide encoded by the nucleic acid molecule. The nucleic acid molecules used in such immunization are generally referred to herein as "nucleic acid vaccines."

[0069] The polypeptides, polynucleotides, vectors or cells of the invention may be present in a substantially isolated form. They may be mixed with carriers or diluents which will not interfere with their intended use and still be regarded as substantially isolated. They may also be in a substantially purified form, in which case they will generally comprise at least 90%, e.g. at least 95%, 98% or 99%, of the proteins, polynucleotides, cells or dry mass of the preparation.

Formulations and Compositions

[0070] The peptides, polynucleotides, vectors and cells of the invention may be provided to an individual either singly or in combination. Each molecule or cell of the invention may be provided to an individual in an isolated, substantially isolated, purified or substantially purified form. For example, a peptide of the invention may be provided to an individual substantially free from the other peptides.

[0071] Whilst it may be possible for the peptides, polynucleotides or compositions according to the invention to be presented in raw form, it is preferable to present them as a pharmaceutical formulation. Thus, according to a further aspect of the invention, the present invention provides a pharmaceutical formulation for tolerising an individual to a protein from which a peptide of the invention derives, comprising a composition, vector or product according to the invention together with one or more pharmaceutically acceptable carriers or diluents and optionally one or more other therapeutic ingredients. The carrier (s) must be `acceptable` in the sense of being compatible with the other ingredients of the formulation and not deleterious to the recipient thereof. Typically, carriers for injection, and the final formulation, are sterile and pyrogen free. The high solubility of the peptide of the invention results in there being little or no requirement for the organic solvents usual in pharmaceutical compositions. Accordingly, the present invention provides a pharmaceutical formulation as defined above comprising less than 5% organic solvent. Subject to this limitation, formulation of a composition comprising the peptide, polynucleotide or cell of the invention can be carried out using standard pharmaceutical formulation chemistries and methodologies all of which are readily available to the reasonably skilled artisan.

[0072] For example, compositions containing one or more molecules or cells of the invention can be combined with one or more pharmaceutically acceptable excipients or vehicles. Auxiliary substances, such as wetting or emulsifying agents, pH buffering substances and the like, may be present in the excipient or vehicle. These excipients, vehicles and auxiliary substances are generally pharmaceutical agents that do not induce an immune response in the individual receiving the composition, and which may be administered without undue toxicity. Pharmaceutically acceptable excipients include, but are not limited to, liquids such as water, saline, polyethyleneglycol, hyaluronic acid, glycerol, and ethanol. Pharmaceutically acceptable salts can also be included therein, for example, mineral acid salts such as hydrochlorides, hydrobromides, phosphates, sulfates, and the like; and the salts of organic acids such as acetates, propionates, malonates, benzoates, and the like. A thorough discussion of pharmaceutically acceptable excipients, vehicles and auxiliary substances is available in Remington's Pharmaceutical Sciences (Mack Pub. Co., N.J. 1991).

[0073] Such compositions may be prepared, packaged, or sold in a form suitable for bolus administration or for continuous administration. Injectable compositions may be prepared, packaged, or sold in unit dosage form, such as in ampoules or in multi-dose containers containing a preservative. Compositions include, but are not limited to, suspensions, solutions, emulsions in oily or aqueous vehicles, pastes, and implantable sustained-release or biodegradable formulations. Such compositions may further comprise one or more additional ingredients including, but not limited to, suspending, stabilizing, or dispersing agents. In one embodiment of a composition for parenteral administration, the active ingredient is provided in dry (for e.g., a powder or granules) form for reconstitution with a suitable vehicle (e. g., sterile pyrogen-free water) prior to parenteral administration of the reconstituted composition. The pharmaceutical compositions may be prepared, packaged, or sold in the form of a sterile injectable aqueous or oily suspension or solution. This suspension or solution may be formulated according to the known art, and may comprise, in addition to the active ingredient, additional ingredients such as the dispersing agents, wetting agents, or suspending agents described herein. Such sterile injectable formulations may be prepared using a non-toxic parenterally-acceptable diluent or solvent, such as water or 1,3-butane diol, for example. Other acceptable diluents and solvents include, but are not limited to, Ringer's solution, isotonic sodium chloride solution, and fixed oils such as synthetic mono-or di-glycerides. Other parentally-administrable compositions which are useful include those which comprise the active ingredient in microcrystalline form, in a liposomal preparation, or as a component of a biodegradable polymer systems. Compositions for sustained release or implantation may comprise pharmaceutically acceptable polymeric or hydrophobic materials such as an emulsion, an ion exchange resin, a sparingly soluble polymer, or a sparingly soluble salt.

[0074] Alternatively, the peptides or polynucleotides of the present invention may be encapsulated, adsorbed to, or associated with, particulate carriers. Suitable particulate carriers include those derived from polymethyl methacrylate polymers, as well as PLG microparticles derived from poly(lactides) and poly(lactide-co-glycolides). See, e.g., Jeffery et al. (1993) Pharm. Res. 10:362-368. Other particulate systems and polymers can also be used, for example, polymers such as polylysine, polyarginine, polyornithine, spermine, spermidine, as well as conjugates of these molecules.

[0075] The formulation of any of the peptides, polynucleotides or cells mentioned herein will depend upon factors such as the nature of the substance and the method of delivery. Any such substance may be administered in a variety of dosage forms. It may be administered orally (e.g. as tablets, troches, lozenges, aqueous or oily suspensions, dispersible powders or granules), parenterally, subcutaneously, by inhalation, intravenously, intramuscularly, intrasternally, transdermally, intradermally, epicutaneously, sublingually, intranasally, buccally or by infusion techniques. The substance may also be administered as suppositories. A physician will be able to determine the required route of administration for each particular individual.

[0076] The compositions of formulations of the invention will comprise a suitable concentration of each peptide/polynucleotide/cell to be effective without causing adverse reaction. Typically, the concentration of each peptide in the composition will be in the range of 0.03 to 200 nmol/ml. More preferably in the range of 0.3 to 200 nmol/ml, 3 to 180 nmol/ml, 10 to 150 nmol/ml or 30 to 120 nmol/ml. Such concentrations are particularly favoured for intradermal administration since an effective dose may be administered in a volume of 60 .mu.l, preferably 50 .mu.l, and most preferably 30 .mu.l. The composition or formulations should have a purity of greater than 95% or 98% or a purity of at least 99%.

[0077] A composition may therefore be formulated which comprises a molecule and/or cell of the invention and also one or more other therapeutic molecules. A composition of the invention may alternatively be used simultaneously, sequentially or separately with one or more other therapeutic compositions as part of a combined treatment.

Therapeutic Methods and Individual to be Treated

[0078] The present invention relates to peptides, polynucleotides, vectors and cells that are capable of desensitising or tolerising human individuals to proteins from which the peptides of the invention derive. Such proteins are typically allergens or other antigens to which an immune response is undesirable. Examples of such antigens include antigens associated with autoimmune diseases, antigens associated with graft-versus-host disease or transplant rejection (herein referred to as alloimmune conditions) and antigens associated with maternal-foetal immune responses, for example Rhesus D Haemolytic Disease of the Newborn. The peptides of the invention are therefore useful in the prevention or treatment an allergic disease, an autoimmune disease, an alloimmune condition or a maternal-foetal immune response. The invention provides compositions, products, vectors and formulations for use in preventing or treating the above conditions. The invention also provides a method of in preventing or treating a subject having the above conditions, comprising administering, either singly or in combination the polypeptides/polynucleotides/cells of the invention as described above.

[0079] The individual to be treated or provided with the composition or formulation of the invention is preferably human. It will be appreciated that the individual to be treated may be known to be sensitised to the particular allergen or antigen, at risk of being sensitised or suspected of being sensitised. The individual can be tested for sensitisation using techniques well known in the art and as described herein. Alternatively, the individual may have a family history of the conditions described above. It may not be necessary to test an individual for sensitisation to allergens because the individual may display symptoms of allergy when brought into proximity to a suitable allergen source. By proximity is meant 10 metres or less, 5 metres or less, 2 metres or less, 1 metre or less, or 0 metres from the source. Symptoms of allergy can include itchy eyes, runny nose, breathing difficulties, red itchy skin or rash. The individual to be treated may be of any age. However, preferably, the individual may be in the age group of 1 to 90, 5 to 60, 10 to 40, or more preferably 18 to 35. Preferably, the individual to be treated is from a population that has MHC allele frequencies within the range of frequencies that are representative of the Caucasian population. Reference population allele frequencies for 11 common DRB 1 allele families are shown in Table 1(Data from HLA Facts Book, Parham and Barber).

TABLE-US-00002 TABLE 1 DRB1 1 3 4 7 8 11 12 13 14 15 16 % 6.4 14.7 15.7 8.8 3.4 8.3 3.9 14.7 2.9 17.6 2.5 Reference 9.4 11.1 12.8 13.2 3.7 13.4 2.3 10.2 3.2 10.7 3.6 population %

Reference frequencies were obtained by analysis of multiple studies reporting frequencies and the figures shown are mean values. Preferably therefore, the individual to be treated is from a population that has equivalent MHC allele frequencies as the reference population for the alleles referred to Table 1 (such as for at least 1, 2, 3, 4, 5 or all of the alleles), for example within the ranges of those figures plus or minus 1, 2, 3, 5, 10, 15 or 20%.

[0080] Preferably the individual is from a population where the allele frequencies of the following DRB 1 alleles is:

[0081] 4--at least 9%

[0082] 7--at least 10%

[0083] 11--at least 8%.

[0084] The individual to be treated for allergic disease may have had allergy for at least 2 weeks, 1 month, 6 months, 1 year or 5 years. The individual may suffer from a rash, nasal congestion, nasal discharge and/or coughing caused by the allergy. The individual may or may not have been administered with other compositions/compounds which treat allergy.

Allergens and Antigens

[0085] Suitable allergens from which the region containing a MHC Class II-binding T cell epitope may derive can of course be obtained and/or produced using known methods. Classes of suitable allergens include, but are not limited to, pollens, animal dander (in particular cat dander), grasses, molds, dusts, antibiotics, stinging insect venoms, and a variety of environmental (including chemicals and metals), drug and food allergens. Common tree allergens include pollens from cottonwood, popular, ash, birch, maple, oak, elm, hickory, and pecan trees; common plant allergens include those from mugwort, ragweed, English plantain, sorrel-dock and pigweed; plant contact allergens include those from poison oak, poison ivy and nettles; common grass allergens include rye grass, Timothy, Johnson, Bermuda, fescue and bluegrass allergens; common allergens can also be obtained from molds or fungi such as Alternaria, Fusarium, Hormodendrum, Aspergillus, Micropolyspora, Mucor and thermophilic actinomycetes; epidermal allergens can be obtained from house or organic dusts (typically fungal in origin), from arthropods such as house mites (Dermatophagoides pteronyssinus), or from animal sources such as feathers, and dog dander; common food allergens include milk and cheese (diary), egg, wheat, nut (e.g., peanut), seafood (e.g., shellfish), pea, bean and gluten allergens; common environmental allergens include metals (nickel and gold), chemicals (formaldehyde, trinitrophenol and turpentine), Latex, rubber, fiber (cotton or wool), burlap, hair dye, cosmetic, detergent and perfume allergens; common drug allergens include local anesthetic and salicylate allergens; antibiotic allergens include penicillin, tetracycline and sulfonamide allergens; and common insect allergens include bee, wasp and ant venom, and cockroach calyx allergens. Particularly well characterized allergens include, but are not limited to, the major allergen produced by the domestic cat Felis catus (Felis domesticus) glycoprotein Fel d1, the major and cryptic epitopes of the Der p I allergen (Hoyne et al. (1994) Immunology83190-195), bee venom phospholipase A2 (PLA) (Akdis et al. (1996) J. Clin. Invest. 98:1676-1683), birch pollen allergen Bet v 1 (Bauer et al. (1997) Clin. Exp. Immunol. 107:536-541), and the multi-epitopic recombinant grass allergen rKBG8.3 (Cao et al. (1997) Immunology90:46-51). These and other suitable allergens are commercially available and/or can be readily prepared as extracts following known techniques.

[0086] Preferably, the allergen is selected from the list of allergen sequences and database accession numbers (NCBI Entrez accession numbers) below. NCBI is the National Center for Biotechnology information and is a division of the US National Institutes of Health. Allergen sequences and database accession numbers (NCBI Entrez accession numbers):

House Dust Mite

Dermatophagoides Pteronyssinus

TABLE-US-00003

[0087] DerP 1 (SEQ ID NO: 316) MKIVLAIASLLALSAVYARPSSIKTFEEYKKAFNKSYATFEDEEAARKNFLES VKYVQSNGGAINHLSDLSLDEFKNRFLMSAEAFEHLKTQFDLNAETNACSIN GNAPAEIDLRQMRTVTPIRMQGGCGSCWAFSGVAATESAYLAYRNQSLDLA EQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESYYRYVAREQSCRRPNAQ RFGISNYCQIYPPNVNKIREALAQTHSAIAVIIGIKDLDAFRHYDGRTIIQRDN GYQPNYHAVNIVGYSNAQGVDYWIVRNSWDTNWGDNGYGYFAANIDLM MIEEYPYVVIL DerP 2 (SEQ ID NO: 317) MMYKILCLSLLVAAVARDQVDVKDCANHEIKKVLVPGCHGSEPCIIHRGKPF QLEAVFEANQNTKTAKIEIKASIDGLEVDVPGIDPNACHYMKCPLVKGQQYD IKYTWNVPKIAPKSENVVVTVKVMGDDGVLACAIATHAKIRD DerP 3 (SEQ ID NO: 318) MIIYNILIVLLLAINTLANPILPASPNATIVGGEKALAGECPYQISLQSSSHFCG GTILDEYWILTAAHCVAGQTASKLSIRYNSLKHSLGGEKISVAKIFAHEKYDS YQ1DNDIALIKLKSPMKLNQKNAKAVGLPAKGSDVKVGDQVRVSGWGYLE EGSYSLPSELRRVDIAVVSRKECNELYSKANAEVTDNMICGGDVANGGKDS CQGDSGGPVVDVKNNQVVGIVSWGYGCARKGYPGVYTRVGNFIDWIESKR SQ DerP 4 (SEQ ID NO: 319) KYXNPHFIGXRSVITXLME DerP 5 (SEQ ID NO: 320) MKFIIAFFVATLAVMTVSGEDKKHDYQNEFDFLLMERIHEQIKKGELALFYL QEQINHFEEKPTKEMKDKIVAEMDTIIAMIDGVRGVLDRLMQRKDLDIFEQY NLEMAKKSGDILERDLKKEEARVKKIEV DerP 6 (SEQ ID NO: 321) AIGXQPAAEAEAPFQISLMK DerP7 (SEQ ID NO: 322) MMKLLLIAAAAFVAVSADPIHYDKITEEINKAVDEAVAAIEKSETFDPMKVP DHSDKFERHIGIIDLKGELDMRNIQVRGLKQMKRVGDANVKSEDGVVKAHL LVGVHDDVVSMEYDLAYKLGDLHPNTHVISDIQDFVVELSLEVSEEGNMTL TSFEVRQFANVVNHIGGLSILDPIFAVLSDVLTAIFQDTVRAEMTKVLAPAFK KELERNNQ DerP9 (SEQ ID NO: 323) IVGGSNASPGDAVYQIAL

Dermatophagoides Farinae

TABLE-US-00004

[0088] Der f 1 (SEQ ID NO: 324) MKFVLAIASLLVLTVYARPASIKTFEFKKAFNKNYATVEEEEVARKN FLESLKYVEANKGAINHLSDLSLDEFKNRYLMSAEAFEQLKTQFDLN AETSACRINSVNVPSELDLRSLRTVTPIRMQGGCGSCWAFSGVAATE SAYLAYRNTSLDLSEQELVDCASQHGCHGDTIPRGIEYIQQNGVVEE RSYPYVAREQRCRRPNSQHYGISNYCQIYPPDVKQIREALTQTHTAI AVIIGIKDLRAFQHYDGRTIIQHDNGYQPNYHAVNIVGYGSTQGDDY WIVRNSWDTTWGDSGYGYFQAGNNLMMIEQYPYVVIM Der f 2 (SEQ ID NO: 325) MISKILCLSLLVAAVVADQVDVKDCANNEIKKVMVDGCHGSDPCIIH RGKPFTLEALFDANQNTKTAKIEIKASLDGLEIDVPGIDTNACHFMK CPLVKGQQYDIKYTWNVPKIAPKSENVVVTVKLIGDNGVLACAIATH GKIRD Der f 3 (SEQ ID NO: 326) MMILTIVVLLAANILATPILPSSPNATIVGGVKAQAGDCPYQISLQS SSHFCGGSILDEYWILTAAHCVNGQSAKKLSIRYNTLKHASGGEKIQ VAEIYQHENYDSMTIDNDVALIKLKTPMTLDQTNAKPVPLPAQGSDV KVGDKIRVSGWGYLQEGSYSLPSELQRVDIDVVSREQCDQLYSKAGA DVSENMICGGDVANGGVDSCQGDSGGPVVDVATKQIVGIVSWGYGCA RKGYPGVYTRVGNFVDWIESKRSQ Der f 4 (SEQ ID NO: 327) AVGGQDADLAEAPFQISLLK Der f 7 (SEQ ID NO: 328) MMKFLLIAAVAFVAVSADPIHYDKITEEINKAIDDAIAAIEQSETID PMKVPDHADKFERHVGIVDFKGELAMRNIEARGLKQMKRQGDANVKG EEGIVKAHLLIGVHDDIVSMEYDLAYKLGDLHPTTHVISDIQDFVVA LSLEISDEGNITMTSFEVRQFANVVNHIGGLSILDPIFGVLSDVLTA IFQDTVRKEMTKVLAPAFKRELEKN

Additional Mite Allergen Sequences (NCBI Entrez Accession):

[0089] 1170095; 1359436; 2440053; 666007; 487661; 1545803; 84702; 84699; 625532; 404370; 1091577; 1460058; 7413; 9072; 387592.

Cat

Felis Sequences (NCBI Entrez Accession):

[0090] 539716; 539715; 423193; 423192; 423191; 423190; 1364213; 1364212; 395407; 163827; 163823; 163825; 1169665; 232086; 1169666.

Latex

Hevea Sequences:

TABLE-US-00005

[0091] Hev b 1 (SEQ ID NO: 329) MAEDEDNQQGQGEGLKYLGFVQDAATYAVTTFSNVYLFAKDKSGPLQPGV DIIEGPVKNVAVPLYNRFSYIPNGALKFVDSTVVASVTIIDRSLPPIVKD ASIQVVSAIRAAPEAARSLASSLPGQTKILAKVFYGEN Hev b 3 (SEQ ID NO: 330) MAEEVEEERLKYLDFVRAAGVYAVDSFSTLYLYAKDISGPLKPGVDTIEN VVKTVVTPVYYIPLEAVKFVDKTVDVSVTSLDGVVPPVIKQVSAQTYSVA QDAPRIVLDVASSVFNTGVQEGAKALYANLEPKAEQYAVITWRALNKLPL VPQVANVVVPTAVYFSEKYNDVVRGTTEQGYRVSSYLPLLPTEKITKVFG DEAS

Additional Hevea Sequences (NCBI Entrez Accession):

[0092] 3319923; 3319921; 3087805; 1493836; 1480457; 1223884; 3452147; 3451147; 1916805; 232267; 123335; 2501578; 3319662; 3288200; 1942537; 2392631; 2392630; 1421554; 1311006; 494093; 3183706; 3172534; 283243; 1170248; 1708278; 1706547; 464775; 266892; 231586; 123337; 116359; 123062; 2213877; 542013; 2144920; 1070656; 2129914; 2129913; 2129912; 100135; 82026; 1076559; 82028; 82027; 282933; 280399; 100138; 1086972; 108697; 1086976; 1086978; 1086978; 1086976; 1086974; 1086972; 913758; 913757; 913756; 234388; 1092500; 228691; 1177405; 18839; 18837; 18835; 18833; 18831; 1209317; 1184668; 168217; 168215; 168213; 168211; 168209; 348137.

Rye Grass

Lolium Sequences:

TABLE-US-00006

[0093] 126385 Lol p 1 (SEQ ID NO: 331) MASSSSVLLVVALFAVFLGSAHGIAKVPPGPNITAEYGDKWLDAKSTWYGK PTGAGPKDNGGACGYKNVDKAPFNGMTGCGNTPIFKDGRGCGSCFEIKCTK PESCSGEAVTVTITDDNEEPIAPYHFDLSGHAFGSMAKKGEEQNVRSAGELE LQFRRVKCKYPDDTKPTFHVEKASNPNYLAILVKYVDGDGDVVAVDIKEKG KDKWIELKESWGAVWRIDTPDKLTGPFTVRYTTEGGTKSEFEDVIPEGWKA DTSYSAK 126386 Lol p 2a (SEQ ID NO: 332) AAPVEFTVEKGSDEKNLALSIKYNKEGDSMAEVELKEHGSNEWLALKKNG DGVWEIKSDKPLKGPFNFRFVSEKGMRNVFDDVVPADFKVGTTYKPE 126387 Lol p 3 (SEQ ID NO: 333) TKVDLTVEKGSDAKTLVLNIKYTRPGDTLAEVELRQHGSEEWEPMTKKGNL WEVKSAKPLTGPMNFRFLSKGGMKNVFDEVIPTAFTVGKTYTPEYN 2498581 Lol p 5a (SEQ ID NO: 334) MAVQKYTVALFLRRGPRGGPGRSYAADAGYTPAAAATPATPAATPAGGWR EGDDRRAEAAGGRQRLASRQPWPPLPTPLRRTSSRSSRPPSPSPPRASSPTSA AKAPGLIPKLDTAYDVAYKAAEAHPRGQVRRLRHCPHRSLRVIAGALEVHA VKPATEEVLAAKIPTGELQIVDKIDAAFKIAATAANAAPTNDKFTVFESAFNK ALNECTGGAMRPTSSSPPSRPRSSRPTPPPSPAAPEVKYAVFEAALTKAITAM TQAQKAGKPAAAAATAAATVATAAATAAAVLPPPLLVVQSLISLLIYY 2498582 Lol p 5b (SEQ ID NO: 335) MAVQKHTVALFLAVALVAGPAASYAADAGYAPATPATPAAPATAATPATP ATPATPAAVPSGKATTEEQKLIEKINAGFKAAVAAAAVVPPADKYKTFVETF GTATNKAFVEGLASGYADQSKNQLTSKLDAALKLAYEAAQGATPEAKYDA YVATLTEALRVIAGTLEVHAVKPAAEEVKVGAIPAAEVQLIDKVDAAYRTA ATAANAAPANDKFTVFENTFNNAIKVSLGAAYDSYKFIPTLVAAVKQAYAA KQATAPEVKYTVSETALKKAVTAMSEAEKEATPAAAATATPTPAAATATAT PAAAYATATPAAATATATPAAATATPAAAGGYKV 455288 Lol p isoform 9 (SEQ ID NO: 336) MAVQKHTVALFLAVALVAGPAASYAADAGYAPATPATPAAPATAATPATP ATPATPAAVPSGKATTEEQKLIEKINAGFKAAVAAAAVVPPADKYKTFVETF GTATNKAFVEGLASGYADQSKNQLTSKLDAALKLAYEAAQGATPEAKYDA YVATLTEALRVIAGTLEVHAVKPAAEEVKVGAIPAAEVQLIDKVDAAYRTA ATAANAAPANDKFTVFENTFNNAIKVSLGAAYDSYKFIPTLVAAVKQAYAA KQATAPEVKYTVSETALKKAVTAMSEAEKEATPAAAATATPTPAAATATAT PAAAYATATPAAATATATPAAATATPAAAGGYKV 1582249 Lol p 11 (SEQ ID NO: 337) DKGPGFVVTGRVYCDPCRAGFETNVSHNVEGATVAVDCRPFDGGESKLKA EATTDKDGWYKIEIDQDHQEEICEVVLAKSPDKSCSEIEEFRDRARVPLTSNX GIKQQGIRYANPIAFFRKEPLKECGGILQAY

Additional Lolium Sequences (NCBI Entrez Accession):

[0094] 135480; 417103; 687261; 687259; 1771355; 2388662; 631955; 542131; 542130; 542129; 100636; 626029; 542132; 320616; 320615; 320614; 100638; 100634; 82450; 626028; 100639; 283345; 542133; 1771353; 1763163; 1040877; 1040875; 250525; 551047; 515377; 510911; 939932; 439950; 2718; 168316; 168314; 485371; 2388664; 2832717; 2828273; 548867.

Olive Tree

Olive Sequences

TABLE-US-00007

[0095] 416610 Ole e 1 (SEQ ID NO: 338) EDIPQPPVSQFHIQGQVYCDTCRAGFITELSEFIPGASLRLQCKDKE NGDVTFTEVGYTRAEGLYSMLVERDHKNEFCEITLISSGRKDCNEIP TEGWAKPSLKFKLNTVNGTTRTVNPLGFFKKEALPKCAQVYNKLGMY PPNM

Parietaria

Parietaria Sequences:

TABLE-US-00008

[0096] 2497750 Par j P2 (SEQ ID NO: 339) MRTVSMAALVVIAAALAWTSSAEPAPAPAPGEEACGKVVQDIMPCLHFVKG EEKEPSKECCSGTKKLSEEVKTTEQKREACKCIVRATKGISGIKNELVAEVPK KCDIKTTLPPITADFDCSKIQSTIFRGYY 1352506 Par j P5 (SEQ ID NO: 340) MVRALMPCLPFVQGKEKEPSKGCCSGAKRLDGETKTGPQRVHACECIQTAM KTYSDIDGKLVSEVPKHCGIVDSKLPPIDVNMDCKTVGVVPRQPQLPVSLRH GPVTGPSDPAHKARLERPQIRVPPPAPEKA 1532056 Par j P8 (SEQ ID NO: 341) MRTVSMAALVVIAAALAWTSSAELASAPAPGEGPCGKVVHHIMPCLKFVKG EEKEPSKSCCSGTKKLSEEVKTTEQKREACKCIVAATKGISGIKNELVAEVPK KCGITTTLPPITADFDCSKIESTIFRGYY 1532058 Par j P9 (SEQ ID NO: 342) MRTVSAPSAVALVVIVAAGLAWTSLASVAPPAPAPGSEETCGTVVRALMPC LPFVQGKEKEPSKGCCSGAKRLDGETKTGLQRVHACECIQTAMKTYSDIDG KLVSEVPKHCGIVDSKLPPIDVNMDCKTLGVVPRQPQLPVSLRHGPVTGPSD PAHKARLERPQIRVPPPAPEKA 2497749 Par j P9 (SEQ ID NO: 343) MRTVSARSSVALVVIVAAVLVWTSSASVAPAPAPGSEETCGTVVGALMPCL PFVQGKEKEPSKGCCSGAKRLDGETKTGPQRVHACECIQTAMKTYSDIDGK LVSEVPKHCGIVDSKLPPIDVNMDCKTLGVLHYKGN 1086003 Par j 1 (SEQ ID NO: 344) MVRALMPCLPFVQGKEKEPSKGCCSGAKRLDGETKTGPQRVHACECIQTAM KTYSDIDGKLVSEVPKHCGIVDSKLPPIDVNMDCKTVGVVPRQPQLPVSLRH GPVTGPSRSRPPTKHGWRDPRLEFRPPHRKKPNPAFSTLG

Additional Parietaria Sequences (NCBI Entrez Accession):

[0097] 543659; 1836011; 1836010; 1311513; 1311512; 1311511; 1311510; 1311509; 240971.

Timothy Grass

Phleum Sequences:

TABLE-US-00009

[0098] Phl p 1 (SEQ ID NO: 345) MASSSSVLLVVVLFAVFLGSAYGIPKVPPGPNITATYGDKWLDAKSTWYGK PTGAGPKDNGGACGYKDVDKPPFSGMTGCGNTPIFKSGRGCGSCFEIKCTKP EACSGEPVVVHITDDNEEPIAPYHFDLSGHAFGAMAKKGDEQKLRSAGELEL QFRRVKCKYPEGTKVTFHVEKGSNPNYLALLVKYVNGDGDVVAVDIKEKG KDKWIELKESWGAIWRIDTPDKLTGPFTVRYTTEGGTKTEAEDVIPEGWKA DTSYESK Phl p 1 (SEQ ID NO: 346) MASSSSVLLVVALFAVFLGSAHGIPKVPPGPNITATYGDKWLDAKSTWYGK PTAAGPKDNGGACGYKDVDKPPFSGMTGCGNTPIFKSGRGCGSCFEIKCTKP EACSGEPVVVHITDDNEEPIAAYHFDLSGIAFGSMAKKGDEQKLRSAGEVEI QFRRVKCKYPEGTKVTFHVEKGSNPNYLALLVKFSGDGDVVAVDIKEKGKD KWIALKESWGAIWRIDTPEVLKGPFTVRYTTEGGTKARAKDVIPEGWKADT AYESK Phlp 2 (SEQ ID NO: 347) MSMASSSSSSLLAMAVLAALFAGAWCVPKVTFTVEKGSNEKHLAVLVKYE GDTMAEVELREHGSDEWVAMTKGEGGVWTFDSEEPLQGPFNFRFLTEKGM KNVFDDVVPEKYTIGATYAPEE Phl p 5 (SEQ ID NO: 348) ADLGYGGPATPAAPAEAAPAGKATTEEQKLIEKINDGFKAALAAAAGVPPA DKYKTFVATFGAASNKAFAEGLSAEPKGAAESSSKAALTSKLDAAYKLAYK TAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIE KVDSAFKVAATAANAAPANDKFTVFEAAFNNAIKASTGGAYESYKFIPALE AAVKQAYAATVATAPEVKYTVFETALKKAFTAMSEAQKAAKPATEATATA TAAVGAATGAATAATGGYKV Phl p 5 (SEQ ID NO: 349) ADLGYGGPATPAAPAEAAPAGKATTEEQKLIEKINDGFKAALAAAAGVPPA DKYKTFVATFGAASNKAFAEGLSAEPKGAAESSSKAALTSKLDAAYKLAYK TAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIE KVDSAFKVAATAANAAPANDKFTVFEAAFNNAIKASTGGAYESYKFIPALE AAVKQAYAATVATAPEVKYTVFETALKKAITAMSEAQKAAKPATEATATA TAAVGAATGAATAATGGYKV Phl p 5b (SEQ ID NO: 350) AAAAVPRRGPRGGPGRSYTADAGYAPATPAAAGAAAGKATTEEQKLIEDIN VGFKAAVAAAASVPAADKFKTFEAAFTSSSKAAAAKAPGLVPKLDAAYSV AYKAAVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEEPGMAKIPA GELQIIDKIDAAFKVAATAAATAPADDKFTVFEAAFNKAIKESTGGAYDTYK CIPSLEAAVKQAYAATVAAAPQVKYAVFEAALTKAITAMSEVQKVSQPATG AATVAAGAATTAAGAASGAATVAAGGYKV Phl p 5a (SEQ ID NO: 351) ADLGYGPATPAAPAAGYTPATPAAPAGADAAGKATTEEQKLIEKINAGFKA ALAGAGVQPADKYRTFVATFGPASNKAFAEGLSGEPKGAAESSSKAALTSK LDAAYKLAYKTAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEV KV1PAGELQVIEKVDAAFKVAATAANAAPANDKFTVFEAAFNDEIKASTGG AYESYKFIPALEAAVKQAYAATVATAPEVKYTVFETALKKAITAMSEAQKA AKPAAAATATATAAVGAATGAATAATGGYKV Phl p 5 (SEQ ID NO: 352) MAVQKYTVALFLAVALVAGPAASYAADAGYAPATPAAAGAEAGKATTEE QKLIEDINVGFKAAVAAAASVPAADKFKTFEAAFTSSSKAATAKAPGLVPKL DAAYSVSYKAAVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEEPG MAK1PAGELQIIDKIDAAFKVAATAAATAPADTVFEAAFNKAIKE STGGAYD TYKCIPSLEAAVKQAYAATVAAAPQVKYAVFEAALTKAITAMSEVQKVSQP ATGAATVAAGAATTAAGAASGAATVAAGGYKV Phl p 5 (SEQ ID NO: 353) MAVQKYTVALFLAVALVAGPAASYAADAGYAPATPAAAGAEAGKATTEE QKLIEDINVGFKAAVAAAASVPAADKFKTFEAAFTSSSKAATAKAPGLVPKL DAAYSVAYKAAVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEDPA WPKIPAGELQIIDKIDAAFKVAATAAATAPADDKFTVFEAAFNKAIKE STGG AYDTYKCIPSLEAAVKQAYAATVAAAPQVKYAVFEAALTKAITAMSEVQK VSQPATGAATVAAGAATTATGAASGAATVAAGGYKV Phl p 5 (SEQ ID NO: 354) ADAGYAPATPAAAGAEAGKATTEEQKLIEDINVGFKAAVAAAASVPAADKF KTFEAAFTSSSKAATAKAPGLVPKLDAAYSVAYKAAVGATPEAKFDSFVAS LTEALRVIAGALEVHAVKPVTEEPGMAKIPAGELQIIDKIDAAFKVAATAAA TAPADDKFTVFEAAFNKAIKESTGGAYDTYKCIPSLEAAVKQAYAATVAAA PQVKYAVFEAALTKAITAMSEVQKVSQPATGAATVAAGAATTAAGAASGA ATVAAGGYKV Phl p 5 (SEQ ID NO: 355) SVKRSNGSAEVHRGAVPRRGPRGGPGRSYAADAGYAPATPAAAGAEAGKA TTEEQKLIEDINVGFKAAVAAAASVPAADKFKTFEAAFTSSSKAATAKAPGL VPKLDAAYSVAYKAAVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVT EEPGMAK1PAGELQIIDKIDAAFKVAATAAATAPADDKFTVFEAAFNKAIKES TGGAYDTYKCIPSLEAAVKQAYAATVAAAPQVKYAVFEAALTKAITAMSEV QKVSQPATGAATVAAGAATTAAGAASGAATVAAGGYKV Phl p 5 (SEQ ID NO: 356) MAVHQYTVALFLAVALVAGPAGSYAADLGYGPATPAAPAAGYTPATPAAP AGAEPAGKATTEEQKLIEKINAGFKAALAAAAGVPPADKYRTFVATFGAAS NKAFAEGLSGEPKGAAESSSKAALTSKLDAAYKLAYKTAEGATPEAKYDAY VATVSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIEKVDAAFKVAATAA NAAPANDKFTVFEAAFNDAIKASTGGAYESYKFIPALEAAVKQAYAATVAT APEVKYTVFETALKKAITAMSEAQKAAKPAAAATATATAAVGAATGAATA ATGGYKV Phl p 5 (SEQ ID NO: 357) ADLGYGGPATPAAPAEAAPAGKATTEEQKLIEKINDGFKAALAAAAGVPPA DKYKTFVATFGAASNKAFAEGLSAEPKGAAESSSKAALTSKLDAAYKLAYK TAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIE KVDSAFKVAATAANAAPANDKFTVFEAAFNNAIKASTGGAYESYKFIPALE AAVKQAYAATVATAPEVKYTVFETALKKAFTAMSEAQKAAKPATEATATA TAAVGAATGAATAATGGYKV Phl p5b (SEQ ID NO: 358) AAAAVPRRGPRGGPGRSYTADAGYAPATPAAAGAAAGKATTEEQKLIEDIN VGFKAAVAAAASVPAADKFKTFEAAFTSSSKAAAAKAPGLVPKLDAAYSV AYKAAVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEEPGMAKIPA GELQIIDKIDAAFKVAATAAATAPADDKFTVFEAAFNKAIKESTGGAYDTYK CIPSLEAAVKQAYAATVAAAPQVKYAVFEAALTKAITAMSEVQKVSQPATG AATVAAGAATTAAGAASGAATVAAGGYKV Phl p5a (SEQ ID NO: 359) ADLGYGPATPAAPAAGYTPATPAAPAGADAAGKATTEEQKLIEKINAGFKA ALAGAGVQPADKYRTFVATFGPASNKAFAEGLSGEPKGAAESSSKAALTSK LDAAYKLAYKTAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEV KV1PAGELQVIEKVDAAFKVAATAANAAPANDKFTVFEAAFNDEIKASTGG AYESYKFIPALEAAVKQAYAATVATAPEVKYTVFETALKKAITAMSEAQKA AKPAAAATATATAAVGAATGAATAATGGYKV Phl p 5 (SEQ ID NO: 360) AVPRRGPRGGPGRSYAADAGYAPATPAAAGAEAGKATTEEQKLIEDINVGF KAAVAAAASVPAGDKFKTFEAAFTSSSKAATAKAPGLVPKLDAAYSVAYK AAVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEEPGMAK1PAGELQ IIDKIDAAFKVAATAAATAPADDKFTVFEAAFNKAIKESTGGAYDTYKCIPSL EAAVKQAYAATVAAAPQVKYAVFEAALTKAITAMSEVQKVSQPATGAATV AAGAATTATGAASGAATVAAGGYKV Phl p 5b (SEQ ID NO: 361) MAVPRRGPRGGPGRSYTADAGYAPATPAAAGAAAGKATTEEQKLIEDINVG FKAAVAARQRPAADKFKTFEAASPRHPRPLRQGAGLVPKLDAAYSVAYKA AVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEEPGMAKIPAGELQII DK1DAAFKVAATAAATAPADDKFTVFEAAFNKAIKESTGGAYDTYKCIPSLE AAVKQAYAATVAAAAEVKYAVFEAALTKAITAMSEVQKVSQPATGAATVA AGAATTAAGAASGAATVAAGGYKV Phl p 5 (SEQ ID NO: 362) MAVHQYTVALFLAVALVAGPAASYAADLGYGPATPAAPAAGYTPATPAAP AEAAPAGKATTEEQKLIEKINAGFKAALAAAAGVQPADKYRTFVATFGAAS NKAFAEGLSGEPKGAAESSSKAALTSKLDAAYKLAYKTAEGATPEAKYDAY VATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIEKVDAAFKVAATAA NAAPANDKFTVFEAAFNDAIKASTGGAYESYKFIPALEAAVKQAYAATVAT APEVKYTVFETALKKAITAMSEAQKAAKPAAAATATATAAVGAATGAATA ATGGYKV

Phlp 5 (SEQ ID NO: 363) EAPAGKATTEEQKLIEKINAGFKAALARRLQPADKYRTFVATFGPASNKAFA EGLSGEPKGAAESSSKAALTSKLDAAYKLAYKTAEGATPEAKYDAYVATLS EALRIIAGTLEVHAVKPAAEEVKVIPAAELQVIEKVDAAFKVAATAANAAPA NDKFTVFEAAFNDEIKASTGGAYESYKFIPALEAAVKQAYAATVATAPEVK YTVFETALKKAITAMSEAQKAAKPPPLPPPPQPPPLAATGAATAATGGYKV Phl p 5 (SEQ ID NO: 364) MAVHQYTVALFLAVALVAGPAASYAADLGYGPATPAAPAAGYTPATPAAP AEAAPAGKATTEEQKLIEKINAGFKAALAAAAGVQPADKYRTFVATFGAAS NKAFAEGLSGEPKGAAESSSKAALTSKLDAAYKLAYKTAEGATPEAKYDAY VATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIEKVDAAFKVAATAA NAAPANDKFTVFEAAFNDAIKASTGGAYESYKFIPALEAAVKQAYAATVAT APEVKYTVFETALKKAITAMSEAQKAAKPAAAATATATAAVGAATGAATA ATGGYKV Phl p 5b (SEQ ID NO: 365) MAVPRRGPRGGPGRSYTADAGYAPATPAAAGAAAGKATTEEQKLIEDINVG FKAAVAARQRPAADKFKTFEAASPRHPRPLRQGAGLVPKLDAAYSVAYKA AVGATPEAKFDSFVASLTEALRVIAGALEVHAVKPVTEEPGMAKIPAGELQII DKIDAAFKVAATAAATAPADDKFTVFEAAFNKAIKESTGGAYDTYKCIPSLE AAVKQAYAATVAAAAEVKYAVFEAALTKAITAMSEVQKVSQPATGAATVA AGAATTAAGAASGAATVAAGGYKV Phl p 5a (SEQ ID NO: 366) ADLGYGPATPAAPAAGYTPATPAAPAGADAAGKATTEEQKLIEKINAGFKA ALAGAGVQPADKYRTFVATFGPASNKAFAEGLSGEPKGAAESSSKAALTSK LDAAYKLAYKTAEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAAEEV KVIPAGELQVIEKVDAAFKVAATAANAAPANDKFTVFEAAFNDEIKASTGG AYESYKFIPALEAAVKQAYAATVATAPEVKYTVFETALKKAITAMSEAQKA AKPPPLPPPPQPPPLAATGAATAATGGYKV Phl p 5 (SEQ ID NO: 367) MAVHQYTVALFLAVALVAGPAASYAADLGYGPATPAAPAAGYTPATPAAP AEAAPAGKATTEEQKLIEKINAGFKAALAAAAGVQPADKYRTFVATFGAAS NKAFAEGLSGEPKGAAESSSKAALTSKLDAAYKLAYKTAEGATPEAKYDAY VATLSEALRIIAGTLEVHAVKPAAEEVKVIPAGELQVIEKVDAAFKVAATAA NAAPANDKFTVFEAAFNDAIKASTGGAYESYKFIPALEAAVKQAYAATVAT APEVKYTVFETALKKAITAMSEAQKAAKPAAAATATATAAVGAATGAATA ATGGYKV Phl p 6 (SEQ ID NO: 368) MAAHKFMVAMFLAVAVVLGLATSPTAEGGKATTEEQKLIEDVNASFRAAM ATTANVPPADKYKTFEAAFTVSSKRNLADAVSKAPQLVPKLDEVYNAAYN AADHAAPEDKYEAFVLHFSEALRIIAGTPEVHAVKPGA Phl p 6 (SEQ ID NO: 369) SKAPQLVPKLDEVYNAAYNAADHAAPEDKYEAFVLHFSEALHIIAGTPEVH AVKPGA Phl p 6 (SEQ ID NO: 370) ADKYKTFEAAFTVSSKRNLADAVSKAPQLVPKLDEVYNAAYNAADHAAPE DKYEAFVLHFSEALHIIAGTPEVHAVKPGA Phl p 6 (SEQ ID NO: 371) TEEQKLIEDVNASFRAAMATTANVPPADKYKTLEAAFTVSSKRNLADAVSK APQLVPKLDEVYNAAYNAADHAAPEDKYEAFVLHFSEALRIIAGTPEVHAV KPGA Phl p 6 (SEQ ID NO: 372) MAAHKFMVAMFLAVAVVLGLATSPTAEGGKATTEEQKLIEDINASFRAAM ATTANVPPADKYKTFEAAFTVSSKRNLADAVSKAPQLVPKLDEVYNAAYN AADHAAPEDKYEAFVLHFSEALHIIAGTPEVHAVKPGA Phl p 6 (SEQ ID NO: 373) MVAMFLAVAVVLGLATSPTAEGGKATTEEQKLIEDVNASFRAAMATTANV PPADKYKTFEAAFTVSSKRNLADAVSKAPQLVPKLDEVYNAAYNAADHAA PEDKYEAFVLHFSEALRIIAGTPEVHAVKPGA Phlp 7 (SEQ ID NO: 374) MADDMERIFKRFDTNGDGKISLSELTDALRTLGSTSADEVQRMMAEIDTDG DGFIDFNEFISFCNANPGLMKDVAKVF Phl p 11 (SEQ ID NO: 375) MSWQTYVDEHLMCEIEGHHLASAAILGHDGTVWAQSADFPQFKPEEITGIM KDFDEPGHLAPTGMFVAGAKYMVIQGEPGRVIRGKKGAGGITIKKTGQALV VGIYDEPMTPGQCNMVVERLGDYLVEQGM

Additional Phleum sequences (NCBI entrez accession): 458878; 548863; 2529314; 2529308; 2415702; 2415700; 2415698; 542168; 542167; 626037; 542169; 541814; 542171; 253337; 253336; 453976; 439960.

Wasp (and Related)

Vespula Sequences:

TABLE-US-00010

[0099] 465054 ALLERGEN VES V 5 (SEQ ID NO: 376) MEISGLVYLIIIVTIIDLPYGKANNYCKIKCLKGGVHTACKYGSLKPNCGNKV VVSYGLTKQEKQDILKEHNDFRQKIARGLETRGNPGPQPPAKNMKNLVWN DELAYVAQVWANQCQYGHDTCRDVAKYQVGQNVALTGSTAAKYDDPVK LVKMWEDEVKDYNPKKKFSGNDFLKTGHYTQMVWANTKEVGCGSIKYIQE KWHKHYLVCNYGPSGNFMNEELYQTK 1709545 ALLERGEN VES M 1 (SEQ ID NO: 377) GPKCPFNSDTVSIIIETRENRNRDLYTLQTLQNHPEFKKKTITRPVVFITHGFTS SASEKNFINLAKALVDKDNYMVISIDWQTAACTNEYPGLKYAYYPTAASNT RLVGQYIATITQKLVKDYKISMANIRLIGHSLGAHVSGFAGKRVQELKLGKY SEIIGLDPARPSFDSNHCSERLCETDAEYVQIIHTSNYLGTEKILGTVDFYMNN GKNNPGCGRFFSEVCSHTRAVIYMAECIKHECCLIGIPRSKSSQPISRCTKQEC VCVGLNAKKYPSRGSFYVPVESTAPFCNNKGKII 1352699 ALLERGEN VES V 1 (SEQ ID NO: 378) MEENMNLKYLLLFVYFVQVLNCCYGHGDPLSYELDRGPKCPFNSDTVSIIIE TRENRNRDLYTLQTLQNHPEFKKKTITRPVVFITHGFTSSASETNFINLAKAL VDKDNYMVISIDWQTAACTNEAAGLKYLYYPTAARNTRLVGQYIATITQKL VKHYKISMANIRLIGHSLGAHASGFAGKKVQELKLGKYSEIIGLDPARPSFDS NHCSERLCETDAEYVQIIHTSNYLGTEKTLGTVDFYMNNGKNQPGCGRFFSE VCSHSRAVIYMAECIKHECCLIGIPKSKSSQPISSCTKQECVCVGLNAKKYPSR GSFYVPVESTAPFCNNKGKII 1346323 ALLERGEN VES V 2 (SEQ ID NO: 379) SERPKRVFNIYWNVPTFMCHQYDLYFDEVTNFNIKRNSKDDFQGDKIAIFYD PGEFPALLSLKDGKYKKRNGGVPQEGNITIHLQKFIENLDKIYPNRNFSGIGVI DFERWRPIFRQNWGNMKIHKNFSIDLVRNEHPTWNKKMIELEASKRFEKYA RFFMEETLKLAKKTRKQADWGYYGYPYCFNMSPNNLVPECDVTAMHEND KMSWLFNNQNVLLPSVYVRQELTPDQRIGLVQGRVKEAVRISNNLKHSPKV LSYWWYVYQDETNTFLTETDVKKTFQEIVINGGDGIIIWGSSSDVNSLSKCK RLQDYLLTVLGPIAINVTEAVN 549194 ALLERGEN VES VI (SEQ ID NO: 380) 5KVNYCKIKCLKGGVHTACKYGTSTKPNCGKMVVKAYGLTEAEKQEILKV HNDFRQKVAKGLETRGNPGPQPPAKNMNNLVWNDELANIAQVWASQCNY GHDTCKDTEKYPVGQNIAKRSTTAALFDSPGKLVKMWENEVKDFNPNIEWS KNNLKKTGHYTQMVWAKTKEIGCGSVKYVKDEWYTHYLVCNYGPSGNFR NEKLYEKK

Additional Vespula Sequences (NCBI Entrez Accession):

[0100] 549193; 549192; 549191; 549190; 549189; 117414; 126761; 69576; 625255; 627189; 627188; 627187; 482382; 112561; 627186; 627185; 1923233; 897645; 897647; 745570; 225764; 162551.

Tree Allergen Sequences (Mainly Birch) Sequences:

TABLE-US-00011

[0101] 114922 Bet v 1 (SEQ ID NO: 381) MGVFNYETETTSVIPAARLFKAFILDGDNLFPKVAPQAISSVENIEGNGGPGTI KKISFPEGFPFKYVKDRVDEVDHTNFKYNYSVIEGGPIGDTLEKISNEIKIVAT PDGGSILKISNKYHTKGDHEVKAEQVKASKEMGETLLRAVESYLLAHSDAYN 130975 Bet v 2 (SEQ ID NO: 382) MSWQTYVDEHLMCDIDGQASNSLASAIVGHDGSVWAQSSSFPQFKPQEITGI MKDFEEPGHLAPTGLHLGGIKYMVIQGEAGAVIRGKKGSGGITIKKTGQALV FGIYEEPVTPGQCNMVVERLGDYLIDQGL 1168696 Bet v 3 (SEQ ID NO: 383) MPCSTEAMEKAGHGHASTPRKRSLSNSSFRLRSESLNTLRLRRIFDLFDKNSD GIITVDELSRALNLLGLETDLSELESTVKSFTREGNIGLQFEDFISLHQSLNDSY FAYGGEDEDDNEEDMRKSILSQEEADSFGGFKVFDEDGDGYISARELQMVL GKLGFSEGSEIDRVEKMIVSVDSNRDGRVDFFEFKDMMRSVLVRSS 809536 Bet v 4 (SEQ ID NO: 384) MADDHPQDKAERERIFKRFDANGDGKISAAELGEALKTLGSITPDEVKHMM AEIDTDGDGFISFQEFTDFGRANRGLLKDVAKIF 543675 Que a I-Quercus alba = oak trees (fragment) (SEQ ID NO: 385) GVFTXESQETSVIAPAXLFKALFL 543509 Car b I-Carpinus betulus = hornbeam trees (fragment) (SEQ ID NO: 386) GVFNYEAETPSVIPAARLFKSYVLDGDKLIPKVAPQAIXK 543491 Aln g I-Alnus glutinosa = alder trees (fragment) (SEQ ID NO: 387) GVFNYEAETPSVIPAARLFKAFILDGDKLLPKVAPEAVSSVENI 1204056 Rubisco (SEQ ID NO: 388) VQCMQVWPPLGLKKFETLSYLPPLSSEQLAKEVDYLLRKNLIPCLEFELEHG FVYREHNRSPGYYDGRYWTMWKLPMFGCNDSSQVLKELEECKKAYPSAFI RIIGFDDK

Additional tree allergen sequences (NCBI entrez accession number): 131919; 128193; 585564; 1942360; 2554672; 2392209; 2414158; 1321728; 1321726; 1321724; 1321722; 1321720; 1321718; 1321716; 1321714; 1321712; 3015520; 2935416; 464576; 1705843; 1168701; 1168710; 1168709; 1168708; 1168707; 1168706; 1168705; 1168704; 1168703; 1168702; 1842188; 2564228; 2564226; 2564224; 2564222; 2564220; 2051993; 1813891; 1536889; 534910; 534900; 534898; 1340000; 1339998; 2149808; 66207; 2129477; 1076249; 1076247; 629480; 481805; 81443; 1361968; 1361967; 1361966; 1361965; 1361964; 1361963; 1361962; 1361961; 1361960; 1361959; 320546; 629483 ; 629482; 629481; 541804; 320545; 81444; 541814; 629484; 474911; 452742; 1834387; 298737; 298736; 1584322; 1584321; 584320; 1542873; 1542871; 1542869; 1542867; 1542865; 1542863; 1542861; 1542859; 1542857; 1483232; 1483230; 1483228; 558561; 551640; 488605; 452746; 452744; 452740; 452738; 452736; 452734; 452732; 452730; 452728; 450885; 17938; 17927; 17925; 17921; 297538; 510951; 289331; 289329; 166953.

Peanut

[0102] Peanut sequences

TABLE-US-00012 1168391 Ara h 1 (SEQ ID NO: 389) MRGRVSPLMLLLGILVLASVSATHAKSSPYQKKTENPCAQRCLQSCQ QEPDDLKQKACESRCTKLEYDPRCVYDPRGHTGTTNQRSPPGERTRG RQPGDYDDDRRQPRREEGGRWGPAGPREREREEDWRQPREDWRRPSH QQPRKIRPEGREGEQEWGTPGSHVREETSRNNPFYFPSRRFSTRYGN QNGRIRVLQRFDQRSRQFQNLQNHRIVQIEAKPNTLVLPKHADADNI LVIQQGQATVTVANGNNRKSFNLDEGHALRIPSGFISYILNRHDNQN LRVAKISMPVNTPGQFEDFFPASSRDQSSYLQGFSRNTLEAAFNAEF NEIRRVLLEENAGGEQEERGQRRWSTRSSENNEGVIVKVSKEHVEEL TKHAKSVSKKGSEEEGDITNPINLREGEPDLSNNFGKLFEVKPDKKN PQLQDLDMMLTCVEIKEGALMLPHFNSKAMVIVVVNKGTGNLELVAV RKEQQQRGRREEEEDEDEEEEGSNREVRRYTARLKEGDVFIMPAAHP VAINTASSELHLLGFGINAENNHRIFLAGDKDNVIDQIEKQAKDLAF PGSGEQVEKLIKNQKESHFVSARPQSQSQSPSSPEKESPEKEDQEEE NQGGKGPLLSILKAFN

Ragweed

Ambrosia Sequences

TABLE-US-00013

[0103] 113478 Amb a 1 (SEQ ID NO: 390) MGIKHCCYILYFTLALVTLLQPVRSAEDLQQILPSANETRSLTTCGT YNIIDGCWRGKADWAENRKALADCAQGFAKGTIGGKDGDIYTVTSEL DDDVANPKEGTLRFGAAQNRPLWIIFARDMVIRLDRELAINNDKTID GRGAKVEIINAGFAIYNVKNIIIHNIIMHDIVVNPGGLIKSHDGPPV PRKGSDGDAIGISGGSQIWIDHCSLSKAVDGLIDAKHGSTHFTVSNC LFTQHQYLLLFWDFDERGMLCTVAFNKFTDNVDQRMPNLRHGFVQVV NNNYERWGSYALGGSAGPTILSQGNRFLASDIKKEVVGRYGESAMSE SINWNWRSYMDVFENGAIFVPSGVDPVLTPEQNAGMIPAEPGEAVLR LTSSAGVLSCQPGAPC 113479 Amb a 2 (SEQ ID NO: 391) MGIKHCCYILYFTLALVTLVQAGRLGEEVDILPSPNDTRRSLQGCEA HNIIDKCWRCKPDWAENRQALGNCAQGFGKATHGGKWGDIYMVTSDQ DDDVVNPKEGTLRFGATQDRPLWIIFQRDMIIYLQQEMVVTSDKTID GRGAKVELVYGGITLMNVKNVIIHNIDIHDVRVLPGGRIKSNGGPAI PRHQSDGDAIHVTGSSDIWIDHCTLSKSFDGLVDVNWGSTGVTISNC KFTHHEKAVLLGASDTHFQDLKMHVTLAYNIFTNTVHERMPRCRFGF FQIVNNFYDRWDKYAIGGSSNPTILSQGNKFVAPDFIYKKNVCLRTG AQEPEWMTWNWRTQNDVLENGAIFVASGSDPVLTAEQNAGMMQAEPG DMVPQLTMNAGVLTCSPGAPC 113477 Amb a 1.3 (SEQ ID NO: 392) MGIKQCCYILYFTLALVALLQPVRSAEGVGEILPSVNETRSLQACEA LNIIDKCWRGKADWENNRQALADCAQGFAKGTYGGKWGDVYTVTSNL DDDVANPKEGTLRFAAAQNRPLWIIFKNDMVINLNQELVVNSDKTID GRGVKVEIINGGLTLMNVKNIIIHNINIHDVKVLPGGMIKSNDGPPI LRQASDGDTINVAGSSQIWIDHCSLSKSFDGLVDVTLGSTHVTISNC KFTQQSKAILLGADDTHVQDKGMLATVAFNMFTDNVDQRMPRCRFGF FQVVNNNYDRWGTYAIGGSSAPTILCQGNRFLAPDDQIKKNVLARTG TGAAESMAWNWRSDKDLLENGAIFVTSGSDPVLTPVQSAGMIPAEPG EAAIKLTSSAGVFSCHPGAPC 113476 Amb a 1.2 (SEQ ID NO: 393) MGIKHCCYILYFTLALVTLLQPVRSAEDVEEFLPSANETRRSLKACE AHNIIDKCWRCKADWANNRQALADCAQGFAKGTYGGKHGDVYTVTSD KDDDVANPKEGTLRFAAAQNRPLWIIFKRNMVIHLNQELVVNSDKTI DGRGVKVNIVNAGLTLMNVKNIIIHNINIHDIKVCPGGMIKSNDGPP ILRQQSDGDAINVAGSSQIWIDHCSLSKASDGLLDITLGSSHVTVSN CKFTQHQFVLLLGADDTHYQDKGMLATVAFNMFTDHVDQRMPRCRFG FFQVVNNNYDRWGTYAIGGSSAPTILSQGNRFFAPDDIIKKNVLART GTGNAESMSWNWRTDRDLLENGAIFLPSGSDPVLTPEQKAGMIPAEP GEAVLRLTSSAGVLSCHQGAPC 113475 Amb a 1.1 (SEQ ID NO: 394) MGIKHCCYILYFTLALVTLLQPVRSAEDLQEILPVNETRRLTTSGAY NIIDGCWRGKADWAENRKALADCAQGFGKGTVGGKDGDIYTVTSELD DDVANPKEGTLRFGAAQNRPLWIIFERDMVIRLDKEMVVNSDKTIDG RGAKVEIINAGFTLNGVKNVIIHNINMHDVKVNPGGLIKSNDGPAAP RAGSDGDAISISGSSQIWIDHCSLSKSVDGLVDAKLGTTRLTVSNSL FTQHQFVLLFGAGDENIEDRGMLATVAFNTFTDNVDQRMPRCRHGFF QVVNNNYDKWGSYAIGGSASPTILSQGNRFCAPDERSKKNVLGRHGE AAAESMKWNWRTNKDVLENGAIFVASGVDPVLTPEQSAGMIPAEPGE SALSLTSSAGVLSCQPGAPC

Cedar Sequences

TABLE-US-00014

[0104] 493634 Cry j IB precursor (SEQ ID NO: 395) MDSPCLVALLVFSFVIGSCFSDNPIDSCWRGDSNWAQNRMKLADCAV GFGSSTMGGKGGDLYTVTNSDDDPVNPPGTLRYGATRDRPLWIIFSG NMNIKLKMPMYIAGYKTFDGRGAQVYIGNGGPCVFIKRVSNVIIHGL YLYGCSTSVLGNVLINESFGVEPVHPQDGDALTLRTATNIWIDHNSF SNSSDGLVDVTLTSTGVTISNNLFFNHHKVMSLGHDDAYSDDKSMKV TVAFNQFGPNCGQRMPRARYGLVHVANNNYDPWTIYAIGGSSNPTIL SEGNSFTAPNESYKKQVTIRIGCKTSSSCSNWVWQSTQDVFYNGAYF VSSGKYEGGNIYTKKEAFNVENGNATPHLTQNAGVLTCSLSKRC 493632 Cry j IA precursor (SEQ ID NO: 396) MDSPCLVALLVLSFVIGSCFSDNPIDSCWRGDSNWAQNRMKLADCAV GFGSSTMGGKGGDLYTVTNSDDDPVNPAPGTLRYGATRDRPLWIIFS GNMNIKLKMPMYIAGYKTFDGRGAQVYIGNGGPCVFIKRVSNVIIHG LHLYGCSTSVLGNVLINESFGVEPVHPQDGDALTLRTATNIWIDHNS FSNSSDGLVDVTLSSTGVTISNNLFFNHHKVMLLGHDDAYSDDKSMK VTVAFNQFGPNCGQRMPRARYGLVHVANNNYDPWTIYAIGGSSNPTI LSEGNSFTAPNESYKKQVTIRIGCKTSSSCSNWVWQSTQDVFYNGAY FVSSGKYEGGNIYTKKEAFNVENGNATPQLTKNAGVLTCSLSKRC 1076242 Cry j II precursor- Japanese cedar (SEQ ID NO: 397) MAMKLIAPMAFLAMQLIIMAAAEDQSAQIMLDSVVEKYLRSNRSLRK VEHSRHDAINIFNVEKYGAVGDGKHDCTEAFSTAWQAACKNPSAMLL VPGSKKFVVNNLFFNGPCQPHFTFKVDGIIAAYQNPASWKNNRIWLQ FAKLTGFTLMGKGVIDGQGKQWWAGQCKWVNGREICNDRDRPTAIKF DFSTGLIIQGLKLMNSPEFHLVFGNCEGVKIIGISITAPRDSPNTDG IDIFASKNFHLQKNTIGTGDDCVAIGTGSSNIVIEDLICGPGHGISI GSLGRENSRAEVSYVHVNGAKFIDTQNGLRIKTWQGGSGMASHIIYE NVEMINSENPILINQFYCTSASACQNQRSAVQIQDVTYKNIRGTSAT AAAIQLKCSDSMPCKDIKLSDISLKLTSGKIASCLNDNANGYFSGHV IPACKNLSPSAKRKESKSHKHPKTVMVENMRAYDKGNRTRILLGSRP PNCTNKCHGCSPCKAKLVIVHRIMPQEYYPQRWICSCHGKIYHP 1076241 Cry j II protein- Japanese cedar (SEQ ID NO: 398) MAMKFIAPMAFVAMQLIIMAAAEDQSAQIMLDSDIEQYLRSNRSLRK VEHSRHDAINIFNVEKYGAVGDGKHDCTEAFSTAWQAACKKPSAMLL VPGNKKFVVNNLFFNGPCQPHFTFKVDGIIAAYQNPASWKNNRIWLQ FAKLTGFTLMGKGVIDGQGKQWWAGQCKWVNGREICNDRDRPTAIKF DFSTGLIIQGLKLMNSPEFHLVFGNCEGVKIIGISITAPRDSPNTDG IDIFASKNFHLQKNTIGTGDDCVAIGTGSSNIVIEDLICGPGHGISI GSLGRENSRAEVSYVHVNGAKFIDTQNGLRIKTWQGGSGMASHIIYE NVEMINSENPILINQFYCTSASACQNQRSAVQIQDVTYKNIRGTSAT AAAIQLKCSDSMPCKDIKLSDISLKLTSGKIASCLNDNANGYFSGHV IPACKNLSPSAKRKESKSHKHPKTVMVKNMGAYDKGNRTRILLGSRP PNCTNKCHGCSPCKAKLVIVHRIMPQEYYPQRWMCSRHGKIYHP 541803 Cry j I precursor- Japanese cedar (SEQ ID NO: 399) MDSPCLVALLVLSFVIGSCFSDNPIDSCWRGDSNWAQNRMKLADCAV GFGSSTMGGKGGDLYTVTNSDDDPVNPPGTLRYGATRDRPLWIIFSG NMNIKLKMPMYIAGYKTFDGRGAQVYIGNGGPCVFIKRVSNVIIHGL HLYGCSTSVLGNVLINESFGVEPVHPQDGDALTLRTATNIWIDHNSF SNSSDGLVDVTLSSTGVTISNNLFFNHHKVMLLGHDDAYSDDKSMKV TVAFNQFGPNCGQRMPRARYGLVHVANNNYDPWTIYAIGGSSNPTIL SEGNSFTAPNESYKKQVTIRIGCKTSSSCSNWVWQSTQDVFYNGAYF VSSGKYEGGNIYTKKEAFNVENGNATPQLTKNAGVLTCSLSKRC 541802 Cry j I precursor- Japanese cedar (SEQ ID NO: 400) MDSPCLVALLVFSFVIGSCFSDNPIDSCWRGDSNWAQNRMKLADCAV GFGSSTMGGKGGDLYTVTNSDDDPVNPAPGTLRYGATRDRPLWIIFS GNMNIKLKMPMYIAGYKTFDGRGAQVYIGNGGPCVFIKRVSNVIIHG LYLYGCSTSVLGNVLINESFGVEPVHPQDGDALTLRTATNIWIDHNS FSNSSDGLVDVTLTSTGVTISNNLFFNHHKVMSLGHDDAYSDDKSMK VTVAFNQFGPNCGQRMPRARYGLVHVANNNYDPWTIYAIGGSSNPTI LSEGNSFTAPNESYKKQVTIRIGCKTSSSCSNWVWQSTQDVFYNGAY FVSSGKYEGGNIYTKKEAFNVENGNATPHLTQNAGVLTCSLSKRC

Dog

Canis Sequences:

TABLE-US-00015

[0105] Can f 1 (SEQ ID NO: 401) MKTLLLTIGFSLIAILQAQDTPALGKDTVAVSGKWYLKAMTADQEVP EKPDSVTPMILKAQKGGNLEAKITMLTNGQCQNITVVLHKTSEPGKY TAYEGQRVVFIQPSPVRDHYILYCEGELHGRQIRMAKLLGRDPEQSQ EALEDFREFSRAKGLNQEILELAQSETCSPGGQ Serum albumin fragment (SEQ ID NO: 402) EAYKSEIAHRYNDLGEEHFRGLVL Serum albumin fragment (SEQ ID NO: 403) LSSAKERFKCASLQKFGDRAFKAWSVARLSQRFPKADFAEISKVVTD LTKVHKECCHGDLLECADDRADLAKYMCENQDSISTKLKECCDKPVL EKSQCLAEVERDELPGDLPSLAADFVEDKEVCKNYQEAKDVFLGTFL YEYSRRHPEYSVSLLLRLAKEYEATLEKCCATDDPPTCYAKVLDEFK PLVDEPQNLVKTNCELFEKLGEYGFQNALLVRYTKKAPQVSTPTLVV EVSRKLGKVGTKCCKKPESERMSCADDFLS Can f 2 (SEQ ID NO: 404) MQLLLLTVGLALICGLQAQEGNHEEPQGGLEELSGRWHSVALASNKS DLIKPWGHFRVFIHSMSAKDGNLHGDILIPQDGQCEKVSLTAFKTAT SNKFDLEYWGHNDLYLAEVDPKSYLILYMINQYNDDTSLVAHLMVRD LSRQQDFLPAFESVCEDIGLHKDQIVVLSDDDRCQGSRD

Additional Dog Allergen Protein (NCBI Entrez Accession):

[0106] 1731859

Horse

Equus Sequences:

TABLE-US-00016

[0107] 1575778 Equ c 1 (SEQ ID NO: 405) MKLLLLCLGLILVCAQQEENSDVAIRNFDISKISGEWYSIFLASDVK EKIEENGSMRVFVDVIRALDNSSLYAEYQTKVNGECTEFPMVFDKTE EDGVYSLNYDGYNVFRISEFENDEHIILYLVNFDKDRPFQLFEFYAR EPDVSPEIKEEFVKIVQKRGIVKENIIDLTKIDRCFQLRGNGVAQA 3121755 Equ c 2 (SEQ ID NO: 406) SQXPQSETDYSQLSGEWNTIYGAASNIXK

Euroglyphus (Mite)

Euroglyphus Sequences:

TABLE-US-00017

[0108] Eur m 1 (variant) (SEQ ID NO: 407) TYACSINSVSLPSELDLRSLRTVTPIRMQGGCGSCWAFSGVASTESA YLAYRNMSLDLAEQELVDCASQNGCHGDTIPRGIEYIQQNGVVQEHY YPYVAREQSCHRPNAQRYGLKNYCQISPPDSNKIRQALTQTHTAVAV IIGIKDLNAFRHYDGRTIMQHDNGYQPNYHAVNIVGYGNTQGVDYWI VRNSWDTTWGDNGYGYFAANINL Eur m 1 (variant) (SEQ ID NO: 408) TYACSINSVSLPSELDLRSLRTVTPIRMQGGCGSCWAFSGVASTESA YLAYRNMSLDLAEQELVDCASQNGCHGDTIPRGIEYIQQNGVVQEHY YPYVAREQSCHRPNAQRYGLKNYCQISPPDSNKIRQALTQTHTAVAV IIGIKDLNAFRHYDGRTIMQHDNGYQPNYHAVNIVGYGNTQGVDYWI VRNSWDTTWGDNGYGYFAANINL Eur m 1 (variant) (SEQ ID NO: 409) ETNACSINGNAPAEIDLRQMRTVTPIRMQGGCGSCWAFSGVAATESA YLAYRNQSLDLAEQELVDCASQHGCHGDTIPRGIEYIQHNGVVQESY YRYVAREQSCRRPNAQRFGISNYCQIYPPNANKIREALAQTHSAIAV IIGIKDLDAFRHYDGRTIIQRDNGYQPNYHAVNIVGYSNAQGVDYWI VRNSWDTNWGDNGYGYFAANIDL Eur m 1 (variant) (SEQ ID NO: 410) ETSACRINSVNVPSELDLRSLRTVTPIRMQGGCGSCWAFSGVAATES AYLAYRNTSLDLSEQELVDCASQHGCHGDTIPRGIEYIQQNGVVEER SYPYVAREQQCRRPNSQHYGISNYCQIYPPDVKQIREALTQTHTAIA VIIGIKDLRAFQHYDGRTIIQHDNGYQPNYHAVNIVGYGSTQGVDYW IVRNSWDTTWGDSGYGYFQAGNNL

Poa (Grass) Sequences

TABLE-US-00018

[0109] 113562 POLLEN ALLERGEN POA P 9 (SEQ ID NO: 411) MAVQKYTVALFLVALVVGPAASYAADLSYGAPATPAAPAAGYTPAAP AGAAPKATTDEQKMIEKINVGFKAAVAAAGGVPAANKYKTFVATFGA ASNKAFAEALSTEPKGAAVDSSKAALTSKLDAAYKLAYKSAEGATPE AKYDDYVATLSEALRIIAGTLEVHGVKPAAEEVKATPAGELQVIDKV DAAFKVAATAANAAPANDKFTVFEAAFNDAIKASTGGAYQSYKFIPA LEAAVKQSYAATVATAPAVKYTVFETALKKAITAMSQAQKAAKPAAA ATGTATAAVGAATGAATAAAGGYKV 113561 POA P 9 (SEQ ID NO: 412) MAVHQYTVALFLAVALVAGPAASYAADVGYGAPATLATPATPAAPAA GYTPAAPAGAAPKATTDEQKLIEKINAGFKAAVAAAAGVPAVDKYKT FVATFGTASNKAFAEALSTEPKGAAAASSNAVLTSKLDAAYKLAYKS AEGATPEAKYDAYVATLSEALRIIAGTLEVHAVKPAGEEVKAIPAGE LQVIDKVDAAFKVAATAANAAPANDKFTVFEAAFNDAIKASTGGAYQ SYKFIPALEAAVKQSYAATVATAPAVKYTVFETALKKAITAMSQAQK AAKPAAAVTATATGAVGAATGAVGAATGAATAAAGGYKTGAATPTAG GYKV 113560 POA P 9 (SEQ ID NO: 413) MDKANGAYKTALKAASAVAPAEKFPVFQATFDKNLKEGLSGPDAVGF AKKLDAFIQTSYLSTKAAEPKEKFDLFVLSLTEVLRFMAGAVKAPPA SKFPAKPAPKVAAYTPAAPAGAAPKATTDEQKLIEKINVGFKAAVAA AAGVPAASKYKTFVATFGAASNKAFAEALSTEPKGAAVASSKAVLTS KLDAAYKLAYKSAEGATPEAKYDAYVATLSEALRIIAGTLEVHGVKP AAEEVKAIPAGELQVIDKVDAAFKVAATAANAAPANDKFTVFEAAFN DAIKASTGGAYQSYKFIPALEAAVKQSYAATVATAPAVKYTVFETAL KKAITAMSQAQKAAKPAAAVTGTATSAVGAATGAATAAAGGYKV

Cockroach Sequences

TABLE-US-00019

[0110] 2833325 Cr p 1 (SEQ ID NO: 414) MKTALVFAAVVAFVAARFPDHKDYKQLADKQFLAKQRDVLRLFHRVH QHNILNDQVEVGIPMTSKQTSATTVPPSGEAVHGVLQEGHARPRGEP FSVNYEKHREQAIMLYDLLYFANDYDTFYKTACWARDRVNEGMFMYS FSIAVFHRDDMQGVMLPPPYEVYPYLFVDHDVIHMAQKYWMKNAGSG EHHSHVIPVNFTLRTQDHLLAYFTSDVNLNAFNTYYRYYYPSWYNTT LYGHNIDRRGEQFYYTYKQIYARYFLERLSNDLPDVYPFYYSKPVKS AYNPNLRYHNGEEMPVRPSNMYVTNFDLYYIADIKNYEKRVEDAIDF GYAFDEHMKPHSLYHDVHGMEYLADMIEGNMDSPNFYFYGSIYHMYH SMIGHIVDPYHKMGLAPSLEHPETVLRDPVFYQLWKRVDHLFQKYKN RLPRYTHDELAFEGVKVENVDVGKLYTYFEQYDMSLDMAVYVNNVDQ ISNVDVQLAVRLNHKPFTYNIEVSSDKAQDVYVAVFLGPKYDYLGRE YDLNDRRHYFVEMDRFPYHVGAGKTVIERNSHDSNIIAPERDSYRTF YKKVQEAYEGKSQYYVDKGHNYCGYPENLLIPKGKKGGQAYTFYVIV TPYVKQDEHDFEPYNYKAFSYCGVGSERKYPDNKPLGYPFDRKIYSN DFYTPNMYFKDVIIFHKKYDEVGVQGH 2231297 Cr p 2 (SEQ ID NO: 415) INEIHSIIGLPPFVPPSRRHARRGVGINGLIDDVIAILPVDELKALF QEKLETSPDFKALYDAIRSPEFQSIISTLNAMQRSEHHQNLRDKGVD VDHFIQLIRALFGLSRAARNLQDDLNDFLHSLEPISPRHRHGLPRQR RRSARVSAYLHADDFHKIITTIEALPEFANFYNFLKEHGLDVVDYIN EIHSIIGLPPFVPPSRRHARRGVGINGLIDDVIAILPVDELKALFQE KLETSPDFKALYDAIRSPEFQSIISTLNAMPEYQELLQNLRDKGVDV DHFIRVDQGTLRTLSSGQRNLQDDLNDFLALIPTDQILAIAMDYLAN DAEVQELVAYLQSDDFHKIITTIEALPEFANFYNFLKEHGLDVVDYI NEIHSIIGLPPFVPPSQRHARRGVGINGLIDDVIAILPVDELKALFQ EKLETSPDFKALYDAIDLRSSRA 1703445 Bla g 2 (SEQ ID NO: 416) MIGLKLVTVLFAVATITHAAELQRVPLYKLVHVFINTQYAGITKIGN QNFLTVFDSTSCNVVVASQECVGGACVCPNLQKYEKLKPKYISDGNV QVKFFDTGSAVGRGIEDSLTISNLTTSQQDIVLADELSQEVCILSAD VVVGIAAPGCPNALKGKTVLENFVEENLIAPVFSIHHARFQDGEHFG EIIFGGSDWKYVDGEFTYVPLVGDDSWKFRLDGVKIGDTTVAPAGTQ AIIDTSKAIIVGPKAYVNPINEAIGCVVEKTTTRRICKLDCSKIPSL PDVTFVINGRNFNISSQYYIQQNGNLCYSGFQPCGHSDHFFIGDFFV DHYYSEFNWENKTMGFGRSVESV 1705483 Bla g 4 (SEQ ID NO: 417) AVLALCATDTLANEDCFRHESLVPNLDYERFRGSWIIAAGTSEALTQ YKCWIDRFSYDDALVSKYTDSQGKNRTTIRGRTKFEGNKFTIDYNDK GKAFSAPYSVLATDYENYAIVEGCPAAANGHVIYVQIRFSVRRFHPK LGDKEMIQHYTLDQVNQHKKAIEEDLKHFNLKYEDLHSTCH 2326190 Bla g 5 (SEQ ID NO: 418) YKLTYCPVKALGEPIRFLLSYGEKDFEDYRFQEGDWPNLKPSMPFGK TPVLEIDGKQTHQSVAISRYLGKQFGLSGKDDWENLEIDMIVDTISD FRAAIANYHYDADENSKQKKWDPLKKETIPYYTKKFDEVVKANGGYL AAGKLTWADFYFVAILDYLNHMAKEDLVANQPNLKALREKVLGLPAI KAWVAKRPPTDL

Additional Cockroach Sequences (NCBI Entrez Accession Numbers):

[0111] 2580504; 1580797; 1580794; 1362590; 544619; 544618; 1531589; 1580792; 1166573; 1176397; 2897849.

Allergen (General) Sequences:

NCBI Accession Numbers

[0112] 2739154; 3719257; 3703107; 3687326; 3643813; 3087805; 1864024; 1493836; 1480457; 2598976; 2598974; 1575778; 763532; 746485; 163827; 163823; 3080761; 163825; 3608493; 3581965; 2253610; 2231297; 2897849; 3409499; 3409498; 3409497; 3409496; 3409495; 3409494; 3409493; 3409492; 3409491; 3409490; 3409489; 3409488; 3409487; 3409486; 3409485; 3409484; 3409483; 3409482; 3409481; 3409480; 3409479; 3409478; 3409477; 3409476; 3409475; 3409474; 3409473; 3409472; 3409471; 3409470; 3409469; 3409468; 3409467; 3409466; 3409465; 3409464; 3409463; 3409462; 3409461; 3409460; 3409459; 3409458; 3409457; 3409456; 3318885; 3396070 ; 3367732; 1916805; 3337403; 2851457; 2851456; 1351295; 549187; 136467; 1173367; 2499810; 2498582; 2498581; 1346478; 1171009; 126608; 114091; 2506771; 1706660; 1169665; 1169531; 232086; 416898; 114922; 2497701; 1703232; 1703233; 1703233; 1703232; 3287877; 3122132; 3182907; 3121758; 3121756; 3121755; 3121746; 3121745; 3319925; 3319923; 3319921; 3319651; 3318789; 3318779; 3309647; 3309047; 3309045; 3309043; 3309041; 3309039; 3288200; 3288068; 2924494; 3256212; 3256210; 3243234; 3210053; 3210052; 3210051; 3210050; 3210049; 3210048; 3210047; 3210046; 3210045; 3210044; 3210043; 3210042; 3210041; 3210040; 3210039; 3210038; 3210037; 3210036; 3210035; 3210034; 3210033; 3210032; 3210031; 3210030; 3210029; 3210028; 3210027; 3210026; 3210025; 3210024; 3210023; 3210022; 3210021; 3210020; 3210019; 3210018; 3210017; 3210016; 3210015; 3210014; 3210013; 3210012; 3210011; 3210010; 3210009; 3210008; 3210007; 3210006; 3210005; 3210004; 3210003; 3210002; 3210001; 3210000; 3209999; 3201547; 2781152; 2392605; 2392604; 2781014; 1942360; 2554672; 2392209; 3114481; 3114480; 2981657; 3183706; 3152922 ; 3135503 ; 3135501; 3135499; 3135497; 2414158; 1321733; 1321731; 1321728; 1321726; 1321724; 1321722; 1321720; 1321718; 1321716; 1321714; 1321712; 3095075; 3062795; 3062793; 3062791; 2266625; 2266623; 2182106; 3044216; 2154736; 3021324; 3004467; 3005841; 3005839; 3004485; 3004473; 3004471; 3004469; 3004465; 2440053; 1805730; 2970629 ; 2959898; 2935527 ; 2935416; 809536; 730091; 585279; 584968; 2498195; 2833325; 2498604; 2498317; 2498299; 2493414; 2498586; 2498585; 2498576; 2497749; 2493446; 2493445; 1513216 ; 729944; 2498099; 548449; 465054; 465053; 465052; 548671; 548670; 548660; 548658; 548657; 2832430; 232084; 2500822; 2498118; 2498119; 2498119; 2498118; 1708296; 1708793; 416607; 416608; 416608; 416607; 2499791; 2498580; 2498579; 2498578; 2498577; 2497750; 1705483; 1703445; 1709542; 1709545; 1710589; 1352699; 1346568; 1346323; 1346322; 2507248; 11352240; 1352239; 1352237; 1352229; 1351935; 1350779; 1346806; 1346804; 1346803; 1170095; 1168701; 1352506; 1171011; 1171008; 1171005; 1171004; 1171002; 1171001; 1168710; 1168709; 1168708; 1168707; 1168706; 1168705; 1168704; 1168703; 1168702; 1168696; 1168391; 1168390; 1168348; 1173075; 1173074; 1173071; 1169290; 1168970; 1168402; 729764; 729320; 729979; 729970; 729315; 730050; 730049; 730048; 549194; 549193; 549192; 549191; 549190; 549189; 549188; 549185; 549184; 549183; 549182; 549181; 549180; 549179; 464471; 585290; 416731; 1169666; 113478; 113479; 113477; 113476; 113475; 130975; 119656; 113562; 113561; 113560; 416610; 126387; 126386; 126385; 132270; 416611; 416612; 416612; 416611; 730035; 127205; 1352238; 125887; 549186; 137395; 730036; 133174; 114090; 131112; 126949; 129293; 124757; 129501; 416636; 2801531; 2796177; 2796175; 2677826; 2735118; 2735116; 2735114; 2735112; 2735110; 2735108; 2735106 ; 2735104; 2735102 ; 2735100 ; 2735098 ; 2735096 ; 2707295 ; 2154730; 2154728; 1684720; 2580504 ; 2465137; 2465135; 2465133; 2465131; 2465129; 2465127; 2564228; 2564226; 2564224; 2564222; 2564220; 2051993; 1313972; 1313970; 1313968; 1313966; 2443824 ; 2488684; 2488683; 2488682; 2488681; 2488680; 2488679; 2488678; 2326190 ; 2464905; 2415702; 2415700; 2415698; 2398759; 2398757; 2353266 ; 2338288 ; 1167836; 414703 ; 2276458 ; 1684718 ; 2293571 ; 1580797 ; 1580794 ; 2245508 ; 2245060; 1261972; 2190552 ; 1881574 ; 511953 ; 1532058; 1532056; 1532054; 1359436; 666007; 487661; 217308; 1731859; 217306; 217304; 1545803; 1514943; 577696; 516728; 506858; 493634; 493632; 2154734; 2154732; 543659; 1086046; 1086045; 2147643; 2147642; 1086003; 1086002; 1086001; 543675; 543623; 543509; 543491; 1364099; 2147108; 2147107; 1364001; 1085628; 631913; 631912; 631911; 2147092; 477301; 543482; 345521; 542131; 542130; 542129; 100636; 2146809; 480443; 2114497; 2144915; 72355; 71728; 319828; 1082946; 1082945; 1082944; 539716; 539715; 423193; 423192; 423191; 423190; 1079187; 627190; 627189; 627188; 627187; 482382; 1362656; 627186; 627185; 627182; 482381; 85299; 85298; 2133756; 2133755; 1079186; 627181; 321044; 321043; 112559; 112558; 1362590; 2133564; 1085122; 1078971; 627144; 627143; 627142; 627141; 280576; 102835; 102834; 102833; 102832; 84703; 84702; 84700; 84699; 84698; 84696; 477888; 477505; 102575; 102572; 478272; 2130094; 629813; 629812; 542172; 542168; 542167; 481432; 320620; 280414; 626029; 542132; 320615; 320614; 100638; 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[0113] Particularly preferred T cell epitopes are derived from the allergens: cat dander protein Fel d1; House dust mite proteins Der P1, Der P2 and Der P7; Ragweed protein amb a 1.1, a 1.2, a1.3 or a1.4; Rye grass proteins lol p1 and lol p5; Timothy grass proteins phl p1 and phl p5; Bermuda grass protein Cyn d 5; Alternaria alternate proteins Alt a 1, Alt a 2 and Enolase (Alt a 6); Birch protein Bet v1 and P14; German Cockroach proteins Bla g 1, Bla g 2, Bla g 3, Bla g 4, Bla g 5 and Bla g 6; Mugwort protein Art v 1; Russian thistle protein Sal k 1 and Sal k 2; peanut Ara h1, Ara h2, Ara h3, Ara h4, Ara h5, Ara h6, plant profilins or lipid transfer proteins or a human leukocyte antigen.

[0114] Suitable autoimmune antigens from which the MHC Class II-binding T cell epitope may derive can of course be obtained and/or produced using known methods. Suitable autoimmune antigens include the major antigens in the following autoimmune diseases: Acute disseminated encephalomyelitis (ADEM); Addison's disease; Ankylosing spondylitis; Antiphospholipid antibody syndrome (APS); Aplastic anemia; Autoimmune hepatitis; Autoimmune Oophoritis; Coeliac disease; Crohn's disease; Diabetes mellitus type 1; Gestational pemphigoid; Goodpasture's syndrome; Graves' disease; Guillain-Barre syndrome (GBS); Hashimoto's disease; Idiopathic thrombocytopenic purpura; Kawasaki's Disease; Lupus erythematosus; Multiple sclerosis; Myasthenia gravis; Opsoclonus myoclonus syndrome (OMS); Optic neuritis; Ord's thyroiditis; Pemphigus; Pernicious anaemia; Polyarthritis in dogs; Primary biliary cirrhosis; Rheumatoid arthritis; Reiter's syndrome; Sjogren's syndrome; Takayasu's arteritis; Temporal arteritis (also known as "giant cell arteritis"); Warm autoimmune hemolytic anemia; Wegener's granulomatosis.

[0115] Other preferred eptiopes may be derived from antigens involved with maternal-foetal immunes responses, for example Rhesus D antigens involved in Rhesus D Haemolytic Disease of the Newborn.

[0116] Other preferred epitopes may be derived from antigens involved in graft-versus-host disease or transplant rejection (alloimmune responses), for example from MHC Class I molecules (otherwise referred to as human leukocyte antigens-HLA), preferably from the .alpha.3 domain and/or transmembrane domain of MHC Class I molecules, most preferably from the human MHC Class I molecule HLA-A2.

[0117] The epitopes may be of proteins which are administered to the individual, for example for therapy. Such proteins may act as neoantigens in the individual, such as for example in the situation where the individual does not express the protein. The therapeutic protein may be factor IIX or salcatonin.

[0118] Particularly suitable proteins from which to derive the epitope sequences of the invention are those which have a low frequency of epitopes per amino acid residue, i.e. the ratio of amino acids in the minimal binding sequence of an epitope, relative to the total number of amino acids in the protein ("the epitope ratio") is low. A protein with a low frequency of epitopes per amino acid residue typically has an epitope ratio of 1:35, 1:40, 1:45, 1:50, 1:55, 1:60 or 1:65. These proteins are preferred sources of epitope sequences of the invention because a high proportion of the different epitope sequences derived from such proteins typically overlap. In general, the percentage of epitope sequences which overlap with at least one other epitope sequence, as a proportion of the total number of epitopes in a protein with a low epitope ratio as defined above, is greater than 60%, 65%, 70%, 80% or 90%.

[0119] The following Examples illustrate the invention:

EXAMPLE 1

House Dust Mite Peptides from Der p 1, Der p2 and Der p 7

MHC Class II Binding Search

[0120] The aim of this study is to identify peptides with strong affinities for the seven most common human MHC Class II HLA-DRB1* allotypes (covering in total around 63% of the allotypes found in the average Caucasian population). In order to identify binding peptides in the House Dust Mite (HDM) allergens, Der p 1, Der p 2 and Der p 7, in vitro binding assays have been performed on a subset of peptides from these allergenic proteins. Peptides for testing in the binding assays were initially identified by an in silico approach known as "peptide threading" (carried out by Biovation, Ltd.,Aberdeen, Scotland, UK). This is a bioinformatic analysis of consecutive peptides from a sequence for the potential to be accommodated within the binding groove of MHC class II HLA-DR molecules. This subset of peptides was pre-screened for solubility in an aqueous, acidic milieu and a final panel of 44 peptides selected for testing in an in vitro MHC Class II binding assay.

Methods

[0121] The assay employed is a competitive MHC class II binding assay, wherein each peptide is analysed for its ability to displace a known control binder from each of the human MHC class II allotypes investigated. The allotypes and control peptides used in this study are shown in the table below.

Control Peptides used in the In Vitro Binding Assays

TABLE-US-00020 Allotype Control Peptide Sequence DRB1*0101 Influenza PKYVKQNTLKLAT haemagglutinin (SEQ ID NO: 1) 307-319 DRB1*0301 Myco. tuberculosis/ AKTIAYDEEARRGLE leprae hsp 65 2-16 (SEQ ID NO: 2) DRB1*0401 Influenza PKYVKQNTLKLAT haemagglutinin (SEQ ID NO: 1) 307-319 DRB1*0701 Influenza PKYVKQNTLKLAT haemagglutinin (SEQ ID NO: 1) 307-319 DRB1*1101 Influenza PKYVKQNTLKLAT haemagglutinin (SEQ ID NO: 1) 307-319 DRB1*1301 HLA-DQB1*0603 21-36 TERVRLVTRHIYNREE (SEQ ID NO: 3) DRB1*1501 Human myelin basic ENPVVHFFKNIVTPR protein 85-99 (SEQ ID NO: 4) DQB1*0602 Human Insulin B 1-15 FVNQHLCGSHLVEAL (SEQ ID NO: 5)

Each of the 44 HDM peptides (which are shown in Tables A and B) were analysed in the competition assay and screened for relative binding compared to the control peptide. Due to the nature of the competitive assay the data for each peptide is represented as a ratio of its own IC50 to that of the control peptide. Thus, a peptide that has an IC50 value that is parity to the control peptide has an identical binding affinity, while peptides with a ratio less than one have a higher affinity and those with a ratio greater than one have a lower affinity.

Results

[0122] Solubility in aqueous solution is an essential criterion for a peptide to be an effective therapeutic agent. Therefore, as a consequence of the solubility screen we will have eliminated very hydrophobic peptides with a high frequency of large hydrophobic amino acid residues in multiple binding registers. This is a characteristic of promiscuous HLA-DRB1* binders. The data from the binding assays is shown in Table 3B. The relative binding of each peptide is shown for each of the allotypes in the study. The data shows that 24 of the 44 peptides tested bound to one or more of the MHC Class II allotypes. A range of cross-reactivity is seen with 5 peptides binding only one allotype, 8 peptides binding two, 9 peptides binding three and two peptides binding four different MHC Class II allotypes (red). It would also be expected that such peptides would have the ability to bind similar allotypes that have not been tested through the homology of MHC structures. This can be seen in the cross-reactivity of peptides for DRB1*0101, *0401, *0701 and *1101 in several cases here. Also shown is the solubility status of the peptide at the highest concentrations in the aqueous solution of the binding assay. The value illustrates the lowest concentration at which an insoluble white precipitate is seen. There appears to be no significant nonspecific effect of the formation of precipitate in the assays. Several peptides that precipitate at high concentrations also bind to MHC class II; however, several also show no ability to compete with the control peptides. It is to be expected that peptides liable to form precipitates may exhibit high affinity and promiscuous binding due to the presence of many hydrophobic residues.

[0123] The % purity of the peptides is indicated in Table 3A. This is of significance as purities were seen to vary from 60-90%. This would have a considerable effect on the ability of a peptide to compete if it is relatively impure. For example, HDM23A and HDM32 show low affinity binding; however, they are of reduced purity (66.7% and 68.7% respectively) compared to other HDM peptides. Therefore, if purity is taken into consideration, they may in fact have an equivalent affinity to a peptide of a higher purity.

[0124] It can be seen that some MHC Class II allotypes bind to more peptides than others; this is probably to be expected as there is variability between the pocket positions in the different MHC class II binding grooves. There are however, also a number of well-characterised differences between the affinities of the various control peptides. Clearly a high affinity control peptide will be more difficult to displace by the competing HDM peptide resulting in the identification of fewer binding peptides. This can be illustrated by the data presented here. For example, the Influenza Haemagglutinin 307-319 control peptide, has varying affinity according to the allotype, where DRB1*0101>*0401>*0701>* 1101. This is reflected in the number of binders to each of the allotypes, where DRB1*0101 has the lowest number of binders (5) and DRB1*1101 has the highest(14). Furthermore, the binding assay for DRB1*1501 is very stringent due to the high affinity of Myelin Basic Protein 85-99 for this allotype. In the high stringency screen the Fel d 1 peptide EQVAQYKALPVVLENA (SEQ ID NO:6), that was tested in an earlier study, gave a ratio of 0.97 indicating that high affinity binders could be identified at this stringency.

[0125] In addition, to identify lower affinity binders, the assay was also carried out under less stringent conditions. All the Der p binding peptides were seen to have a high ratio when tested against this allotype, showing they were low affinity binders compared to the control peptide. The DQA1*0102/DQB1*0602 binding assay uses a peptide from the B-chain of human insulin which is of lower affinity compared to those used in the DR assays. This dictates that the DQ assay is very sensitive and tends to produce very low ratio values for the strongest binders to this MHC Class II allotype. This sensitivity also accounts for the relatively higher number of DQ binding peptides within the panel screened. Finally, on closer analysis, the peptides identified as ligands for the DRB1*0101,*0401, *0701 superfamily, are found to incorporate a motif that is characteristic of promiscuous binders to this family of allotypes where: P1=Y, F, W, L, I, V, or M (Large aromatic or hydrophobic residue), P6=S, T, C, A, P, V, I, M (small, non-charged residue) Out of the 16 peptides (e.g. HDM 21B RGKPFQLEAVFEANQNT SEQ ID NO: 26) identified as binders to all or a combination of these 3 allotypes, 14 (87.5%) contain this motif, which suggests that these are promiscuous binders with a range of affinities for the 1-4-7 allotypes.

Conclusions

[0126] A range of peptides have been shown to have the capacity to bind the MHC Class II allotypes and are considered to represent T cell epitopes. Thus the inventors were able to identify sequences comprising T cell epitopes which are close together in the overall protein sequence and therefore construct peptides which comprise overlapping epitopes. A number of such sequences will be apparent to the skilled person when considering Tables 1A and 1B. Specific illustrative examples include:

[0127] HDM01 (residues 112-124) and HDM02 (118-130). Providing a combination of these two sequences, the inventors devised a longer sequence spanning residues 112 to 130. In order to reduce dimer formation by this longer peptide, the cysteine at position 129 is replaced with serine to give new peptide HDM01A:

TABLE-US-00021 (SEQ ID NO: 7) IDLRQMRTVTPIRMQGGSG

(HDM01=underlined, HDM02=bold).

[0128] HDM34 (residues 74-88) and HDM35 (79-91). Providing a combination of these two sequences, the inventors devised a longer sequence spanning residues 72 to 89. Residues 72 and 73 were added, and residues 90 and 91 removed in order to improve solubility for the new peptide, HDM207:

TABLE-US-00022 (SEQ ID NO: 8) DMRNIQVRGLKQMKRVGD

(HDM34=underlined, HDM35=bold).

[0129] Evidence that these new peptides are suitable for tolerisation to house dust mite allergens is shown in Table 1C. Table 1C presents results from a cytokine release assay performed on four house dust mite allergic individuals for HDM01A compared to HDM01 and HDM02, and on three house dust mite allergic individuals for HDM34, HDM35 and HDM207.

[0130] Cytokine secretion profiles from PBMC's were analysed in response to the peptide stimulation using the above peptides. Supernatants from the cytokine release assay were tested for the presence of 2 cytokines, IFN-.gamma. and IL-13, using either an ELISA assay or a multiplex bead array assay.

[0131] A typical cytokine release assay requires 40.times.10.sup.6 PBMC's per subject. In more detail, 250 .mu.l of a 200 .mu.g/ml solution of the appropriate antigen or peptide concentration is distributed into the appropriate wells of 48 well plates. Plates are the incubated in a humidified 5% CO.sub.2 incubator at 37.degree. C. for a maximum of 4 hours. 250 .mu.l of a 5.times.10.sup.6 cell/ml PBMC suspension is then added to each well and the plates returned to the incubator for 5 days. Following stimulation, samples of culture supernatant are harvested for testing by ELISA or multiplex bead assay according to standard protocols.

[0132] As can be seen, the new peptides HDM01A and HDM207 give rise to significantly higher cytokine production in all patients tested than the original "single epitope" peptides from which they derive.

TABLE-US-00023 TABLE 1A Residues in parent % Solubility Precipitation SEQ Peptide Sequence molecule purity test in assay ID NO HDM01 IDLRQMRTVTPIR 112-124 79.2 YES None 9 HDM02 RTVTPIRMQGGCG 118-130 79.6 YES None 10 HDM03C RNQSLDLAEQELVDCASQH 149-167 60.1 YES None 11 HDM05 EYIQHNGVVQESY 179-191 77.5 YES None 12 HDM06 RYVAREQSCRRPN 193-205 79.7 YES None 13 HDM07 PNVNKIREALAQT 220-232 88.6 YES None 14 HDM08 NKIREALAQTHSA 223-235 87.6 YES None 15 HDM09A REALAQTHSAIAVI 226-239 69.6 YES 1000 .mu.M 16 (2.9 mg/ml) HDM11 IGIKDLDAFRHYD 240-252 77.6 YES None 17 HDM12 KDLDAFRHYDGRT 243-255 72.9 YES None 18 HDM13 RTIIQRDNGYQPNY 254-267 70.7 NO None 19 HDM16A RNSWDTNWGDNGYG 287-300 70.0 YES None 20 HDM17 NSVNVPSELDLRSLRT 105-120 74.5 YES None 21 HDM19 DQVDVKDCANHEIKK 18-32 81.4 YES None 22 HDM20 CIIHRGKPFQLEA 44-56 77.4 YES None 23 HDM21 KPFQLEAVFEANQNT 50-64 88.7 YES 200 .mu.M 24 (0.3 mg/ml) HDM21A KPFQLEAVFEANQNTK 50-65 90.1 YES 5000 .mu.M 25 (9.3 mg/ml) HDM21B RGKPFQLEAVFEANQNT 48-64 82.6 YES 1000 .mu.M 26 (1.98 mg/ml) HDM22A EAVFEANQNTKTAK 55-68 90.3 YES None 27 HDM23A DGLEVDVPGIDPNACH 76-88 66.7 YES None 28 HDM26A DGVLACAIATHAKIR 131-145 1000 .mu.M 29 (1.5 mg/ml) HDM27 AKIEIKASLDGLE 67-79 65.9 YES 1000 .mu.M 30 (1.4 mg/ml) HDM28 KAVDEAVAAIEKS 31-43 86.8 YES 1000 .mu.M 31 (1.3 mg/ml) HDM29 ETFDPMKVPDHSD 44-56 84.7 YES None 32 HDM29A ETFDPMKVPDHSDK 44-57 91.7 YES None 33 HDM29B KSETFDPMKVPDHSD 42-56 92.5 YES 1000 .mu.M 34 (1.7 mg/ml) HDM30 DKFERHIGIIDLK 56-68 81.4 YES 5000 .mu.M 35 (7.9 mg/ml) HDM31 IGIIDLKGELDMRN 62-75 1000 .mu.M 36 (1.8 mg/ml) HDM31A HIGIIDLKGELDMRN 61-75 66.4 YES 1000 .mu.M 37 (1.7 mg/ml) HDM32 IDLKGELDMRNIQ 65-77 68.7 YES 5000 .mu.M 38 (7.7 mg/ml) HDM32A IDLKGELDMRNIQVR 65-79 85.2 YES 5000 .mu.M 39 (9.0 mg/ml) HDM33 LDMRNIQVRGLKQ 71-83 70.3 YES None 40 HDM34 RNIQVRGLKQMKRVG 74-88 74.7 YES None 41 HDM35 RGLKQMKRVGDAN 79-91 84.0 YES None 42 HDM36 KRVGDANVKSEDG 85-97 82.9 YES None 43 HDM37 ANVKSEDGVVKAH 90-102 76.5 YES None 44 HDM39 DDVVSMEYDLAYK 109-121 84.9 NO* None 45 HDM39A HDDVVSMEYDLAYKL 108-121 80.9 YES 1000 .mu.M 46 (1.8 mg/ml) HDM40A VSMEYDLAYKLGDLH 112-124 66.9 YES 1000 .mu.M 47 (1.8 mg/ml) HDM48 TAIFQDTVRAEMTK 187-200 79.1 YES 1000 .mu.M 48 (1.6 mg/ml) HDM49 DTVRAEMTKVLAP 192-204 69.5 YES None 49 Peptides HDM01 to 116A are from Der p1; peptide HDM17 is from Der f1. Peptides HDM19 to 26A are from Der p2; peptide HDM37 is from Der f2. Peptides HDM 28 to 49 are from Der p 7. The sequence of Der p 1 from which the "residues in parent" positions are derived is the publically available sequence with NCBI Accession No. P08176. The corresponding sequences for Der p 2 and Der p 7 are NCBI Accession Nos. P49278 and P49273, respectively.

TABLE-US-00024 TABLE 1B DQA1* 0102 DRB1 DRB1* DRB1* DRB1* DRB1* DRB1* DRB1* DQB1* Peptide *0101 0301 0401 0701 1101 1301 1501 0602 HDM01 19.23 16 HDM02 80 0.03 HDM03C 0.16 HDM05 HDM06 30.36 0.86 HDM07 HDM08 HDM09A 0.49 21.15 200 HDM11 HDM12 HDM13 HDM16A HDM17 HDM19 HDM20 1.1 28 242.11 2.37 HDM21 92 11.15 11.73 HDM21A 200 52.17 10.27 HDM21B 13.5 0.78 4.1 HDM22A 328.6 80 HDM23A 347 0.76 HDM26A 42.3 16.28 0.61 HDM27 HDM28 HDM29 HDM29A HDM29B HDM30 6.2 HDM31 HDM31A HDM32A HDM33 46.51 41.5 263.16 HDM34 3.38 3.7 769.23 HDM35 1.26 HDM36 HDM37 HDM39 HDM39A 76.19 0.71 0.1 HDM40A 2.29 6 HDM48 211.26 15.71 13.57 HDM49 671.43 1.7 HDM50 HDM51 20.93 30.91

TABLE-US-00025 TABLE 1C (cytokine levels shown in pg/ml) Subject Cytokine HDM01 HDM02 HDM01A 1 Il-13 73 61 502 IFN-.gamma. 139 350 459 2 Il-13 47 11 82 IFN-.gamma. 63 58 166 3 Il-13 26 24 57 IFN-.gamma. 0 22 44 4 Il-13 81 37 135 IFN-.gamma. 31 0 44 HDM34 HDM35A HDM207 A Il-13 0 0 11 IFN-.gamma. 0 0 72 B Il-13 0 0 169 IFN-.gamma. 26 20 341 C Il-13 4 25 676 IFN-.gamma. 113 247 609

EXAMPLE 2

Grass Peptides

[0133] The Timothy Grass pollen allergen Phl p 5 Accession number 2003342A was analysed by methods analogous to those used in Example 1. A number of peptides sequences containing MHC Class II binding epitopes were identified. As above, the inventors were able to identify sequences comprising T cell epitopes which are close together in the overall protein sequence and therefore construct peptides which comprise overlapping epitopes.

[0134] A specific example is peptide Tim10B, which consists of residues 260 to 277 of Phl p5. This peptide was constructed by extending peptide Tim10C (residues 268 to 276 of Phl p5) to include a second, third and fourth T cell epitope (As confirmed in the further in silico analysis of Phl p 5 in Example 5). Production of IL13 in response to both peptides was measured as in Example 1. As shown in FIG. 1, Tim 10B demonstrates consistently greater cytokine production in the panel of subjects tested than the "single epitope" peptide Tim 10C.

TABLE-US-00026 Tim 10B 260 KYTVFETALKKAITAMSE 277 (SEQ ID NO: 50) Tim 10C 268 LKKAITAMS 276 (SEQ ID NO: 51)

EXAMPLE 3

[0135] Peptides Comprising Multiple Epitopes from House Dust Mite Allergens Der Pl

[0136] The peptides listed in this Example were identified as containing T cell epitopes by an in silico MHC binding analysis. The peptides identified have strong affinities for the seven most common human MHC Class II HLA-DRB1* allotypes (covering in total around 63% of the allotypes found in the average Caucasian population).

[0137] In order to identify additional binding peptides in the House dust mite allergen der p 1, the inventors used an in silico approach known as "peptide threading" using the commercially available EpiMatrix algorithm (EpiVax Inc.) This is a bioinformatic analysis of peptides from a sequence for the potential to be accommodated within the binding groove of MHC class II HLA-DR molecules. EpiMatrix is a matrix-based algorithm that ranks amino acid segments from any polypeptide sequence by estimated probability of binding to each of the selected MHC molecules. (De Groot et al., AIDS Research and Human Retroviruses 13:539-41 (1997)). The procedure for developing matrix motifs was published by Schafer et al, 16 Vaccine 1998 (1998). In this Example, binding potential for HLA DR1, DR2, DR3, DR4, DR7, DR8, DR11, DR13 and DR15 is assessed. Putative MHC ligands are selected by scoring each 9-mer frame in a protein sequence. This score is derived by comparing the sequence of the 9-mer to the matrix of amino acid sequences known to bind to each MHC allele. Retrospective studies have demonstrated that EpiMatrix accurately predicts published MHC ligands (Jesdale et al., in Vaccines '97 (Cold Spring Harbor Press, Cold Spring Harbor, N.Y., 1997)). Successful prediction of peptides which bind to multiple MHC molecules has also been confirmed. The tables shown below show Epivax data for consecutive 9-mers in specific regions of each of the above allergen proteins. The regions are identified by "Frame start" and "Frame stop" values, which refer to the amino acid positions in the published sequences of each protein (the protein concerned and the relevant public database accession number for its sequence is shown at the top of each table). Flanking amino acids, added to stabilize the cluster during in-vitro testing, are shown underlined. Epivax also analysed hydrophobicity of peptides containing epitopes. Scores of greater than 1 are considered to be unsuitable for administration and/or manufacture.

[0138] The "Z-score" under each HLA allele indicates the potential of a given 9-mer to bind to that HLA allele. All scores in the Top 5% (Z-Score>=1.64) are considered "Hits". "Hits" in each 9 mer scoring above 1.64 are considered to comprise T cell epitopes (summarised in the "Hits" column). Thus the inventors were able to identify sequences which are close together in the overall protein sequence and therefore construct peptides which comprise overlapping epitopes. Examples of such sequences are provided beneath the Table for the relevant section of each protein. Where such sequences comprise greater than two epitopes, it will be appreciated that any fragment of these sequences comprising at least two overlapping epitopes would also be suitable.

TABLE-US-00027 DER P 1: Accession No, P08176 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hit ID NO 51 LESVKYVQS 59 1.31 0 52 52 ESVKYVQSN 60 0 53 53 SVKYVQSNG 61 1.37 0 54 54 VKYVQSNGG 62 1.43 1.84 1.97 1.63 1.53 1.28 2.37 3 55 55 KYVQSNGGA 63 0 56 56 YVQSNGGAI 64 2.24 2.88 1.45 2.04 3 57 57 VQSNGGAIN 65 1.54 0 58 58 QSNGGAINH 66 0 59 Suitable sequence HDM_1_ME1 = VKYVQSNGGAI (SEQ ID NO: 60) (residues 54-64) [epitope 1 = bold, epitope 2 = underlined] DER P 1: Accession No. P08176 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 72 LDEFKNRFL 80 0 61 73 DEFKNRFLM 81 1.61 1.49 0 62 74 EFKNRFLMS 82 0 63 75 FKNRFLMSA 83 2.19 2.20 2.28 3 64 76 KNRFLMSAE 84 0 65 77 NRFLMSAEA 85 2.21 2.26 1.87 3 66 78 RFLMSAEAF 86 0 67 79 FLMSAEAFE 87 1.53 1.56 1.28 0 68 Suitable sequence HDM_1_ME3 = LRQMRTVTPIRMQGGCGS_ (SEQ ID NO: 81) (residues 114-131) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] DER P 1: Accession No. P08176 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 114 LRQMRTVTP 122 2.44 2.22 2.66 1.37 1.77 2.45 1.78 6 70 115 RQMRTVTPI 123 0 71 116 QMRTVTPIR 124 0 72 117 MRTVTPIRM 125 1.78 2.04 1.37 2.16 1.97 2.36 5 73 118 RTVTPIRMQ 126 0 74 119 TVTPIRMQG 127 1.28 0 75 120 VTPIRMQGG 128 0 76 121 TPIRMQGGC 129 0 77 122 PIRMQGGCG 130 1.29 0 78 123 IRMQGGCGS 131 2.85 2.26 1.36 1.98 2.22 1.65 5 79 124 RMQGGCGSC 132 0 80 Suitable sequence HDM_1_ME3 = LRQMRTVTPIRMQGGCGS_ (SEQ ID NO: 81) (residues 114-131) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] DER P 1: Accession No. P08176 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 144 AYLAYRNQS 152 1.95 1.39 1 82 145 YLAYRNQSL 153 1.95 1.52 1.81 1.81 3.13 4 83 146 LAYRNQSLD 154 2.22 1 84 147 AYRNQSLDL 155 1.42 1.79 1.67 2 85 148 YRNQSLDLA 156 1.52 1.80 1.87 1.69 1.36 3 86 149 RNQSLDLAE 157 0 87 Suitable sequence HDM_1_ME4 = A DLA (SEQ ID NO: 88) (residues 144-156) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background, epitope 5 = last 9 amino acids] DER P 1: Accession No. P08176 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 190 SYYRYVARE 198 0 89 191 YYRYVAREQ 199 1.96 1.51 1.41 2.67 2.08 1.38 1.49 3 90 192 YRYVAREQS 200 1.90 2.57 1.85 1.90 2.92 3.69 2.31 7 91 193 RYVAREQSC 201 0 92 194 YVAREQSCR 202 1.29 1.28 2.24 1.68 2 93 195 VAREQSCRR 203 0 94 196 AREQSCRRP 204 0 95 197 REQSCRRPN 205 0 96 198 EQSCRRPNA 206 2.03 1.29 1.71 2 97 199 QSCRRPNAQ 207 0 98 Suitable sequence HDM_1_ME5 = Y SCRRPNA (SEQ ID NO: 99) (residues 191-206) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background] DER P 1: Accession No. P08176 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 298 GYGYFAANI 306 0 100 299 YGYFAANID 307 1.44 2.74 1.65 2 101 300 GYFAANIDL 308 1.40 1.78 1.94 2 102 301 YFAANIDLM 309 1.55 1.53 0 103 302 FAANIDLMM 310 1.41 1.50 1.87 1.46 1.74 1.83 3 104 303 AANIDLMMI 311 0 105 304 ANIDLMMIE 312 0 106 Suitable sequence HDM_1_ME6 = YGYFAANIDLMM (SEQ ID NO: 107) (residues 299-310) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background]

EXAMPLE 4

Peptides Comprising Multiple Epitopes from Birch Pollen Allergens

[0139] The peptides listed in this Example were identified as in Example 3.

TABLE-US-00028 BET V 1: Accession No. 1FM4A Frame Frame Hydro- DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop phobicity Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 14 PAARMFKAF 22 .07 0 108 15 AARMFKAFI 23 1.00 1.41 1.86 1.33 1.91 2 109 16 ARMFKAFIL 24 1.22 2.26 1.99 1.68 3.25 4 110 17 RMFKAFILD 25 .14 0 111 Suitable sequence BET_1_ME1 = AARMFKAFIL (SEQ ID NO: 112) (residues 15-24) [epitope 1 = bold, epitope 2 = underlined] BET V 1: CAA04829.1 Frame Frame Hydro- DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop phobicity Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 2 VFNYEIGAT 10 .09 2.11 1 113 3 FNYEIGATS 11 -.12 2.27 2.09 1.46 2 114 4 NYEIGATSV 12 .03 0 115 5 YEIGATSVI 13 .92 2.11 1.91 1.87 1.77 1.69 5 116 6 EIGATSVIP 14 .19 0 117 7 IGATSVIPA 15 .32 1.90 1.42 1.45 1 118 8 GATSVIPAA 16 .25 0 119 Suitable sequence BET_1_ME2 = V VIPA (SEQ ID NO: 120) (residues 2-15) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background] BET V 1: Accession No. P43186 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 63 SPFKYVKER 71 -.86 -1.47 -1.35 -.95 -.31 -1.42 -.48 -1.14 0 121 64 PFKYVKERV 72 -.85 .85 -1.38 -.65 .85 -.16 1.15 .85 0 122 65 FKYVKERVD 73 .71 .71 .05 .62 2.34 1.79 1.15 .15 2 123 66 KYVKERVDE 74 -.77 .51 -1.53 -.65 2.29 .47 .86 -.47 1 124 67 YVKERVDEV 75 1.89 .79 2.27 1.72 .09 .42 -.83 -.09 3 125 68 VKERVDEVD 76 -1.55 -.39 -.95 -.52 1.50 -.80 .28 .19 0 126 69 KERVDEVDH 77 -.75 -.15 .00 -.26 .20 .99 -.28 -.35 0 127 Suitable sequence BET_1_ME3 = F V (SEQ ID NO: 314) (residues 65-75) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] BET V 1: Accession No. P43186 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 79 NFKYSYSMI 87 -.16 -.59 -1.04 -.25 -.18 -1.28 -.47 1.09 0 128 80 FKYSYSMIE 88 .81 .41 1.87 1.30 1.46 1.32 -.15 1.43 1 129 81 KYSYSMIEG 89 -1.13 -.38 -.95 -1.37 .65 -1.20 .13 .41 0 130 82 YSYSMIEGG 90 .26 .69 1.34 1.35 .56 .82 -.05 -.51 0 131 83 SYSMIEGGA 91 .21 .42 -.24 -.94 .28 1.51 -1.01 .48 0 132 84 YSMIEGGAL 92 .11 .67 .28 1.26 -.63 1.93 3 133 85 SMIEGGALG 93 1.26 .23 .75 -1.29 .23 .14 -.86 -.68 0 134 Suitable sequence BET_1_ME4 = FKYSYSMIEGGAL (SEQ ID NO: 135) (residues 80-92) [epitope 1 = bold, epitope 2 = underlined] BET V 1: Accession No. P43177 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 143 ALLRAVESY 151 -.81 .35 -.34 .29 -.06 -.84 1.00 -.32 0 136 144 LLRAVESYL 152 1.26 1.52 .46 1.47 .78 .46 .90 1.73 1 137 145 LRAVESYLL 153 1.91 1.66 1.36 1.73 1.51 6 138 146 RAVESYLLA 154 .65 -.01 .83 -.65 -.88 -.23 -.76 .09 0 139 147 AVESYLLAH 155 -1.28 -.03 .05 -.69 -.71 .28 -.36 -.38 0 140 148 VESYLLAHS 156 -.53 .94 -.18 -2.13 1.08 .59 1.28 1.06 0 141 149 ESYLLAHSD 157 .75 -1.02 .25 .44 1.28 .13 -.18 -1.41 0 142 150 SYLLAHSDA 158 .44 .48 .81 -.78 .66 1.33 .17 .28 0 143 151 YLLAHSDAY 159 1.61 1.73 1.83 1.48 .14 .13 .88 .83 2 144 Suitable sequence BET_1_ME5 = L AHSDAY (SEQ ID NO: 145) (residues 144-151) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic]

EXAMPLE 5

Peptides Comprising Multiple Epitopes from Timothy Grass Pollen Allergens

[0140] The peptides listed in this Example were identified as in Example 3.

TABLE-US-00029 Phl P 1: Accession No. P43213 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 142 GDEQKLRSA 150 -.62 -.54 -1.14 -2.14 -1.22 -.15 .20 -1.31 0 146 143 DEQKLRSAG 151 -.71 .34 -1.29 -1.40 1.88 .74 .42 -.25 1 147 144 EQKLRSAGE 152 1.04 .00 1.00 -.03 1.42 .61 -.03 -.85 0 148 145 QKLRSAGEL 153 .85 .25 -.69 2.11 1.23 .54 .74 2.14 2 149 146 KLRSAGELE 154 -.07 -.03 -.17 .56 -.13 -.63 -.74 -.84 0 150 147 LRSAGELEL 155 1.80 1.91 1.14 2.02 1.17 .86 1.89 2.40 5 151 148 RSAGELELQ 156 -1.14 .12 -.35 -.95 -.18 -.28 -1.20 -.57 0 152 Suitable sequence Phl_1_ME1 = DE EL (SEQ ID NO: 153) (residues 143-155) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] Phl P 1: Accession No. P43213 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 181 NYLALLVKY 189 .08 1.23 -.26 -.23 -.14 -.20 .89 .20 0 154 182 YLALLVKYV 190 2.74 -.32 1.97 2.80 1.32 1.50 .23 .48 3 155 183 LALLVKYVN 191 1.27 1.27 -.08 -.19 2.09 1.78 .99 .97 2 156 184 ALLVKYVNG 192 .65 .48 .31 .38 .43 .57 .33 .98 0 157 Suitable sequence Phl_1_ME2 = YLALLVKYVN (SEQ ID NO: 158) (residues 182-191) [epitope 1 = bold, epitope 2 = underlined] Phl P 1: Accession No. P43213 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 215 SWGAIWRID 223 -.68 -1.26 -1.15 -.21 .08 -1.12 -.91 -1.80 0 159 216 WGAIWRIDT 224 1.95 1.28 1.03 2.16 1.37 1.93 .83 1.35 3 160 217 GAIWRIDTP 225 -1.73 -1.00 .04 -.45 -1.91 -.96 -.46 -1.40 0 161 218 AIWRIDTPD 226 -1.52 -1.01 -1.25 -1.34 .35 -1.57 -.66 .32 0 162 219 IWRIDTPDK 227 .79 .96 1.81 .21 .13 1.44 .52 .69 1 163 220 WRIDTPDKL 228 1.97 2.87 2.36 2.86 1.13 .63 .28 1.09 4 164 221 RIDTPDKLT 229 -.75 -2.52 -1.02 -.36 -1.45 -1.27 -1.42 -.12 0 165 Suitable sequence Phl_1_ME3 = WGA L (SEQ ID NO: 166) (residues 216-228) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] Phl P 1: Accession No. P43213 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 142 GDEQKLRSA 150 -.62 -.54 -1.14 -2.14 -1.22 -.15 .20 -1.31 0 167 143 DEQKLRSAG 151 -.71 .34 -1.29 -1.40 1.88 .74 .42 -.25 1 168 144 EQKLRSAGE 152 1.04 .00 1.00 -.03 1.42 .61 -.03 -.85 0 169 145 QKLRSAGEL 153 .85 .25 -.69 2.11 1.23 .54 .74 2.14 2 170 146 KLRSAGELE 154 -.07 -.03 -.17 .56 -.13 -.63 -.74 -.84 0 171 147 LRSAGELEL 155 1.80 1.91 1.14 2.02 1.17 .86 1.89 2.40 5 172 148 RSAGELELQ 156 -1.14 .12 -.35 -.95 -.18 -.28 -1.20 -.57 0 173 Suitable sequence Phl_1_ME4 = (residues 143-155) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] Phl P 5: Accession No. 2003342A Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits NO 69 KINAGFKAA 77 .34 -.85 .04 -.03 -.48 -.24 -.55 -.41 0 174 70 INAGFKAAL 78 1.39 2.68 -.06 -.20 1.06 1.08 1.32 1.38 1 175 71 NAGFKAALA 79 1.10 -.02 .67 -1.09 .41 .72 .23 .50 0 176 72 AGFKAALAA 80 .67 .42 .52 -.36 .93 .68 1.11 1.15 0 177 73 GFKAALAAA 81 .26 .83 .22 -1.54 .06 .51 .51 -.07 0 178 74 FKAALAAAA 82 3.20 2.30 2.70 1.16 1.80 2.26 1.93 1.53 6 179 75 KAALAAAAG 83 1.74 .29 1.03 -.47 1.34 1.29 .25 -.64 1 180 76 AALAAAAGV 84 1.74 .84 .69 .63 .24 .26 .52 .51 1 181 77 ALAAAAGVQ 85 1.05 .43 .84 1.31 1.09 1.08 -.09 1.39 0 182 Suitable sequence Phl_5_ME1 = INAG GV (SEQ ID NO: 183) (residues 70-84) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background] Phl P 5: Accession No. 2003342A Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 89 KYRTFVATF 97 .31 -.73 .91 .36 -.58 -.03 -.25 -.91 0 184 90 YRTFVATFG 98 2.56 1.50 2.20 1.06 1.84 1.45 1.32 2.45 4 185 91 RTFVATFGA 99 1.13 .96 1.02 .76 .59 1.08 1.23 1.74 1 186 92 TFVATFGAA 100 -.30 -.25 -.40 -.34 -.54 -.03 -.74 .03 0 315 93 FVATFGAAS 101 2.41 .66 2.30 .87 1.30 1.96 1.09 1.34 3 187 94 VATFGAASN 102 1.00 .22 .20 -.81 .98 .25 .45 1.07 0 188 Suitable sequence Phl_5_ME2 = Y AS (SEQ ID NO: 189) (residues 90-101) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] Phl P 5: Accession No. 2003342A Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 126 TSKLDAAYK 134 .83 -.45 .60 -.78 .26 .86 -.47 -1.50 0 190 127 SKLDAAYKL 135 1.53 2.11 1.00 1.99 .61 .03 -.16 1.07 2 191 128 KLDAAYKLA 136 .44 -1.45 -.32 -.26 -1.06 -.83 -1.13 -.32 0 192 129 LDAAYKLAY 137 .53 2.43 .00 -.42 .69 .59 2.39 1.24 2 193 130 DAAYKLAYK 138 -1.58 -.35 -1.07 -2.56 .28 -.30 .03 -.49 0 194 131 AAYKLAYKT 139 .54 -.12 -.68 -.01 .70 .09 .05 .80 0 195 132 AYKLAYKTA 140 1.09 -.95 .16 .08 -.27 .33 -.38 -.04 0 196 133 YKLAYKTAE 141 1.65 2.54 1.18 .69 2.43 1.44 1.79 1.30 4 197 134 KLAYKTAEG 142 .38 .66 .85 -1.04 1.73 .49 1.01 .72 1 198 135 LAYKTAEGA 143 .64 1.05 .61 .12 1.26 .93 1.35 .61 0 199 Suitable sequence Phl_5_ME3 = SK KTAEG (SEQ ID NO: 200) (residues 127-142) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background] Phl P 5: Accession No. 2003342A Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 192 KVDAAFKVA 200 .00 -1.20 -.30 -.37 -.82 -.58 -.89 -.73 0 201 193 VDAAFKVAA 201 .90 2.21 .46 -.23 .91 1.28 1.84 1.53 2 202 194 DAAFKVAAT 202 .48 -.86 .42 -.65 -.18 -.26 -.59 .03 0 203 195 AAFKVAATA 203 .70 .50 .26 -1.24 1.02 .90 .86 .09 0 204 196 AFKVAATAA 204 1.13 .81 .68 -.03 -.78 .50 .28 1.14 0 205 197 FKVAATAAN 205 2.18 1.37 2.22 .91 1.95 1.38 1.03 .89 3 206 198 KVAATAANA 206 2.23 1.24 1.72 .20 .84 1.29 .91 .57 2 207 199 VAATAANAA 207 1.63 1.24 1.78 1.50 .63 .94 1.23 2.07 2 208 200 AATAANAAP 208 .33 .10 .73 -1.15 -.38 -.33 -.20 -.12 0 209 Suitable sequence Phl_5_ME4 = VDAAFKVAATAANAA (SEQ ID NO: 210) (residues 193-207) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background] Phl P 5: Accession as 2003342A Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 234 SYKFIPALE 242 .10 -.05 -.16 -1.19 1.21 -.12 .19 -.10 0 211 235 YKFIPALEA 243 3.30 1.48 3.23 2.19 1.37 2.79 1.24 2.12 5 212 236 KFIPALEAA 244 -1.07 -.16 -.36 -.59 -.58 -.16 .31 -.52 0 213 237 FIPALEAAV 245 1.33 1.18 .76 .60 .94 .96 .84 .47 0 214 238 IPALEAAVK 246 1.26 .59 1.04 -.36 .69 1.29 .54 -.55 0 215 239 PALEAAVKQ 247 1.37 .40 1.65 .90 .74 .92 -.70 .20 1 216 240 ALEAAVKQA 248 .50 -.89 .43 -.03 -.94 -.71 -.58 -.17 0 217 241 LEAAVKQAY 249 .95 2.96 .15 -.19 1.07 .99 1.71 1.41 2 218 242 EAAVKQAYA 250 .83 .63 .22 -.67 .51 1.62 .47 -.66 0 219 Suitable sequence Phl_5_ME5 = YKFIPALEAAVKQAY (SEQ ID NO: 220) (residues 235-249) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic] Phl P 5: Accession No. 2003342A Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ Start Sequence Stop Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits ID NO 260 KYTVFETAL 268 .18 .07 -.69 .38 -.89 -.24 -.44 .55 0 221 261 YTVFETALK 269 1.27 .76 2.24 .19 1.77 1.87 .98 .70 3 222 262 TVFETALKK 270 1.34 .66 1.84 .52 .44 .87 -.11 .09 1 223 263 VFETALKKA 271 -.26 -.71 -.35 -.32 -.39 .18 .33 .53 0 224 264 FETALKKAI 272 1.66 1.28 .09 1.25 1.50 1.16 1.52 1.32 1 225 265 ETALKKAIT 273 1.19 .67 .08 -.69 1.38 1.82 .62 -.43 1 226 266 TALKKAITA 274 .51 -.01 .23 -.09 .89 .16 .48 .62 0 227 267 ALKKAITAM 275 -.55 .17 -.37 -.50 -.39 -.70 .15 .32 0 228 268 LKKAITAMS 276 2.13 2.14 2.85 .58 1.67 2.00 1.77 1.25 6 229 269 KKAITAMSE 277 .70 -.73 .82 -.09 .93 .99 -1.11 .57 0 230 Suitable sequence Phl_5_ME6 = YTVFETALKKAITAMS (SEQ ID NO: 231) (residues 261-276) [epitope 1 = bold, epitope 2 = underlined, epitope 3 = italic, epitope 4 = grey background, epitope 5 = last 9 amino acids]

EXAMPLE 6

Peptides Comprising Multiple Epitopes from Alternaria Allergens

[0141] The peptides listed in this Example were identified as in Example 3.

TABLE-US-00030 ALT A 1: Accession No. AAD00097 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ ID Start Sequence Stop Hydrophobicity Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits NO 40 QLLMLSAKR 48 .06 1.52 0 232 41 LLMLSAKRM 49 .87 2.83 1.44 2.17 1.46 1.71 1.47 1.33 3 233 42 LMLSAKRMK 50 .01 1.62 2.04 1.49 1 234 43 MLSAKRMKV 51 .06 1.29 1.49 1.65 1.83 1.28 2.34 3 235 44 LSAKRMKVA 52 .04 0 236 45 SAKRMKVAF 53 -.07 0 237 46 AKRMKVAFK 54 -.41 1.67 1.38 1 238 47 KRMKVAFKL 55 -.19 1.81 1.79 1.81 1.37 1.96 4 239 48 RMKVAFKLD 56 -.14 0 240 49 MKVAFKLDI 57 .86 1.82 2.87 1.74 1.49 2.82 2.60 5 241 50 KVAFKLDIE 58 .05 0 242 ##STR00001## ##STR00002## Sequences ALT_1_ME1 and ALT_1_ME2 may also be combined to create ALT_1_ME3 = LLMLSAKRMKVAFKLDI (SEQ ID NO: 245) containing 6 epitopes 77 GFKRCLQFT 85 -.03 0 246 78 FKRCLQFTL 86 .34 1.63 1.84 2.35 1.96 3 247 79 KRCLQFTLY 87 -.11 0 248 80 RCLQFTLYR 88 -.18 1.31 0 249 81 CLQFTLYRP 89 .14 0 250 82 LQFTLYRPR 90 -.63 1.31 1.73 1 251 83 QFTLYRPRD 91 -1.44 2.03 1 252 84 FTLYRPRDL 92 -.63 1.92 1.65 1.57 1.92 1.97 4 253 85 TLYRPRDLL 93 -.52 0 254 86 LYRPRDLLS 94 -.53 1.28 1.71 1 255 87 YRPRDLLSL 95 -.53 1.37 2.34 2.46 1.58 1.93 2.44 4 256 88 RPRDLLSLL 96 .01 0 257 ##STR00003## ##STR00004## Sequences ALT_1_ME4 and ALT_1_ME5 may also be combined to create ALT_1_ME6 = FKRCLQFTLYRPRDLLSL (SEQ ID NO: 260)(residues 78-95)containing 6 epitopes ALT A 2: Accession No. AAM90320 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ ID Start Sequence Stop Hydrophobicity Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits NO 53 TYYNSLGFN 61 -.12 0 261 54 YYNSLGFNI 62 .03 2.47 2.66 1.94 3 262 55 YNSLGFNIK 63 -.26 1.48 0 263 56 NSLGFNIKA 64 .09 0 264 57 SLGFNIKAT 65 .40 0 265 58 LGFNIKATN 66 .10 1.72 2.04 1.82 1.62 3 266 59 GFNIKATNG 67 -.37 0 267 60 FNIKATNGG 68 -.37 1.58 1.92 2.97 1.50 1.48 1.55 2 268 61 NIKATNGGT 69 -.76 0 269 62 IKATNGGTL 70 .06 1.96 2.71 2.94 3 270 63 KATNGGTLD 71 -.18 0 271 ##STR00005## 115 DITYVATAT 123 .13 0 273 116 ITYVATATL 124 1.41 2.04 1.81 1.54 1.65 1.73 1.62 1.59 4 274 117 TYVATATLP 125 .73 0 275 118 YVATATLPN 126 .42 2.17 2.84 2.45 2.11 1.74 1.92 6 276 119 VATATLPNY 127 .42 2.10 1.87 2 277 120 ATATLPNYC 128 .23 0 278 ##STR00006## 146 AYITLVTLP 154 .33 0 280 147 YITLVTLPK 155 .90 1.80 2.79 1.47 1.67 2.15 4 281 148 ITLVTLPKS 156 .96 1.70 2.21 1.63 1.66 3 282 149 TLVTLPKSS 157 .08 0 283 ##STR00007## ALT A 6: Accession No. Q9HDT3 Frame Frame DRB1*0101 DRB1*0301 DRB1*0401 DRB1*0701 DRB1*0801 DRB1*1101 DRB1*1301 DRB1*1501 SEQ ID Start Sequence Stop Hydrophobicity Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Z-Score Hits NO 188 EVYQKLKAL 196 -.06 0 285 189 VYQKLKALA 197 .31 1.90 2.13 2.02 2.21 4 286 190 YQKLKALAK 198 -.59 2.57 2.63 1.84 1.92 2.40 5 287 191 QKLKALAKK 199 -.88 0 288 192 KLKALAKKT 200 -.57 1.74 1.47 1 289 193 LKALAKKTY 201 -.28 1.49 1.97 1.69 1.87 2.45 4 290 194 KALAKKTYG 202 -.16 1.44 0 291 ##STR00008## 236 GYTGKIKIA 244 .00 0 293 237 YTGKIKIAM 245 .28 1.57 2.68 1.60 2.02 2 294 238 TGKIKIAMD 246 .03 0 295 239 GKIKIAMDV 247 .58 1.40 1.65 1 296 240 KIKIAMDVA 248 .82 0 297 241 IKIAMDVAS 249 1.17 1.56 1.88 2.15 1.39 1.52 2.28 3 298 242 KIAMDVASS 250 .58 1.53 1.92 1.63 1 299 243 IAMDVASSE 251 .62 2.53 1.54 1 300 244 AMDVASSEF 252 .09 0 301 ##STR00009## 364 AFGAGWGVM 372 .25 0 303 365 FGAGWGVMV 373 1.42 2.11 1.55 1.90 2 304 366 GAGWGVMVS 374 1.02 1.47 0 305 367 AGWGVMVSH 375 .71 0 306 368 GWGVMVSHR 376 .01 0 307 369 WGVMVSHRS 377 -.03 2.54 3.16 1.50 1.56 2.57 3 308 370 GVMVSHRSG 378 .02 1.44 1.97 1.59 1 309 371 VMVSHRSGE 379 -.32 1.85 1 310 372 MVSHRSGET 380 -.87 2.20 1.65 2 311 373 VSHRSGETE 381 -.31 0 312 ##STR00010##

Sequence CWU 1

1

420113PRTInfluenza virus 1Pro Lys Tyr Val Lys Gln Asn Thr Leu Lys Leu Ala Thr 1 5 10 215PRTMycobacterium tuberculosis 2Ala Lys Thr Ile Ala Tyr Asp Glu Glu Ala Arg Arg Gly Leu Glu 1 5 10 15 316PRTHomo sapiens 3Thr Glu Arg Val Arg Leu Val Thr Arg His Ile Tyr Asn Arg Glu Glu 1 5 10 15 415PRTHomo sapiens 4Glu Asn Pro Val Val His Phe Phe Lys Asn Ile Val Thr Pro Arg 1 5 10 15 515PRTHomo sapiens 5Phe Val Asn Gln His Leu Cys Gly Ser His Leu Val Glu Ala Leu 1 5 10 15 616PRTFelis catus 6Glu Gln Val Ala Gln Tyr Lys Ala Leu Pro Val Val Leu Glu Asn Ala 1 5 10 15 719PRTArtificial sequenceHDM01A synthetic peptide 7Ile Asp Leu Arg Gln Met Arg Thr Val Thr Pro Ile Arg Met Gln Gly 1 5 10 15 Gly Ser Gly 818PRTArtificial sequenceHDM207 synthetic peptide 8Asp Met Arg Asn Ile Gln Val Arg Gly Leu Lys Gln Met Lys Arg Val 1 5 10 15 Gly Asp 913PRTDermatophagoides pteronyssinus 9Ile Asp Leu Arg Gln Met Arg Thr Val Thr Pro Ile Arg 1 5 10 1013PRTDermatophagoides pteronyssinus 10Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly Cys Gly 1 5 10 1119PRTDermatophagoides pteronyssinus 11Arg Asn Gln Ser Leu Asp Leu Ala Glu Gln Glu Leu Val Asp Cys Ala 1 5 10 15 Ser Gln His 1213PRTDermatophagoides pteronyssinus 12Glu Tyr Ile Gln His Asn Gly Val Val Gln Glu Ser Tyr 1 5 10 1313PRTDermatophagoides pteronyssinus 13Arg Tyr Val Ala Arg Glu Gln Ser Cys Arg Arg Pro Asn 1 5 10 1413PRTDermatophagoides pteronyssinus 14Pro Asn Val Asn Lys Ile Arg Glu Ala Leu Ala Gln Thr 1 5 10 1513PRTDermatophagoides pteronyssinus 15Asn Lys Ile Arg Glu Ala Leu Ala Gln Thr His Ser Ala 1 5 10 1614PRTDermatophagoides pteronyssinus 16Arg Glu Ala Leu Ala Gln Thr His Ser Ala Ile Ala Val Ile 1 5 10 1713PRTDermatophagoides pteronyssinus 17Ile Gly Ile Lys Asp Leu Asp Ala Phe Arg His Tyr Asp 1 5 10 1813PRTDermatophagoides pteronyssinus 18Lys Asp Leu Asp Ala Phe Arg His Tyr Asp Gly Arg Thr 1 5 10 1914PRTDermatophagoides pteronyssinus 19Arg Thr Ile Ile Gln Arg Asp Asn Gly Tyr Gln Pro Asn Tyr 1 5 10 2014PRTDermatophagoides pteronyssinus 20Arg Asn Ser Trp Asp Thr Asn Trp Gly Asp Asn Gly Tyr Gly 1 5 10 2116PRTDermatophagoides farinae 21Asn Ser Val Asn Val Pro Ser Glu Leu Asp Leu Arg Ser Leu Arg Thr 1 5 10 15 2215PRTDermatophagoides pteronyssinus 22Asp Gln Val Asp Val Lys Asp Cys Ala Asn His Glu Ile Lys Lys 1 5 10 15 2313PRTDermatophagoides pteronyssinus 23Cys Ile Ile His Arg Gly Lys Pro Phe Gln Leu Glu Ala 1 5 10 2415PRTDermatophagoides pteronyssinus 24Lys Pro Phe Gln Leu Glu Ala Val Phe Glu Ala Asn Gln Asn Thr 1 5 10 15 2516PRTDermatophagoides pteronyssinus 25Lys Pro Phe Gln Leu Glu Ala Val Phe Glu Ala Asn Gln Asn Thr Lys 1 5 10 15 2617PRTDermatophagoides pteronyssinus 26Arg Gly Lys Pro Phe Gln Leu Glu Ala Val Phe Glu Ala Asn Gln Asn 1 5 10 15 Thr 2714PRTDermatophagoides pteronyssinus 27Glu Ala Val Phe Glu Ala Asn Gln Asn Thr Lys Thr Ala Lys 1 5 10 2816PRTDermatophagoides pteronyssinus 28Asp Gly Leu Glu Val Asp Val Pro Gly Ile Asp Pro Asn Ala Cys His 1 5 10 15 2915PRTDermatophagoides pteronyssinus 29Asp Gly Val Leu Ala Cys Ala Ile Ala Thr His Ala Lys Ile Arg 1 5 10 15 3013PRTDermatophagoides pteronyssinus 30Ala Lys Ile Glu Ile Lys Ala Ser Leu Asp Gly Leu Glu 1 5 10 3113PRTDermatophagoides pteronyssinus 31Lys Ala Val Asp Glu Ala Val Ala Ala Ile Glu Lys Ser 1 5 10 3213PRTDermatophagoides pteronyssinus 32Glu Thr Phe Asp Pro Met Lys Val Pro Asp His Ser Asp 1 5 10 3314PRTDermatophagoides pteronyssinus 33Glu Thr Phe Asp Pro Met Lys Val Pro Asp His Ser Asp Lys 1 5 10 3415PRTDermatophagoides pteronyssinus 34Lys Ser Glu Thr Phe Asp Pro Met Lys Val Pro Asp His Ser Asp 1 5 10 15 3513PRTDermatophagoides pteronyssinus 35Asp Lys Phe Glu Arg His Ile Gly Ile Ile Asp Leu Lys 1 5 10 3614PRTDermatophagoides pteronyssinus 36Ile Gly Ile Ile Asp Leu Lys Gly Glu Leu Asp Met Arg Asn 1 5 10 3715PRTDermatophagoides pteronyssinus 37His Ile Gly Ile Ile Asp Leu Lys Gly Glu Leu Asp Met Arg Asn 1 5 10 15 3813PRTDermatophagoides pteronyssinus 38Ile Asp Leu Lys Gly Glu Leu Asp Met Arg Asn Ile Gln 1 5 10 3915PRTDermatophagoides pteronyssinus 39Ile Asp Leu Lys Gly Glu Leu Asp Met Arg Asn Ile Gln Val Arg 1 5 10 15 4013PRTDermatophagoides pteronyssinus 40Leu Asp Met Arg Asn Ile Gln Val Arg Gly Leu Lys Gln 1 5 10 4115PRTDermatophagoides pteronyssinus 41Arg Asn Ile Gln Val Arg Gly Leu Lys Gln Met Lys Arg Val Gly 1 5 10 15 4213PRTDermatophagoides pteronyssinus 42Arg Gly Leu Lys Gln Met Lys Arg Val Gly Asp Ala Asn 1 5 10 4313PRTDermatophagoides pteronyssinus 43Lys Arg Val Gly Asp Ala Asn Val Lys Ser Glu Asp Gly 1 5 10 4413PRTDermatophagoides farinae 44Ala Asn Val Lys Ser Glu Asp Gly Val Val Lys Ala His 1 5 10 4513PRTDermatophagoides pteronyssinus 45Asp Asp Val Val Ser Met Glu Tyr Asp Leu Ala Tyr Lys 1 5 10 4615PRTDermatophagoides pteronyssinus 46His Asp Asp Val Val Ser Met Glu Tyr Asp Leu Ala Tyr Lys Leu 1 5 10 15 4715PRTDermatophagoides pteronyssinus 47Val Ser Met Glu Tyr Asp Leu Ala Tyr Lys Leu Gly Asp Leu His 1 5 10 15 4814PRTDermatophagoides pteronyssinus 48Thr Ala Ile Phe Gln Asp Thr Val Arg Ala Glu Met Thr Lys 1 5 10 4913PRTDermatophagoides pteronyssinus 49Asp Thr Val Arg Ala Glu Met Thr Lys Val Leu Ala Pro 1 5 10 5018PRTPhleum pratense 50Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile Thr Ala Met 1 5 10 15 Ser Glu 519PRTPhleum pratense 51Leu Lys Lys Ala Ile Thr Ala Met Ser 1 5 529PRTDermatophagoides pteronyssinus 52Leu Glu Ser Val Lys Tyr Val Gln Ser 1 5 539PRTDermatophagoides pteronyssinus 53Glu Ser Val Lys Tyr Val Gln Ser Asn 1 5 549PRTDermatophagoides pteronyssinus 54Ser Val Lys Tyr Val Gln Ser Asn Gly 1 5 559PRTDermatophagoides pteronyssinus 55Val Lys Tyr Val Gln Ser Asn Gly Gly 1 5 569PRTDermatophagoides pteronyssinus 56Lys Tyr Val Gln Ser Asn Gly Gly Ala 1 5 579PRTDermatophagoides pteronyssinus 57Tyr Val Gln Ser Asn Gly Gly Ala Ile 1 5 589PRTDermatophagoides pteronyssinus 58Val Gln Ser Asn Gly Gly Ala Ile Asn 1 5 599PRTDermatophagoides pteronyssinus 59Gln Ser Asn Gly Gly Ala Ile Asn His 1 5 6011PRTDermatophagoides pteronyssinus 60Val Lys Tyr Val Gln Ser Asn Gly Gly Ala Ile 1 5 10 619PRTDermatophagoides pteronyssinus 61Leu Asp Glu Phe Lys Asn Arg Phe Leu 1 5 629PRTDermatophagoides pteronyssinus 62Asp Glu Phe Lys Asn Arg Phe Leu Met 1 5 639PRTDermatophagoides pteronyssinus 63Glu Phe Lys Asn Arg Phe Leu Met Ser 1 5 649PRTDermatophagoides pteronyssinus 64Phe Lys Asn Arg Phe Leu Met Ser Ala 1 5 659PRTDermatophagoides pteronyssinus 65Lys Asn Arg Phe Leu Met Ser Ala Glu 1 5 669PRTDermatophagoides pteronyssinus 66Asn Arg Phe Leu Met Ser Ala Glu Ala 1 5 679PRTDermatophagoides pteronyssinus 67Arg Phe Leu Met Ser Ala Glu Ala Phe 1 5 689PRTDermatophagoides pteronyssinus 68Phe Leu Met Ser Ala Glu Ala Phe Glu 1 5 6911PRTDermatophagoides pteronyssinus 69Phe Lys Asn Arg Phe Leu Met Ser Ala Glu Ala 1 5 10 709PRTDermatophagoides pteronyssinus 70Leu Arg Gln Met Arg Thr Val Thr Pro 1 5 719PRTDermatophagoides pteronyssinus 71Arg Gln Met Arg Thr Val Thr Pro Ile 1 5 729PRTDermatophagoides pteronyssinus 72Gln Met Arg Thr Val Thr Pro Ile Arg 1 5 739PRTDermatophagoides pteronyssinus 73Met Arg Thr Val Thr Pro Ile Arg Met 1 5 749PRTDermatophagoides pteronyssinus 74Arg Thr Val Thr Pro Ile Arg Met Gln 1 5 759PRTDermatophagoides pteronyssinus 75Thr Val Thr Pro Ile Arg Met Gln Gly 1 5 769PRTDermatophagoides pteronyssinus 76Val Thr Pro Ile Arg Met Gln Gly Gly 1 5 779PRTDermatophagoides pteronyssinus 77Thr Pro Ile Arg Met Gln Gly Gly Cys 1 5 789PRTDermatophagoides pteronyssinus 78Pro Ile Arg Met Gln Gly Gly Cys Gly 1 5 799PRTDermatophagoides pteronyssinus 79Ile Arg Met Gln Gly Gly Cys Gly Ser 1 5 809PRTDermatophagoides pteronyssinus 80Arg Met Gln Gly Gly Cys Gly Ser Cys 1 5 8118PRTDermatophagoides pteronyssinus 81Leu Arg Gln Met Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly Cys 1 5 10 15 Gly Ser 829PRTDermatophagoides pteronyssinus 82Ala Tyr Leu Ala Tyr Arg Asn Gln Ser 1 5 839PRTDermatophagoides pteronyssinus 83Tyr Leu Ala Tyr Arg Asn Gln Ser Leu 1 5 849PRTDermatophagoides pteronyssinus 84Leu Ala Tyr Arg Asn Gln Ser Leu Asp 1 5 859PRTDermatophagoides pteronyssinus 85Ala Tyr Arg Asn Gln Ser Leu Asp Leu 1 5 869PRTDermatophagoides pteronyssinus 86Tyr Arg Asn Gln Ser Leu Asp Leu Ala 1 5 879PRTDermatophagoides pteronyssinus 87Arg Asn Gln Ser Leu Asp Leu Ala Glu 1 5 8813PRTDermatophagoides pteronyssinus 88Ala Tyr Leu Ala Tyr Arg Asn Gln Ser Leu Asp Leu Ala 1 5 10 899PRTDermatophagoides pteronyssinus 89Ser Tyr Tyr Arg Tyr Val Ala Arg Glu 1 5 909PRTDermatophagoides pteronyssinus 90Tyr Tyr Arg Tyr Val Ala Arg Glu Gln 1 5 919PRTDermatophagoides pteronyssinus 91Tyr Arg Tyr Val Ala Arg Glu Gln Ser 1 5 929PRTDermatophagoides pteronyssinus 92Arg Tyr Val Ala Arg Glu Gln Ser Cys 1 5 939PRTDermatophagoides pteronyssinus 93Tyr Val Ala Arg Glu Gln Ser Cys Arg 1 5 949PRTDermatophagoides pteronyssinus 94Val Ala Arg Glu Gln Ser Cys Arg Arg 1 5 959PRTDermatophagoides pteronyssinus 95Ala Arg Glu Gln Ser Cys Arg Arg Pro 1 5 969PRTDermatophagoides pteronyssinus 96Arg Glu Gln Ser Cys Arg Arg Pro Asn 1 5 979PRTDermatophagoides pteronyssinus 97Glu Gln Ser Cys Arg Arg Pro Asn Ala 1 5 989PRTDermatophagoides pteronyssinus 98Gln Ser Cys Arg Arg Pro Asn Ala Gln 1 5 9916PRTDermatophagoides pteronyssinus 99Tyr Tyr Arg Tyr Val Ala Arg Glu Gln Ser Cys Arg Arg Pro Asn Ala 1 5 10 15 1009PRTDermatophagoides pteronyssinus 100Gly Tyr Gly Tyr Phe Ala Ala Asn Ile 1 5 1019PRTDermatophagoides pteronyssinus 101Tyr Gly Tyr Phe Ala Ala Asn Ile Asp 1 5 1029PRTDermatophagoides pteronyssinus 102Gly Tyr Phe Ala Ala Asn Ile Asp Leu 1 5 1039PRTDermatophagoides pteronyssinus 103Tyr Phe Ala Ala Asn Ile Asp Leu Met 1 5 1049PRTDermatophagoides pteronyssinus 104Phe Ala Ala Asn Ile Asp Leu Met Met 1 5 1059PRTDermatophagoides pteronyssinus 105Ala Ala Asn Ile Asp Leu Met Met Ile 1 5 1069PRTDermatophagoides pteronyssinus 106Ala Asn Ile Asp Leu Met Met Ile Glu 1 5 10712PRTDermatophagoides pteronyssinus 107Tyr Gly Tyr Phe Ala Ala Asn Ile Asp Leu Met Met 1 5 10 1089PRTBetula pendula 108Pro Ala Ala Arg Met Phe Lys Ala Phe 1 5 1099PRTBetula pendula 109Ala Ala Arg Met Phe Lys Ala Phe Ile 1 5 1109PRTBetula pendula 110Ala Arg Met Phe Lys Ala Phe Ile Leu 1 5 1119PRTBetula pendula 111Arg Met Phe Lys Ala Phe Ile Leu Asp 1 5 11210PRTBetula pendula 112Ala Ala Arg Met Phe Lys Ala Phe Ile Leu 1 5 10 1139PRTBetula pendula 113Val Phe Asn Tyr Glu Ile Gly Ala Thr 1 5 1149PRTBetula pendula 114Phe Asn Tyr Glu Ile Gly Ala Thr Ser 1 5 1159PRTBetula pendula 115Asn Tyr Glu Ile Gly Ala Thr Ser Val 1 5 1169PRTBetula pendula 116Tyr Glu Ile Gly Ala Thr Ser Val Ile 1 5 1179PRTBetula pendula 117Glu Ile Gly Ala Thr Ser Val Ile Pro 1 5 1189PRTBetula pendula 118Ile Gly Ala Thr Ser Val Ile Pro Ala 1 5 1199PRTBetula pendula 119Gly Ala Thr Ser Val Ile Pro Ala Ala 1 5 12014PRTBetula pendula 120Val Phe Asn Tyr Glu Ile Gly Ala Thr Ser Val Ile Pro Ala 1 5 10 1219PRTBetula pendula 121Ser Pro Phe Lys Tyr Val Lys Glu Arg 1 5 1229PRTBetula pendula 122Pro Phe Lys Tyr Val Lys Glu Arg Val 1 5 1239PRTBetula pendula 123Phe Lys Tyr Val Lys Glu Arg Val Asp 1 5 1249PRTBetula pendula 124Lys Tyr Val Lys Glu Arg Val Asp Glu 1 5 1259PRTBetula pendula 125Tyr Val Lys Glu Arg Val Asp Glu Val 1 5 1269PRTBetula pendula 126Val Lys Glu Arg Val Asp Glu Val Asp 1 5 1279PRTBetula pendula 127Lys Glu Arg Val Asp Glu Val Asp His 1 5 1289PRTBetula pendula 128Asn Phe Lys Tyr Ser Tyr Ser Met Ile 1 5 1299PRTBetula pendula 129Phe Lys Tyr Ser Tyr Ser Met Ile Glu 1 5 1309PRTBetula pendula 130Lys Tyr Ser Tyr Ser Met Ile Glu Gly 1 5 1319PRTBetula pendula 131Tyr Ser Tyr Ser Met Ile Glu Gly Gly 1 5 1329PRTBetula pendula 132Ser Tyr Ser Met Ile Glu Gly Gly Ala 1 5 1339PRTBetula pendula 133Tyr Ser Met Ile Glu Gly Gly Ala Leu 1 5 1349PRTBetula pendula 134Ser Met Ile Glu Gly Gly Ala Leu Gly 1 5 13513PRTBetula pendula 135Phe Lys Tyr Ser Tyr Ser Met Ile Glu Gly Gly Ala Leu 1 5 10 1369PRTBetula pendula 136Ala Leu Leu Arg Ala Val Glu Ser Tyr 1 5 1379PRTBetula pendula 137Leu Leu Arg Ala Val Glu Ser Tyr Leu 1 5 1389PRTBetula pendula 138Leu Arg Ala Val Glu Ser Tyr Leu Leu 1 5 1399PRTBetula pendula 139Arg Ala Val Glu Ser Tyr Leu Leu Ala 1 5 1409PRTBetula pendula 140Ala Val Glu Ser Tyr Leu Leu Ala His 1 5 1419PRTBetula pendula 141Val Glu Ser Tyr Leu Leu Ala His Ser 1 5 1429PRTBetula pendula 142Glu Ser Tyr Leu Leu Ala His Ser Asp 1 5 1439PRTBetula

pendula 143Ser Tyr Leu Leu Ala His Ser Asp Ala 1 5 1449PRTBetula pendula 144Tyr Leu Leu Ala His Ser Asp Ala Tyr 1 5 14516PRTBetula pendula 145Leu Leu Arg Ala Val Glu Ser Tyr Leu Leu Ala His Ser Asp Ala Tyr 1 5 10 15 1469PRTPhleum pratense 146Gly Asp Glu Gln Lys Leu Arg Ser Ala 1 5 1479PRTPhleum pratense 147Asp Glu Gln Lys Leu Arg Ser Ala Gly 1 5 1489PRTPhleum pratense 148Glu Gln Lys Leu Arg Ser Ala Gly Glu 1 5 1499PRTPhleum pratense 149Gln Lys Leu Arg Ser Ala Gly Glu Leu 1 5 1509PRTPhleum pratense 150Lys Leu Arg Ser Ala Gly Glu Leu Glu 1 5 1519PRTPhleum pratense 151Leu Arg Ser Ala Gly Glu Leu Glu Leu 1 5 1529PRTPhleum pratense 152Arg Ser Ala Gly Glu Leu Glu Leu Gln 1 5 15313PRTPhleum pratense 153Asp Glu Gln Lys Leu Arg Ser Ala Gly Glu Leu Glu Leu 1 5 10 1549PRTPhleum pratense 154Asn Tyr Leu Ala Leu Leu Val Lys Tyr 1 5 1559PRTPhleum pratense 155Tyr Leu Ala Leu Leu Val Lys Tyr Val 1 5 1569PRTPhleum pratense 156Leu Ala Leu Leu Val Lys Tyr Val Asn 1 5 1579PRTPhleum pratense 157Ala Leu Leu Val Lys Tyr Val Asn Gly 1 5 15810PRTPhleum pratense 158Tyr Leu Ala Leu Leu Val Lys Tyr Val Asn 1 5 10 1599PRTPhleum pratense 159Ser Trp Gly Ala Ile Trp Arg Ile Asp 1 5 1609PRTPhleum pratense 160Trp Gly Ala Ile Trp Arg Ile Asp Thr 1 5 1619PRTPhleum pratense 161Gly Ala Ile Trp Arg Ile Asp Thr Pro 1 5 1629PRTPhleum pratense 162Ala Ile Trp Arg Ile Asp Thr Pro Asp 1 5 1639PRTPhleum pratense 163Ile Trp Arg Ile Asp Thr Pro Asp Lys 1 5 1649PRTPhleum pratense 164Trp Arg Ile Asp Thr Pro Asp Lys Leu 1 5 1659PRTPhleum pratense 165Arg Ile Asp Thr Pro Asp Lys Leu Thr 1 5 16613PRTPhleum pratense 166Trp Gly Ala Ile Trp Arg Ile Asp Thr Pro Asp Lys Leu 1 5 10 1679PRTPhleum pratense 167Gly Asp Glu Gln Lys Leu Arg Ser Ala 1 5 1689PRTPhleum pratense 168Asp Glu Gln Lys Leu Arg Ser Ala Gly 1 5 1699PRTPhleum pratense 169Glu Gln Lys Leu Arg Ser Ala Gly Glu 1 5 1709PRTPhleum pratense 170Gln Lys Leu Arg Ser Ala Gly Glu Leu 1 5 1719PRTPhleum pratense 171Lys Leu Arg Ser Ala Gly Glu Leu Glu 1 5 1729PRTPhleum pratense 172Leu Arg Ser Ala Gly Glu Leu Glu Leu 1 5 1739PRTPhleum pratense 173Arg Ser Ala Gly Glu Leu Glu Leu Gln 1 5 1749PRTPhleum pratense 174Lys Ile Asn Ala Gly Phe Lys Ala Ala 1 5 1759PRTPhleum pratense 175Ile Asn Ala Gly Phe Lys Ala Ala Leu 1 5 1769PRTPhleum pratense 176Asn Ala Gly Phe Lys Ala Ala Leu Ala 1 5 1779PRTPhleum pratense 177Ala Gly Phe Lys Ala Ala Leu Ala Ala 1 5 1789PRTPhleum pratense 178Gly Phe Lys Ala Ala Leu Ala Ala Ala 1 5 1799PRTPhleum pratense 179Phe Lys Ala Ala Leu Ala Ala Ala Ala 1 5 1809PRTPhleum pratense 180Lys Ala Ala Leu Ala Ala Ala Ala Gly 1 5 1819PRTPhleum pratense 181Ala Ala Leu Ala Ala Ala Ala Gly Val 1 5 1829PRTPhleum pratense 182Ala Leu Ala Ala Ala Ala Gly Val Gln 1 5 18315PRTPhleum pratense 183Ile Asn Ala Gly Phe Lys Ala Ala Leu Ala Ala Ala Ala Gly Val 1 5 10 15 1849PRTPhleum pratense 184Lys Tyr Arg Thr Phe Val Ala Thr Phe 1 5 1859PRTPhleum pratense 185Tyr Arg Thr Phe Val Ala Thr Phe Gly 1 5 1869PRTPhleum pratense 186Arg Thr Phe Val Ala Thr Phe Gly Ala 1 5 1879PRTPhleum pratense 187Phe Val Ala Thr Phe Gly Ala Ala Ser 1 5 1889PRTPhleum pratense 188Val Ala Thr Phe Gly Ala Ala Ser Asn 1 5 18912PRTPhleum pratense 189Tyr Arg Thr Phe Val Ala Thr Phe Gly Ala Ala Ser 1 5 10 1909PRTPhleum pratense 190Thr Ser Lys Leu Asp Ala Ala Tyr Lys 1 5 1919PRTPhleum pratense 191Ser Lys Leu Asp Ala Ala Tyr Lys Leu 1 5 1929PRTPhleum pratense 192Lys Leu Asp Ala Ala Tyr Lys Leu Ala 1 5 1939PRTPhleum pratense 193Leu Asp Ala Ala Tyr Lys Leu Ala Tyr 1 5 1949PRTPhleum pratense 194Asp Ala Ala Tyr Lys Leu Ala Tyr Lys 1 5 1959PRTPhleum pratense 195Ala Ala Tyr Lys Leu Ala Tyr Lys Thr 1 5 1969PRTPhleum pratense 196Ala Tyr Lys Leu Ala Tyr Lys Thr Ala 1 5 1979PRTPhleum pratense 197Tyr Lys Leu Ala Tyr Lys Thr Ala Glu 1 5 1989PRTPhleum pratense 198Lys Leu Ala Tyr Lys Thr Ala Glu Gly 1 5 1999PRTPhleum pratense 199Leu Ala Tyr Lys Thr Ala Glu Gly Ala 1 5 20016PRTPhleum pratense 200Ser Lys Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly 1 5 10 15 2019PRTPhleum pratense 201Lys Val Asp Ala Ala Phe Lys Val Ala 1 5 2029PRTPhleum pratense 202Val Asp Ala Ala Phe Lys Val Ala Ala 1 5 2039PRTPhleum pratense 203Asp Ala Ala Phe Lys Val Ala Ala Thr 1 5 2049PRTPhleum pratense 204Ala Ala Phe Lys Val Ala Ala Thr Ala 1 5 2059PRTPhleum pratense 205Ala Phe Lys Val Ala Ala Thr Ala Ala 1 5 2069PRTPhleum pratense 206Phe Lys Val Ala Ala Thr Ala Ala Asn 1 5 2079PRTPhleum pratense 207Lys Val Ala Ala Thr Ala Ala Asn Ala 1 5 2089PRTPhleum pratense 208Val Ala Ala Thr Ala Ala Asn Ala Ala 1 5 2099PRTPhleum pratense 209Ala Ala Thr Ala Ala Asn Ala Ala Pro 1 5 21015PRTPhleum pratense 210Val Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala 1 5 10 15 2119PRTPhleum pratense 211Ser Tyr Lys Phe Ile Pro Ala Leu Glu 1 5 2129PRTPhleum pratense 212Tyr Lys Phe Ile Pro Ala Leu Glu Ala 1 5 2139PRTPhleum pratense 213Lys Phe Ile Pro Ala Leu Glu Ala Ala 1 5 2149PRTPhleum pratense 214Phe Ile Pro Ala Leu Glu Ala Ala Val 1 5 2159PRTPhleum pratense 215Ile Pro Ala Leu Glu Ala Ala Val Lys 1 5 2169PRTPhleum pratense 216Pro Ala Leu Glu Ala Ala Val Lys Gln 1 5 2179PRTPhleum pratense 217Ala Leu Glu Ala Ala Val Lys Gln Ala 1 5 2189PRTPhleum pratense 218Leu Glu Ala Ala Val Lys Gln Ala Tyr 1 5 2199PRTPhleum pratense 219Glu Ala Ala Val Lys Gln Ala Tyr Ala 1 5 22015PRTPhleum pratense 220Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala Val Lys Gln Ala Tyr 1 5 10 15 2219PRTPhleum pratense 221Lys Tyr Thr Val Phe Glu Thr Ala Leu 1 5 2229PRTPhleum pratense 222Tyr Thr Val Phe Glu Thr Ala Leu Lys 1 5 2239PRTPhleum pratense 223Thr Val Phe Glu Thr Ala Leu Lys Lys 1 5 2249PRTPhleum pratense 224Val Phe Glu Thr Ala Leu Lys Lys Ala 1 5 2259PRTPhleum pratense 225Phe Glu Thr Ala Leu Lys Lys Ala Ile 1 5 2269PRTPhleum pratense 226Glu Thr Ala Leu Lys Lys Ala Ile Thr 1 5 2279PRTPhleum pratense 227Thr Ala Leu Lys Lys Ala Ile Thr Ala 1 5 2289PRTPhleum pratense 228Ala Leu Lys Lys Ala Ile Thr Ala Met 1 5 2299PRTPhleum pratense 229Leu Lys Lys Ala Ile Thr Ala Met Ser 1 5 2309PRTPhleum pratense 230Lys Lys Ala Ile Thr Ala Met Ser Glu 1 5 23116PRTPhleum pratense 231Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile Thr Ala Met Ser 1 5 10 15 2329PRTAlternaria alternata 232Gln Leu Leu Met Leu Ser Ala Lys Arg 1 5 2339PRTAlternaria alternata 233Leu Leu Met Leu Ser Ala Lys Arg Met 1 5 2349PRTAlternaria alternata 234Leu Met Leu Ser Ala Lys Arg Met Lys 1 5 2359PRTAlternaria alternata 235Met Leu Ser Ala Lys Arg Met Lys Val 1 5 2369PRTAlternaria alternata 236Leu Ser Ala Lys Arg Met Lys Val Ala 1 5 2379PRTAlternaria alternata 237Ser Ala Lys Arg Met Lys Val Ala Phe 1 5 2389PRTAlternaria alternata 238Ala Lys Arg Met Lys Val Ala Phe Lys 1 5 2399PRTAlternaria alternata 239Lys Arg Met Lys Val Ala Phe Lys Leu 1 5 2409PRTAlternaria alternata 240Arg Met Lys Val Ala Phe Lys Leu Asp 1 5 2419PRTAlternaria alternata 241Met Lys Val Ala Phe Lys Leu Asp Ile 1 5 2429PRTAlternaria alternata 242Lys Val Ala Phe Lys Leu Asp Ile Glu 1 5 24311PRTAlternaria alternata 243Leu Leu Met Leu Ser Ala Lys Arg Met Lys Val 1 5 10 24412PRTAlternaria alternata 244Ala Lys Arg Met Lys Val Ala Phe Lys Leu Asp Ile 1 5 10 24517PRTAlternaria alternata 245Leu Leu Met Leu Ser Ala Lys Arg Met Lys Val Ala Phe Lys Leu Asp 1 5 10 15 Ile 2469PRTAlternaria alternata 246Gly Phe Lys Arg Cys Leu Gln Phe Thr 1 5 2479PRTAlternaria alternata 247Phe Lys Arg Cys Leu Gln Phe Thr Leu 1 5 2489PRTAlternaria alternata 248Lys Arg Cys Leu Gln Phe Thr Leu Tyr 1 5 2499PRTAlternaria alternata 249Arg Cys Leu Gln Phe Thr Leu Tyr Arg 1 5 2509PRTAlternaria alternata 250Cys Leu Gln Phe Thr Leu Tyr Arg Pro 1 5 2519PRTAlternaria alternata 251Leu Gln Phe Thr Leu Tyr Arg Pro Arg 1 5 2529PRTAlternaria alternata 252Gln Phe Thr Leu Tyr Arg Pro Arg Asp 1 5 2539PRTAlternaria alternata 253Phe Thr Leu Tyr Arg Pro Arg Asp Leu 1 5 2549PRTAlternaria alternata 254Thr Leu Tyr Arg Pro Arg Asp Leu Leu 1 5 2559PRTAlternaria alternata 255Leu Tyr Arg Pro Arg Asp Leu Leu Ser 1 5 2569PRTAlternaria alternata 256Tyr Arg Pro Arg Asp Leu Leu Ser Leu 1 5 2579PRTAlternaria alternata 257Arg Pro Arg Asp Leu Leu Ser Leu Leu 1 5 25815PRTAlternaria alternata 258Phe Lys Arg Cys Leu Gln Phe Thr Leu Tyr Arg Pro Arg Asp Leu 1 5 10 15 25912PRTAlternaria alternata 259Phe Thr Leu Tyr Arg Pro Arg Asp Leu Leu Ser Leu 1 5 10 26018PRTAlternaria alternata 260Phe Lys Arg Cys Leu Gln Phe Thr Leu Tyr Arg Pro Arg Asp Leu Leu 1 5 10 15 Ser Leu 2619PRTAlternaria alternata 261Thr Tyr Tyr Asn Ser Leu Gly Phe Asn 1 5 2629PRTAlternaria alternata 262Tyr Tyr Asn Ser Leu Gly Phe Asn Ile 1 5 2639PRTAlternaria alternata 263Tyr Asn Ser Leu Gly Phe Asn Ile Lys 1 5 2649PRTAlternaria alternata 264Asn Ser Leu Gly Phe Asn Ile Lys Ala 1 5 2659PRTAlternaria alternata 265Ser Leu Gly Phe Asn Ile Lys Ala Thr 1 5 2669PRTAlternaria alternata 266Leu Gly Phe Asn Ile Lys Ala Thr Asn 1 5 2679PRTAlternaria alternata 267Gly Phe Asn Ile Lys Ala Thr Asn Gly 1 5 2689PRTAlternaria alternata 268Phe Asn Ile Lys Ala Thr Asn Gly Gly 1 5 2699PRTAlternaria alternata 269Asn Ile Lys Ala Thr Asn Gly Gly Thr 1 5 2709PRTAlternaria alternata 270Ile Lys Ala Thr Asn Gly Gly Thr Leu 1 5 2719PRTAlternaria alternata 271Lys Ala Thr Asn Gly Gly Thr Leu Asp 1 5 27217PRTAlternaria alternata 272Tyr Tyr Asn Ser Leu Gly Phe Asn Ile Lys Ala Thr Asn Gly Gly Thr 1 5 10 15 Leu 2739PRTAlternaria alternata 273Asp Ile Thr Tyr Val Ala Thr Ala Thr 1 5 2749PRTAlternaria alternata 274Ile Thr Tyr Val Ala Thr Ala Thr Leu 1 5 2759PRTAlternaria alternata 275Thr Tyr Val Ala Thr Ala Thr Leu Pro 1 5 2769PRTAlternaria alternata 276Tyr Val Ala Thr Ala Thr Leu Pro Asn 1 5 2779PRTAlternaria alternata 277Val Ala Thr Ala Thr Leu Pro Asn Tyr 1 5 2789PRTAlternaria alternata 278Ala Thr Ala Thr Leu Pro Asn Tyr Cys 1 5 27912PRTAlternaria alternata 279Ile Thr Tyr Val Ala Thr Ala Thr Leu Pro Asn Tyr 1 5 10 2809PRTAlternaria alternata 280Ala Tyr Ile Thr Leu Val Thr Leu Pro 1 5 2819PRTAlternaria alternata 281Tyr Ile Thr Leu Val Thr Leu Pro Lys 1 5 2829PRTAlternaria alternata 282Ile Thr Leu Val Thr Leu Pro Lys Ser 1 5 2839PRTAlternaria alternata 283Thr Leu Val Thr Leu Pro Lys Ser Ser 1 5 28410PRTAlternaria alternata 284Tyr Ile Thr Leu Val Thr Leu Pro Lys Ser 1 5 10 2859PRTAlternaria alternata 285Glu Val Tyr Gln Lys Leu Lys Ala Leu 1 5 2869PRTAlternaria alternata 286Val Tyr Gln Lys Leu Lys Ala Leu Ala 1 5 2879PRTAlternaria alternata 287Tyr Gln Lys Leu Lys Ala Leu Ala Lys 1 5 2889PRTAlternaria alternata 288Gln Lys Leu Lys Ala Leu Ala Lys Lys 1 5 2899PRTAlternaria alternata 289Lys Leu Lys Ala Leu Ala Lys Lys Thr 1 5 2909PRTAlternaria alternata 290Leu Lys Ala Leu Ala Lys Lys Thr Tyr 1 5 2919PRTAlternaria alternata 291Lys Ala Leu Ala Lys Lys Thr Tyr Gly 1 5 29213PRTAlternaria alternata 292Val Tyr Gln Lys Leu Lys Ala Leu Ala Lys Lys Thr Tyr 1 5 10 2939PRTAlternaria alternata 293Gly Tyr Thr Gly Lys Ile Lys Ile Ala 1 5 2949PRTAlternaria alternata 294Tyr Thr Gly Lys Ile Lys Ile Ala Met 1 5 2959PRTAlternaria alternata 295Thr Gly Lys Ile Lys Ile Ala Met Asp 1 5 2969PRTAlternaria alternata 296Gly Lys Ile Lys Ile Ala Met Asp Val 1 5 2979PRTAlternaria alternata 297Lys Ile Lys Ile Ala Met Asp Val Ala 1 5 2989PRTAlternaria alternata 298Ile Lys Ile Ala Met Asp Val Ala Ser 1 5 2999PRTAlternaria alternata 299Lys Ile Ala Met Asp Val Ala Ser Ser 1 5 3009PRTAlternaria alternata 300Ile Ala Met Asp Val Ala Ser Ser Glu 1 5 3019PRTAlternaria alternata 301Ala Met Asp Val Ala Ser Ser Glu Phe 1 5 30215PRTAlternaria alternata 302Tyr Thr Gly Lys Ile Lys Ile Ala Met Asp Val Ala Ser Ser Glu 1 5 10 15 3039PRTAlternaria alternata 303Ala Phe Gly Ala Gly Trp Gly Val Met 1 5 3049PRTAlternaria alternata 304Phe Gly Ala Gly Trp Gly Val Met Val 1 5 3059PRTAlternaria alternata 305Gly Ala Gly Trp Gly Val Met Val Ser 1 5 3069PRTAlternaria alternata 306Ala Gly Trp Gly Val Met Val Ser His 1 5 3079PRTAlternaria alternata 307Gly Trp Gly Val Met Val Ser His Arg 1 5 3089PRTAlternaria alternata 308Trp Gly Val Met Val Ser His Arg Ser 1 5 3099PRTAlternaria alternata 309Gly Val Met Val Ser His Arg Ser Gly 1 5 3109PRTAlternaria alternata 310Val Met Val Ser His Arg Ser Gly Glu 1 5 3119PRTAlternaria alternata 311Met Val Ser His Arg Ser Gly Glu Thr 1 5 3129PRTAlternaria alternata 312Val Ser His Arg Ser Gly Glu Thr Glu 1 5 31316PRTAlternaria alternata 313Phe Gly Ala

Gly Trp Gly Val Met Val Ser His Arg Ser Gly Glu Thr 1 5 10 15 31411PRTBetula pendula 314Phe Lys Tyr Val Lys Glu Arg Val Asp Glu Val 1 5 10 3159PRTPhleum pratense 315Thr Phe Val Ala Thr Phe Gly Ala Ala 1 5 316320PRTDermatophagoides pteronyssinus 316Met Lys Ile Val Leu Ala Ile Ala Ser Leu Leu Ala Leu Ser Ala Val 1 5 10 15 Tyr Ala Arg Pro Ser Ser Ile Lys Thr Phe Glu Glu Tyr Lys Lys Ala 20 25 30 Phe Asn Lys Ser Tyr Ala Thr Phe Glu Asp Glu Glu Ala Ala Arg Lys 35 40 45 Asn Phe Leu Glu Ser Val Lys Tyr Val Gln Ser Asn Gly Gly Ala Ile 50 55 60 Asn His Leu Ser Asp Leu Ser Leu Asp Glu Phe Lys Asn Arg Phe Leu 65 70 75 80 Met Ser Ala Glu Ala Phe Glu His Leu Lys Thr Gln Phe Asp Leu Asn 85 90 95 Ala Glu Thr Asn Ala Cys Ser Ile Asn Gly Asn Ala Pro Ala Glu Ile 100 105 110 Asp Leu Arg Gln Met Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly 115 120 125 Cys Gly Ser Cys Trp Ala Phe Ser Gly Val Ala Ala Thr Glu Ser Ala 130 135 140 Tyr Leu Ala Tyr Arg Asn Gln Ser Leu Asp Leu Ala Glu Gln Glu Leu 145 150 155 160 Val Asp Cys Ala Ser Gln His Gly Cys His Gly Asp Thr Ile Pro Arg 165 170 175 Gly Ile Glu Tyr Ile Gln His Asn Gly Val Val Gln Glu Ser Tyr Tyr 180 185 190 Arg Tyr Val Ala Arg Glu Gln Ser Cys Arg Arg Pro Asn Ala Gln Arg 195 200 205 Phe Gly Ile Ser Asn Tyr Cys Gln Ile Tyr Pro Pro Asn Val Asn Lys 210 215 220 Ile Arg Glu Ala Leu Ala Gln Thr His Ser Ala Ile Ala Val Ile Ile 225 230 235 240 Gly Ile Lys Asp Leu Asp Ala Phe Arg His Tyr Asp Gly Arg Thr Ile 245 250 255 Ile Gln Arg Asp Asn Gly Tyr Gln Pro Asn Tyr His Ala Val Asn Ile 260 265 270 Val Gly Tyr Ser Asn Ala Gln Gly Val Asp Tyr Trp Ile Val Arg Asn 275 280 285 Ser Trp Asp Thr Asn Trp Gly Asp Asn Gly Tyr Gly Tyr Phe Ala Ala 290 295 300 Asn Ile Asp Leu Met Met Ile Glu Glu Tyr Pro Tyr Val Val Ile Leu 305 310 315 320 317146PRTDermatophagoides pteronyssinus 317Met Met Tyr Lys Ile Leu Cys Leu Ser Leu Leu Val Ala Ala Val Ala 1 5 10 15 Arg Asp Gln Val Asp Val Lys Asp Cys Ala Asn His Glu Ile Lys Lys 20 25 30 Val Leu Val Pro Gly Cys His Gly Ser Glu Pro Cys Ile Ile His Arg 35 40 45 Gly Lys Pro Phe Gln Leu Glu Ala Val Phe Glu Ala Asn Gln Asn Thr 50 55 60 Lys Thr Ala Lys Ile Glu Ile Lys Ala Ser Ile Asp Gly Leu Glu Val 65 70 75 80 Asp Val Pro Gly Ile Asp Pro Asn Ala Cys His Tyr Met Lys Cys Pro 85 90 95 Leu Val Lys Gly Gln Gln Tyr Asp Ile Lys Tyr Thr Trp Asn Val Pro 100 105 110 Lys Ile Ala Pro Lys Ser Glu Asn Val Val Val Thr Val Lys Val Met 115 120 125 Gly Asp Asp Gly Val Leu Ala Cys Ala Ile Ala Thr His Ala Lys Ile 130 135 140 Arg Asp 145 318261PRTDermatophagoides pteronyssinus 318Met Ile Ile Tyr Asn Ile Leu Ile Val Leu Leu Leu Ala Ile Asn Thr 1 5 10 15 Leu Ala Asn Pro Ile Leu Pro Ala Ser Pro Asn Ala Thr Ile Val Gly 20 25 30 Gly Glu Lys Ala Leu Ala Gly Glu Cys Pro Tyr Gln Ile Ser Leu Gln 35 40 45 Ser Ser Ser His Phe Cys Gly Gly Thr Ile Leu Asp Glu Tyr Trp Ile 50 55 60 Leu Thr Ala Ala His Cys Val Ala Gly Gln Thr Ala Ser Lys Leu Ser 65 70 75 80 Ile Arg Tyr Asn Ser Leu Lys His Ser Leu Gly Gly Glu Lys Ile Ser 85 90 95 Val Ala Lys Ile Phe Ala His Glu Lys Tyr Asp Ser Tyr Gln Ile Asp 100 105 110 Asn Asp Ile Ala Leu Ile Lys Leu Lys Ser Pro Met Lys Leu Asn Gln 115 120 125 Lys Asn Ala Lys Ala Val Gly Leu Pro Ala Lys Gly Ser Asp Val Lys 130 135 140 Val Gly Asp Gln Val Arg Val Ser Gly Trp Gly Tyr Leu Glu Glu Gly 145 150 155 160 Ser Tyr Ser Leu Pro Ser Glu Leu Arg Arg Val Asp Ile Ala Val Val 165 170 175 Ser Arg Lys Glu Cys Asn Glu Leu Tyr Ser Lys Ala Asn Ala Glu Val 180 185 190 Thr Asp Asn Met Ile Cys Gly Gly Asp Val Ala Asn Gly Gly Lys Asp 195 200 205 Ser Cys Gln Gly Asp Ser Gly Gly Pro Val Val Asp Val Lys Asn Asn 210 215 220 Gln Val Val Gly Ile Val Ser Trp Gly Tyr Gly Cys Ala Arg Lys Gly 225 230 235 240 Tyr Pro Gly Val Tyr Thr Arg Val Gly Asn Phe Ile Asp Trp Ile Glu 245 250 255 Ser Lys Arg Ser Gln 260 31919PRTDermatophagoides pteronyssinusUNSURE(3)..(3)Xaa = unknown 319Lys Tyr Xaa Asn Pro His Phe Ile Gly Xaa Arg Ser Val Ile Thr Xaa 1 5 10 15 Leu Met Glu 320132PRTDermatophagoides pteronyssinus 320Met Lys Phe Ile Ile Ala Phe Phe Val Ala Thr Leu Ala Val Met Thr 1 5 10 15 Val Ser Gly Glu Asp Lys Lys His Asp Tyr Gln Asn Glu Phe Asp Phe 20 25 30 Leu Leu Met Glu Arg Ile His Glu Gln Ile Lys Lys Gly Glu Leu Ala 35 40 45 Leu Phe Tyr Leu Gln Glu Gln Ile Asn His Phe Glu Glu Lys Pro Thr 50 55 60 Lys Glu Met Lys Asp Lys Ile Val Ala Glu Met Asp Thr Ile Ile Ala 65 70 75 80 Met Ile Asp Gly Val Arg Gly Val Leu Asp Arg Leu Met Gln Arg Lys 85 90 95 Asp Leu Asp Ile Phe Glu Gln Tyr Asn Leu Glu Met Ala Lys Lys Ser 100 105 110 Gly Asp Ile Leu Glu Arg Asp Leu Lys Lys Glu Glu Ala Arg Val Lys 115 120 125 Lys Ile Glu Val 130 32120PRTDermatophagoides pteronyssinusUNSURE(4)..(4)Xaa = unknown 321Ala Ile Gly Xaa Gln Pro Ala Ala Glu Ala Glu Ala Pro Phe Gln Ile 1 5 10 15 Ser Leu Met Lys 20 322215PRTDermatophagoides pteronyssinus 322Met Met Lys Leu Leu Leu Ile Ala Ala Ala Ala Phe Val Ala Val Ser 1 5 10 15 Ala Asp Pro Ile His Tyr Asp Lys Ile Thr Glu Glu Ile Asn Lys Ala 20 25 30 Val Asp Glu Ala Val Ala Ala Ile Glu Lys Ser Glu Thr Phe Asp Pro 35 40 45 Met Lys Val Pro Asp His Ser Asp Lys Phe Glu Arg His Ile Gly Ile 50 55 60 Ile Asp Leu Lys Gly Glu Leu Asp Met Arg Asn Ile Gln Val Arg Gly 65 70 75 80 Leu Lys Gln Met Lys Arg Val Gly Asp Ala Asn Val Lys Ser Glu Asp 85 90 95 Gly Val Val Lys Ala His Leu Leu Val Gly Val His Asp Asp Val Val 100 105 110 Ser Met Glu Tyr Asp Leu Ala Tyr Lys Leu Gly Asp Leu His Pro Asn 115 120 125 Thr His Val Ile Ser Asp Ile Gln Asp Phe Val Val Glu Leu Ser Leu 130 135 140 Glu Val Ser Glu Glu Gly Asn Met Thr Leu Thr Ser Phe Glu Val Arg 145 150 155 160 Gln Phe Ala Asn Val Val Asn His Ile Gly Gly Leu Ser Ile Leu Asp 165 170 175 Pro Ile Phe Ala Val Leu Ser Asp Val Leu Thr Ala Ile Phe Gln Asp 180 185 190 Thr Val Arg Ala Glu Met Thr Lys Val Leu Ala Pro Ala Phe Lys Lys 195 200 205 Glu Leu Glu Arg Asn Asn Gln 210 215 32318PRTDermatophagoides pteronyssinus 323Ile Val Gly Gly Ser Asn Ala Ser Pro Gly Asp Ala Val Tyr Gln Ile 1 5 10 15 Ala Leu 324319PRTDermatophagoides farinae 324Met Lys Phe Val Leu Ala Ile Ala Ser Leu Leu Val Leu Thr Val Tyr 1 5 10 15 Ala Arg Pro Ala Ser Ile Lys Thr Phe Glu Phe Lys Lys Ala Phe Asn 20 25 30 Lys Asn Tyr Ala Thr Val Glu Glu Glu Glu Val Ala Arg Lys Asn Phe 35 40 45 Leu Glu Ser Leu Lys Tyr Val Glu Ala Asn Lys Gly Ala Ile Asn His 50 55 60 Leu Ser Asp Leu Ser Leu Asp Glu Phe Lys Asn Arg Tyr Leu Met Ser 65 70 75 80 Ala Glu Ala Phe Glu Gln Leu Lys Thr Gln Phe Asp Leu Asn Ala Glu 85 90 95 Thr Ser Ala Cys Arg Ile Asn Ser Val Asn Val Pro Ser Glu Leu Asp 100 105 110 Leu Arg Ser Leu Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly Cys 115 120 125 Gly Ser Cys Trp Ala Phe Ser Gly Val Ala Ala Thr Glu Ser Ala Tyr 130 135 140 Leu Ala Tyr Arg Asn Thr Ser Leu Asp Leu Ser Glu Gln Glu Leu Val 145 150 155 160 Asp Cys Ala Ser Gln His Gly Cys His Gly Asp Thr Ile Pro Arg Gly 165 170 175 Ile Glu Tyr Ile Gln Gln Asn Gly Val Val Glu Glu Arg Ser Tyr Pro 180 185 190 Tyr Val Ala Arg Glu Gln Arg Cys Arg Arg Pro Asn Ser Gln His Tyr 195 200 205 Gly Ile Ser Asn Tyr Cys Gln Ile Tyr Pro Pro Asp Val Lys Gln Ile 210 215 220 Arg Glu Ala Leu Thr Gln Thr His Thr Ala Ile Ala Val Ile Ile Gly 225 230 235 240 Ile Lys Asp Leu Arg Ala Phe Gln His Tyr Asp Gly Arg Thr Ile Ile 245 250 255 Gln His Asp Asn Gly Tyr Gln Pro Asn Tyr His Ala Val Asn Ile Val 260 265 270 Gly Tyr Gly Ser Thr Gln Gly Asp Asp Tyr Trp Ile Val Arg Asn Ser 275 280 285 Trp Asp Thr Thr Trp Gly Asp Ser Gly Tyr Gly Tyr Phe Gln Ala Gly 290 295 300 Asn Asn Leu Met Met Ile Glu Gln Tyr Pro Tyr Val Val Ile Met 305 310 315 325146PRTDermatophagoides farinae 325Met Ile Ser Lys Ile Leu Cys Leu Ser Leu Leu Val Ala Ala Val Val 1 5 10 15 Ala Asp Gln Val Asp Val Lys Asp Cys Ala Asn Asn Glu Ile Lys Lys 20 25 30 Val Met Val Asp Gly Cys His Gly Ser Asp Pro Cys Ile Ile His Arg 35 40 45 Gly Lys Pro Phe Thr Leu Glu Ala Leu Phe Asp Ala Asn Gln Asn Thr 50 55 60 Lys Thr Ala Lys Ile Glu Ile Lys Ala Ser Leu Asp Gly Leu Glu Ile 65 70 75 80 Asp Val Pro Gly Ile Asp Thr Asn Ala Cys His Phe Met Lys Cys Pro 85 90 95 Leu Val Lys Gly Gln Gln Tyr Asp Ile Lys Tyr Thr Trp Asn Val Pro 100 105 110 Lys Ile Ala Pro Lys Ser Glu Asn Val Val Val Thr Val Lys Leu Ile 115 120 125 Gly Asp Asn Gly Val Leu Ala Cys Ala Ile Ala Thr His Gly Lys Ile 130 135 140 Arg Asp 145 326259PRTDermatophagoides farinae 326Met Met Ile Leu Thr Ile Val Val Leu Leu Ala Ala Asn Ile Leu Ala 1 5 10 15 Thr Pro Ile Leu Pro Ser Ser Pro Asn Ala Thr Ile Val Gly Gly Val 20 25 30 Lys Ala Gln Ala Gly Asp Cys Pro Tyr Gln Ile Ser Leu Gln Ser Ser 35 40 45 Ser His Phe Cys Gly Gly Ser Ile Leu Asp Glu Tyr Trp Ile Leu Thr 50 55 60 Ala Ala His Cys Val Asn Gly Gln Ser Ala Lys Lys Leu Ser Ile Arg 65 70 75 80 Tyr Asn Thr Leu Lys His Ala Ser Gly Gly Glu Lys Ile Gln Val Ala 85 90 95 Glu Ile Tyr Gln His Glu Asn Tyr Asp Ser Met Thr Ile Asp Asn Asp 100 105 110 Val Ala Leu Ile Lys Leu Lys Thr Pro Met Thr Leu Asp Gln Thr Asn 115 120 125 Ala Lys Pro Val Pro Leu Pro Ala Gln Gly Ser Asp Val Lys Val Gly 130 135 140 Asp Lys Ile Arg Val Ser Gly Trp Gly Tyr Leu Gln Glu Gly Ser Tyr 145 150 155 160 Ser Leu Pro Ser Glu Leu Gln Arg Val Asp Ile Asp Val Val Ser Arg 165 170 175 Glu Gln Cys Asp Gln Leu Tyr Ser Lys Ala Gly Ala Asp Val Ser Glu 180 185 190 Asn Met Ile Cys Gly Gly Asp Val Ala Asn Gly Gly Val Asp Ser Cys 195 200 205 Gln Gly Asp Ser Gly Gly Pro Val Val Asp Val Ala Thr Lys Gln Ile 210 215 220 Val Gly Ile Val Ser Trp Gly Tyr Gly Cys Ala Arg Lys Gly Tyr Pro 225 230 235 240 Gly Val Tyr Thr Arg Val Gly Asn Phe Val Asp Trp Ile Glu Ser Lys 245 250 255 Arg Ser Gln 32720PRTDermatophagoides farinae 327Ala Val Gly Gly Gln Asp Ala Asp Leu Ala Glu Ala Pro Phe Gln Ile 1 5 10 15 Ser Leu Leu Lys 20 328213PRTDermatophagoides farinae 328Met Met Lys Phe Leu Leu Ile Ala Ala Val Ala Phe Val Ala Val Ser 1 5 10 15 Ala Asp Pro Ile His Tyr Asp Lys Ile Thr Glu Glu Ile Asn Lys Ala 20 25 30 Ile Asp Asp Ala Ile Ala Ala Ile Glu Gln Ser Glu Thr Ile Asp Pro 35 40 45 Met Lys Val Pro Asp His Ala Asp Lys Phe Glu Arg His Val Gly Ile 50 55 60 Val Asp Phe Lys Gly Glu Leu Ala Met Arg Asn Ile Glu Ala Arg Gly 65 70 75 80 Leu Lys Gln Met Lys Arg Gln Gly Asp Ala Asn Val Lys Gly Glu Glu 85 90 95 Gly Ile Val Lys Ala His Leu Leu Ile Gly Val His Asp Asp Ile Val 100 105 110 Ser Met Glu Tyr Asp Leu Ala Tyr Lys Leu Gly Asp Leu His Pro Thr 115 120 125 Thr His Val Ile Ser Asp Ile Gln Asp Phe Val Val Ala Leu Ser Leu 130 135 140 Glu Ile Ser Asp Glu Gly Asn Ile Thr Met Thr Ser Phe Glu Val Arg 145 150 155 160 Gln Phe Ala Asn Val Val Asn His Ile Gly Gly Leu Ser Ile Leu Asp 165 170 175 Pro Ile Phe Gly Val Leu Ser Asp Val Leu Thr Ala Ile Phe Gln Asp 180 185 190 Thr Val Arg Lys Glu Met Thr Lys Val Leu Ala Pro Ala Phe Lys Arg 195 200 205 Glu Leu Glu Lys Asn 210 329138PRTHevea brasiliensis 329Met Ala Glu Asp Glu Asp Asn Gln Gln Gly Gln Gly Glu Gly Leu Lys 1 5 10 15 Tyr Leu Gly Phe Val Gln Asp Ala Ala Thr Tyr Ala Val Thr Thr Phe 20 25 30 Ser Asn Val Tyr Leu Phe Ala Lys Asp Lys Ser Gly Pro Leu Gln Pro 35 40 45 Gly Val Asp Ile Ile Glu Gly Pro Val Lys Asn Val Ala Val Pro Leu 50 55 60 Tyr Asn Arg Phe Ser Tyr Ile Pro Asn Gly Ala Leu Lys Phe Val Asp 65 70 75 80 Ser Thr Val Val Ala Ser Val Thr Ile Ile Asp Arg Ser Leu Pro Pro

85 90 95 Ile Val Lys Asp Ala Ser Ile Gln Val Val Ser Ala Ile Arg Ala Ala 100 105 110 Pro Glu Ala Ala Arg Ser Leu Ala Ser Ser Leu Pro Gly Gln Thr Lys 115 120 125 Ile Leu Ala Lys Val Phe Tyr Gly Glu Asn 130 135 330204PRTHevea brasiliensis 330Met Ala Glu Glu Val Glu Glu Glu Arg Leu Lys Tyr Leu Asp Phe Val 1 5 10 15 Arg Ala Ala Gly Val Tyr Ala Val Asp Ser Phe Ser Thr Leu Tyr Leu 20 25 30 Tyr Ala Lys Asp Ile Ser Gly Pro Leu Lys Pro Gly Val Asp Thr Ile 35 40 45 Glu Asn Val Val Lys Thr Val Val Thr Pro Val Tyr Tyr Ile Pro Leu 50 55 60 Glu Ala Val Lys Phe Val Asp Lys Thr Val Asp Val Ser Val Thr Ser 65 70 75 80 Leu Asp Gly Val Val Pro Pro Val Ile Lys Gln Val Ser Ala Gln Thr 85 90 95 Tyr Ser Val Ala Gln Asp Ala Pro Arg Ile Val Leu Asp Val Ala Ser 100 105 110 Ser Val Phe Asn Thr Gly Val Gln Glu Gly Ala Lys Ala Leu Tyr Ala 115 120 125 Asn Leu Glu Pro Lys Ala Glu Gln Tyr Ala Val Ile Thr Trp Arg Ala 130 135 140 Leu Asn Lys Leu Pro Leu Val Pro Gln Val Ala Asn Val Val Val Pro 145 150 155 160 Thr Ala Val Tyr Phe Ser Glu Lys Tyr Asn Asp Val Val Arg Gly Thr 165 170 175 Thr Glu Gln Gly Tyr Arg Val Ser Ser Tyr Leu Pro Leu Leu Pro Thr 180 185 190 Glu Lys Ile Thr Lys Val Phe Gly Asp Glu Ala Ser 195 200 331263PRTLolium perenne 331Met Ala Ser Ser Ser Ser Val Leu Leu Val Val Ala Leu Phe Ala Val 1 5 10 15 Phe Leu Gly Ser Ala His Gly Ile Ala Lys Val Pro Pro Gly Pro Asn 20 25 30 Ile Thr Ala Glu Tyr Gly Asp Lys Trp Leu Asp Ala Lys Ser Thr Trp 35 40 45 Tyr Gly Lys Pro Thr Gly Ala Gly Pro Lys Asp Asn Gly Gly Ala Cys 50 55 60 Gly Tyr Lys Asn Val Asp Lys Ala Pro Phe Asn Gly Met Thr Gly Cys 65 70 75 80 Gly Asn Thr Pro Ile Phe Lys Asp Gly Arg Gly Cys Gly Ser Cys Phe 85 90 95 Glu Ile Lys Cys Thr Lys Pro Glu Ser Cys Ser Gly Glu Ala Val Thr 100 105 110 Val Thr Ile Thr Asp Asp Asn Glu Glu Pro Ile Ala Pro Tyr His Phe 115 120 125 Asp Leu Ser Gly His Ala Phe Gly Ser Met Ala Lys Lys Gly Glu Glu 130 135 140 Gln Asn Val Arg Ser Ala Gly Glu Leu Glu Leu Gln Phe Arg Arg Val 145 150 155 160 Lys Cys Lys Tyr Pro Asp Asp Thr Lys Pro Thr Phe His Val Glu Lys 165 170 175 Ala Ser Asn Pro Asn Tyr Leu Ala Ile Leu Val Lys Tyr Val Asp Gly 180 185 190 Asp Gly Asp Val Val Ala Val Asp Ile Lys Glu Lys Gly Lys Asp Lys 195 200 205 Trp Ile Glu Leu Lys Glu Ser Trp Gly Ala Val Trp Arg Ile Asp Thr 210 215 220 Pro Asp Lys Leu Thr Gly Pro Phe Thr Val Arg Tyr Thr Thr Glu Gly 225 230 235 240 Gly Thr Lys Ser Glu Phe Glu Asp Val Ile Pro Glu Gly Trp Lys Ala 245 250 255 Asp Thr Ser Tyr Ser Ala Lys 260 33297PRTLolium perenne 332Ala Ala Pro Val Glu Phe Thr Val Glu Lys Gly Ser Asp Glu Lys Asn 1 5 10 15 Leu Ala Leu Ser Ile Lys Tyr Asn Lys Glu Gly Asp Ser Met Ala Glu 20 25 30 Val Glu Leu Lys Glu His Gly Ser Asn Glu Trp Leu Ala Leu Lys Lys 35 40 45 Asn Gly Asp Gly Val Trp Glu Ile Lys Ser Asp Lys Pro Leu Lys Gly 50 55 60 Pro Phe Asn Phe Arg Phe Val Ser Glu Lys Gly Met Arg Asn Val Phe 65 70 75 80 Asp Asp Val Val Pro Ala Asp Phe Lys Val Gly Thr Thr Tyr Lys Pro 85 90 95 Glu 33397PRTLolium perenne 333Thr Lys Val Asp Leu Thr Val Glu Lys Gly Ser Asp Ala Lys Thr Leu 1 5 10 15 Val Leu Asn Ile Lys Tyr Thr Arg Pro Gly Asp Thr Leu Ala Glu Val 20 25 30 Glu Leu Arg Gln His Gly Ser Glu Glu Trp Glu Pro Met Thr Lys Lys 35 40 45 Gly Asn Leu Trp Glu Val Lys Ser Ala Lys Pro Leu Thr Gly Pro Met 50 55 60 Asn Phe Arg Phe Leu Ser Lys Gly Gly Met Lys Asn Val Phe Asp Glu 65 70 75 80 Val Ile Pro Thr Ala Phe Thr Val Gly Lys Thr Tyr Thr Pro Glu Tyr 85 90 95 Asn 334308PRTLolium perenne 334Met Ala Val Gln Lys Tyr Thr Val Ala Leu Phe Leu Arg Arg Gly Pro 1 5 10 15 Arg Gly Gly Pro Gly Arg Ser Tyr Ala Ala Asp Ala Gly Tyr Thr Pro 20 25 30 Ala Ala Ala Ala Thr Pro Ala Thr Pro Ala Ala Thr Pro Ala Gly Gly 35 40 45 Trp Arg Glu Gly Asp Asp Arg Arg Ala Glu Ala Ala Gly Gly Arg Gln 50 55 60 Arg Leu Ala Ser Arg Gln Pro Trp Pro Pro Leu Pro Thr Pro Leu Arg 65 70 75 80 Arg Thr Ser Ser Arg Ser Ser Arg Pro Pro Ser Pro Ser Pro Pro Arg 85 90 95 Ala Ser Ser Pro Thr Ser Ala Ala Lys Ala Pro Gly Leu Ile Pro Lys 100 105 110 Leu Asp Thr Ala Tyr Asp Val Ala Tyr Lys Ala Ala Glu Ala His Pro 115 120 125 Arg Gly Gln Val Arg Arg Leu Arg His Cys Pro His Arg Ser Leu Arg 130 135 140 Val Ile Ala Gly Ala Leu Glu Val His Ala Val Lys Pro Ala Thr Glu 145 150 155 160 Glu Val Leu Ala Ala Lys Ile Pro Thr Gly Glu Leu Gln Ile Val Asp 165 170 175 Lys Ile Asp Ala Ala Phe Lys Ile Ala Ala Thr Ala Ala Asn Ala Ala 180 185 190 Pro Thr Asn Asp Lys Phe Thr Val Phe Glu Ser Ala Phe Asn Lys Ala 195 200 205 Leu Asn Glu Cys Thr Gly Gly Ala Met Arg Pro Thr Ser Ser Ser Pro 210 215 220 Pro Ser Arg Pro Arg Ser Ser Arg Pro Thr Pro Pro Pro Ser Pro Ala 225 230 235 240 Ala Pro Glu Val Lys Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala 245 250 255 Ile Thr Ala Met Thr Gln Ala Gln Lys Ala Gly Lys Pro Ala Ala Ala 260 265 270 Ala Ala Thr Ala Ala Ala Thr Val Ala Thr Ala Ala Ala Thr Ala Ala 275 280 285 Ala Val Leu Pro Pro Pro Leu Leu Val Val Gln Ser Leu Ile Ser Leu 290 295 300 Leu Ile Tyr Tyr 305 335339PRTLolium perenne 335Met Ala Val Gln Lys His Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Ala Gly Tyr Ala Pro 20 25 30 Ala Thr Pro Ala Thr Pro Ala Ala Pro Ala Thr Ala Ala Thr Pro Ala 35 40 45 Thr Pro Ala Thr Pro Ala Thr Pro Ala Ala Val Pro Ser Gly Lys Ala 50 55 60 Thr Thr Glu Glu Gln Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys 65 70 75 80 Ala Ala Val Ala Ala Ala Ala Val Val Pro Pro Ala Asp Lys Tyr Lys 85 90 95 Thr Phe Val Glu Thr Phe Gly Thr Ala Thr Asn Lys Ala Phe Val Glu 100 105 110 Gly Leu Ala Ser Gly Tyr Ala Asp Gln Ser Lys Asn Gln Leu Thr Ser 115 120 125 Lys Leu Asp Ala Ala Leu Lys Leu Ala Tyr Glu Ala Ala Gln Gly Ala 130 135 140 Thr Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Leu Thr Glu Ala 145 150 155 160 Leu Arg Val Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro Ala 165 170 175 Ala Glu Glu Val Lys Val Gly Ala Ile Pro Ala Ala Glu Val Gln Leu 180 185 190 Ile Asp Lys Val Asp Ala Ala Tyr Arg Thr Ala Ala Thr Ala Ala Asn 195 200 205 Ala Ala Pro Ala Asn Asp Lys Phe Thr Val Phe Glu Asn Thr Phe Asn 210 215 220 Asn Ala Ile Lys Val Ser Leu Gly Ala Ala Tyr Asp Ser Tyr Lys Phe 225 230 235 240 Ile Pro Thr Leu Val Ala Ala Val Lys Gln Ala Tyr Ala Ala Lys Gln 245 250 255 Ala Thr Ala Pro Glu Val Lys Tyr Thr Val Ser Glu Thr Ala Leu Lys 260 265 270 Lys Ala Val Thr Ala Met Ser Glu Ala Glu Lys Glu Ala Thr Pro Ala 275 280 285 Ala Ala Ala Thr Ala Thr Pro Thr Pro Ala Ala Ala Thr Ala Thr Ala 290 295 300 Thr Pro Ala Ala Ala Tyr Ala Thr Ala Thr Pro Ala Ala Ala Thr Ala 305 310 315 320 Thr Ala Thr Pro Ala Ala Ala Thr Ala Thr Pro Ala Ala Ala Gly Gly 325 330 335 Tyr Lys Val 336339PRTLolium perenne 336Met Ala Val Gln Lys His Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Ala Gly Tyr Ala Pro 20 25 30 Ala Thr Pro Ala Thr Pro Ala Ala Pro Ala Thr Ala Ala Thr Pro Ala 35 40 45 Thr Pro Ala Thr Pro Ala Thr Pro Ala Ala Val Pro Ser Gly Lys Ala 50 55 60 Thr Thr Glu Glu Gln Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys 65 70 75 80 Ala Ala Val Ala Ala Ala Ala Val Val Pro Pro Ala Asp Lys Tyr Lys 85 90 95 Thr Phe Val Glu Thr Phe Gly Thr Ala Thr Asn Lys Ala Phe Val Glu 100 105 110 Gly Leu Ala Ser Gly Tyr Ala Asp Gln Ser Lys Asn Gln Leu Thr Ser 115 120 125 Lys Leu Asp Ala Ala Leu Lys Leu Ala Tyr Glu Ala Ala Gln Gly Ala 130 135 140 Thr Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Leu Thr Glu Ala 145 150 155 160 Leu Arg Val Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro Ala 165 170 175 Ala Glu Glu Val Lys Val Gly Ala Ile Pro Ala Ala Glu Val Gln Leu 180 185 190 Ile Asp Lys Val Asp Ala Ala Tyr Arg Thr Ala Ala Thr Ala Ala Asn 195 200 205 Ala Ala Pro Ala Asn Asp Lys Phe Thr Val Phe Glu Asn Thr Phe Asn 210 215 220 Asn Ala Ile Lys Val Ser Leu Gly Ala Ala Tyr Asp Ser Tyr Lys Phe 225 230 235 240 Ile Pro Thr Leu Val Ala Ala Val Lys Gln Ala Tyr Ala Ala Lys Gln 245 250 255 Ala Thr Ala Pro Glu Val Lys Tyr Thr Val Ser Glu Thr Ala Leu Lys 260 265 270 Lys Ala Val Thr Ala Met Ser Glu Ala Glu Lys Glu Ala Thr Pro Ala 275 280 285 Ala Ala Ala Thr Ala Thr Pro Thr Pro Ala Ala Ala Thr Ala Thr Ala 290 295 300 Thr Pro Ala Ala Ala Tyr Ala Thr Ala Thr Pro Ala Ala Ala Thr Ala 305 310 315 320 Thr Ala Thr Pro Ala Ala Ala Thr Ala Thr Pro Ala Ala Ala Gly Gly 325 330 335 Tyr Lys Val 337134PRTLolium perenneUNSURE(103)..(103)Xaa = unknown 337Asp Lys Gly Pro Gly Phe Val Val Thr Gly Arg Val Tyr Cys Asp Pro 1 5 10 15 Cys Arg Ala Gly Phe Glu Thr Asn Val Ser His Asn Val Glu Gly Ala 20 25 30 Thr Val Ala Val Asp Cys Arg Pro Phe Asp Gly Gly Glu Ser Lys Leu 35 40 45 Lys Ala Glu Ala Thr Thr Asp Lys Asp Gly Trp Tyr Lys Ile Glu Ile 50 55 60 Asp Gln Asp His Gln Glu Glu Ile Cys Glu Val Val Leu Ala Lys Ser 65 70 75 80 Pro Asp Lys Ser Cys Ser Glu Ile Glu Glu Phe Arg Asp Arg Ala Arg 85 90 95 Val Pro Leu Thr Ser Asn Xaa Gly Ile Lys Gln Gln Gly Ile Arg Tyr 100 105 110 Ala Asn Pro Ile Ala Phe Phe Arg Lys Glu Pro Leu Lys Glu Cys Gly 115 120 125 Gly Ile Leu Gln Ala Tyr 130 338145PRTOlea europaea 338Glu Asp Ile Pro Gln Pro Pro Val Ser Gln Phe His Ile Gln Gly Gln 1 5 10 15 Val Tyr Cys Asp Thr Cys Arg Ala Gly Phe Ile Thr Glu Leu Ser Glu 20 25 30 Phe Ile Pro Gly Ala Ser Leu Arg Leu Gln Cys Lys Asp Lys Glu Asn 35 40 45 Gly Asp Val Thr Phe Thr Glu Val Gly Tyr Thr Arg Ala Glu Gly Leu 50 55 60 Tyr Ser Met Leu Val Glu Arg Asp His Lys Asn Glu Phe Cys Glu Ile 65 70 75 80 Thr Leu Ile Ser Ser Gly Arg Lys Asp Cys Asn Glu Ile Pro Thr Glu 85 90 95 Gly Trp Ala Lys Pro Ser Leu Lys Phe Lys Leu Asn Thr Val Asn Gly 100 105 110 Thr Thr Arg Thr Val Asn Pro Leu Gly Phe Phe Lys Lys Glu Ala Leu 115 120 125 Pro Lys Cys Ala Gln Val Tyr Asn Lys Leu Gly Met Tyr Pro Pro Asn 130 135 140 Met 145 339133PRTParietaria judaica 339Met Arg Thr Val Ser Met Ala Ala Leu Val Val Ile Ala Ala Ala Leu 1 5 10 15 Ala Trp Thr Ser Ser Ala Glu Pro Ala Pro Ala Pro Ala Pro Gly Glu 20 25 30 Glu Ala Cys Gly Lys Val Val Gln Asp Ile Met Pro Cys Leu His Phe 35 40 45 Val Lys Gly Glu Glu Lys Glu Pro Ser Lys Glu Cys Cys Ser Gly Thr 50 55 60 Lys Lys Leu Ser Glu Glu Val Lys Thr Thr Glu Gln Lys Arg Glu Ala 65 70 75 80 Cys Lys Cys Ile Val Arg Ala Thr Lys Gly Ile Ser Gly Ile Lys Asn 85 90 95 Glu Leu Val Ala Glu Val Pro Lys Lys Cys Asp Ile Lys Thr Thr Leu 100 105 110 Pro Pro Ile Thr Ala Asp Phe Asp Cys Ser Lys Ile Gln Ser Thr Ile 115 120 125 Phe Arg Gly Tyr Tyr 130 340133PRTParietaria judaica 340Met Val Arg Ala Leu Met Pro Cys Leu Pro Phe Val Gln Gly Lys Glu 1 5 10 15 Lys Glu Pro Ser Lys Gly Cys Cys Ser Gly Ala Lys Arg Leu Asp Gly 20 25 30 Glu Thr Lys Thr Gly Pro Gln Arg Val His Ala Cys Glu Cys Ile Gln 35 40 45 Thr Ala Met Lys Thr Tyr Ser Asp Ile Asp Gly Lys Leu Val Ser Glu 50 55 60 Val Pro Lys His Cys Gly Ile Val Asp Ser Lys Leu Pro Pro Ile Asp 65 70 75 80 Val Asn Met Asp Cys Lys Thr Val Gly Val Val Pro Arg Gln Pro Gln 85 90 95 Leu Pro Val Ser Leu Arg His Gly Pro Val Thr Gly Pro Ser Asp Pro 100 105 110 Ala His Lys Ala Arg Leu Glu Arg Pro Gln Ile Arg Val Pro Pro Pro 115 120 125 Ala Pro Glu Lys Ala 130 341133PRTParietaria judaica 341Met Arg Thr Val Ser Met Ala Ala Leu Val Val Ile Ala Ala Ala Leu 1 5 10

15 Ala Trp Thr Ser Ser Ala Glu Leu Ala Ser Ala Pro Ala Pro Gly Glu 20 25 30 Gly Pro Cys Gly Lys Val Val His His Ile Met Pro Cys Leu Lys Phe 35 40 45 Val Lys Gly Glu Glu Lys Glu Pro Ser Lys Ser Cys Cys Ser Gly Thr 50 55 60 Lys Lys Leu Ser Glu Glu Val Lys Thr Thr Glu Gln Lys Arg Glu Ala 65 70 75 80 Cys Lys Cys Ile Val Ala Ala Thr Lys Gly Ile Ser Gly Ile Lys Asn 85 90 95 Glu Leu Val Ala Glu Val Pro Lys Lys Cys Gly Ile Thr Thr Thr Leu 100 105 110 Pro Pro Ile Thr Ala Asp Phe Asp Cys Ser Lys Ile Glu Ser Thr Ile 115 120 125 Phe Arg Gly Tyr Tyr 130 342176PRTParietaria judaica 342Met Arg Thr Val Ser Ala Pro Ser Ala Val Ala Leu Val Val Ile Val 1 5 10 15 Ala Ala Gly Leu Ala Trp Thr Ser Leu Ala Ser Val Ala Pro Pro Ala 20 25 30 Pro Ala Pro Gly Ser Glu Glu Thr Cys Gly Thr Val Val Arg Ala Leu 35 40 45 Met Pro Cys Leu Pro Phe Val Gln Gly Lys Glu Lys Glu Pro Ser Lys 50 55 60 Gly Cys Cys Ser Gly Ala Lys Arg Leu Asp Gly Glu Thr Lys Thr Gly 65 70 75 80 Leu Gln Arg Val His Ala Cys Glu Cys Ile Gln Thr Ala Met Lys Thr 85 90 95 Tyr Ser Asp Ile Asp Gly Lys Leu Val Ser Glu Val Pro Lys His Cys 100 105 110 Gly Ile Val Asp Ser Lys Leu Pro Pro Ile Asp Val Asn Met Asp Cys 115 120 125 Lys Thr Leu Gly Val Val Pro Arg Gln Pro Gln Leu Pro Val Ser Leu 130 135 140 Arg His Gly Pro Val Thr Gly Pro Ser Asp Pro Ala His Lys Ala Arg 145 150 155 160 Leu Glu Arg Pro Gln Ile Arg Val Pro Pro Pro Ala Pro Glu Lys Ala 165 170 175 343138PRTParietaria judaica 343Met Arg Thr Val Ser Ala Arg Ser Ser Val Ala Leu Val Val Ile Val 1 5 10 15 Ala Ala Val Leu Val Trp Thr Ser Ser Ala Ser Val Ala Pro Ala Pro 20 25 30 Ala Pro Gly Ser Glu Glu Thr Cys Gly Thr Val Val Gly Ala Leu Met 35 40 45 Pro Cys Leu Pro Phe Val Gln Gly Lys Glu Lys Glu Pro Ser Lys Gly 50 55 60 Cys Cys Ser Gly Ala Lys Arg Leu Asp Gly Glu Thr Lys Thr Gly Pro 65 70 75 80 Gln Arg Val His Ala Cys Glu Cys Ile Gln Thr Ala Met Lys Thr Tyr 85 90 95 Ser Asp Ile Asp Gly Lys Leu Val Ser Glu Val Pro Lys His Cys Gly 100 105 110 Ile Val Asp Ser Lys Leu Pro Pro Ile Asp Val Asn Met Asp Cys Lys 115 120 125 Thr Leu Gly Val Leu His Tyr Lys Gly Asn 130 135 344143PRTParietaria judaica 344Met Val Arg Ala Leu Met Pro Cys Leu Pro Phe Val Gln Gly Lys Glu 1 5 10 15 Lys Glu Pro Ser Lys Gly Cys Cys Ser Gly Ala Lys Arg Leu Asp Gly 20 25 30 Glu Thr Lys Thr Gly Pro Gln Arg Val His Ala Cys Glu Cys Ile Gln 35 40 45 Thr Ala Met Lys Thr Tyr Ser Asp Ile Asp Gly Lys Leu Val Ser Glu 50 55 60 Val Pro Lys His Cys Gly Ile Val Asp Ser Lys Leu Pro Pro Ile Asp 65 70 75 80 Val Asn Met Asp Cys Lys Thr Val Gly Val Val Pro Arg Gln Pro Gln 85 90 95 Leu Pro Val Ser Leu Arg His Gly Pro Val Thr Gly Pro Ser Arg Ser 100 105 110 Arg Pro Pro Thr Lys His Gly Trp Arg Asp Pro Arg Leu Glu Phe Arg 115 120 125 Pro Pro His Arg Lys Lys Pro Asn Pro Ala Phe Ser Thr Leu Gly 130 135 140 345263PRTPhleum pratense 345Met Ala Ser Ser Ser Ser Val Leu Leu Val Val Val Leu Phe Ala Val 1 5 10 15 Phe Leu Gly Ser Ala Tyr Gly Ile Pro Lys Val Pro Pro Gly Pro Asn 20 25 30 Ile Thr Ala Thr Tyr Gly Asp Lys Trp Leu Asp Ala Lys Ser Thr Trp 35 40 45 Tyr Gly Lys Pro Thr Gly Ala Gly Pro Lys Asp Asn Gly Gly Ala Cys 50 55 60 Gly Tyr Lys Asp Val Asp Lys Pro Pro Phe Ser Gly Met Thr Gly Cys 65 70 75 80 Gly Asn Thr Pro Ile Phe Lys Ser Gly Arg Gly Cys Gly Ser Cys Phe 85 90 95 Glu Ile Lys Cys Thr Lys Pro Glu Ala Cys Ser Gly Glu Pro Val Val 100 105 110 Val His Ile Thr Asp Asp Asn Glu Glu Pro Ile Ala Pro Tyr His Phe 115 120 125 Asp Leu Ser Gly His Ala Phe Gly Ala Met Ala Lys Lys Gly Asp Glu 130 135 140 Gln Lys Leu Arg Ser Ala Gly Glu Leu Glu Leu Gln Phe Arg Arg Val 145 150 155 160 Lys Cys Lys Tyr Pro Glu Gly Thr Lys Val Thr Phe His Val Glu Lys 165 170 175 Gly Ser Asn Pro Asn Tyr Leu Ala Leu Leu Val Lys Tyr Val Asn Gly 180 185 190 Asp Gly Asp Val Val Ala Val Asp Ile Lys Glu Lys Gly Lys Asp Lys 195 200 205 Trp Ile Glu Leu Lys Glu Ser Trp Gly Ala Ile Trp Arg Ile Asp Thr 210 215 220 Pro Asp Lys Leu Thr Gly Pro Phe Thr Val Arg Tyr Thr Thr Glu Gly 225 230 235 240 Gly Thr Lys Thr Glu Ala Glu Asp Val Ile Pro Glu Gly Trp Lys Ala 245 250 255 Asp Thr Ser Tyr Glu Ser Lys 260 346262PRTPhleum pratense 346Met Ala Ser Ser Ser Ser Val Leu Leu Val Val Ala Leu Phe Ala Val 1 5 10 15 Phe Leu Gly Ser Ala His Gly Ile Pro Lys Val Pro Pro Gly Pro Asn 20 25 30 Ile Thr Ala Thr Tyr Gly Asp Lys Trp Leu Asp Ala Lys Ser Thr Trp 35 40 45 Tyr Gly Lys Pro Thr Ala Ala Gly Pro Lys Asp Asn Gly Gly Ala Cys 50 55 60 Gly Tyr Lys Asp Val Asp Lys Pro Pro Phe Ser Gly Met Thr Gly Cys 65 70 75 80 Gly Asn Thr Pro Ile Phe Lys Ser Gly Arg Gly Cys Gly Ser Cys Phe 85 90 95 Glu Ile Lys Cys Thr Lys Pro Glu Ala Cys Ser Gly Glu Pro Val Val 100 105 110 Val His Ile Thr Asp Asp Asn Glu Glu Pro Ile Ala Ala Tyr His Phe 115 120 125 Asp Leu Ser Gly Ile Ala Phe Gly Ser Met Ala Lys Lys Gly Asp Glu 130 135 140 Gln Lys Leu Arg Ser Ala Gly Glu Val Glu Ile Gln Phe Arg Arg Val 145 150 155 160 Lys Cys Lys Tyr Pro Glu Gly Thr Lys Val Thr Phe His Val Glu Lys 165 170 175 Gly Ser Asn Pro Asn Tyr Leu Ala Leu Leu Val Lys Phe Ser Gly Asp 180 185 190 Gly Asp Val Val Ala Val Asp Ile Lys Glu Lys Gly Lys Asp Lys Trp 195 200 205 Ile Ala Leu Lys Glu Ser Trp Gly Ala Ile Trp Arg Ile Asp Thr Pro 210 215 220 Glu Val Leu Lys Gly Pro Phe Thr Val Arg Tyr Thr Thr Glu Gly Gly 225 230 235 240 Thr Lys Ala Arg Ala Lys Asp Val Ile Pro Glu Gly Trp Lys Ala Asp 245 250 255 Thr Ala Tyr Glu Ser Lys 260 347122PRTPhleum pratense 347Met Ser Met Ala Ser Ser Ser Ser Ser Ser Leu Leu Ala Met Ala Val 1 5 10 15 Leu Ala Ala Leu Phe Ala Gly Ala Trp Cys Val Pro Lys Val Thr Phe 20 25 30 Thr Val Glu Lys Gly Ser Asn Glu Lys His Leu Ala Val Leu Val Lys 35 40 45 Tyr Glu Gly Asp Thr Met Ala Glu Val Glu Leu Arg Glu His Gly Ser 50 55 60 Asp Glu Trp Val Ala Met Thr Lys Gly Glu Gly Gly Val Trp Thr Phe 65 70 75 80 Asp Ser Glu Glu Pro Leu Gln Gly Pro Phe Asn Phe Arg Phe Leu Thr 85 90 95 Glu Lys Gly Met Lys Asn Val Phe Asp Asp Val Val Pro Glu Lys Tyr 100 105 110 Thr Ile Gly Ala Thr Tyr Ala Pro Glu Glu 115 120 348276PRTPhleum pratense 348Ala Asp Leu Gly Tyr Gly Gly Pro Ala Thr Pro Ala Ala Pro Ala Glu 1 5 10 15 Ala Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu 20 25 30 Lys Ile Asn Asp Gly Phe Lys Ala Ala Leu Ala Ala Ala Ala Gly Val 35 40 45 Pro Pro Ala Asp Lys Tyr Lys Thr Phe Val Ala Thr Phe Gly Ala Ala 50 55 60 Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Ala Glu Pro Lys Gly Ala 65 70 75 80 Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala 85 90 95 Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys 100 105 110 Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala 115 120 125 Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala Glu Glu Val Lys 130 135 140 Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys Val Asp Ser Ala 145 150 155 160 Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys 165 170 175 Phe Thr Val Phe Glu Ala Ala Phe Asn Asn Ala Ile Lys Ala Ser Thr 180 185 190 Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala 195 200 205 Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala Pro Glu Val Lys 210 215 220 Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Phe Thr Ala Met Ser 225 230 235 240 Glu Ala Gln Lys Ala Ala Lys Pro Ala Thr Glu Ala Thr Ala Thr Ala 245 250 255 Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr Ala Ala Thr Gly 260 265 270 Gly Tyr Lys Val 275 349276PRTPhleum pratense 349Ala Asp Leu Gly Tyr Gly Gly Pro Ala Thr Pro Ala Ala Pro Ala Glu 1 5 10 15 Ala Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu 20 25 30 Lys Ile Asn Asp Gly Phe Lys Ala Ala Leu Ala Ala Ala Ala Gly Val 35 40 45 Pro Pro Ala Asp Lys Tyr Lys Thr Phe Val Ala Thr Phe Gly Ala Ala 50 55 60 Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Ala Glu Pro Lys Gly Ala 65 70 75 80 Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala 85 90 95 Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys 100 105 110 Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala 115 120 125 Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala Glu Glu Val Lys 130 135 140 Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys Val Asp Ser Ala 145 150 155 160 Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys 165 170 175 Phe Thr Val Phe Glu Ala Ala Phe Asn Asn Ala Ile Lys Ala Ser Thr 180 185 190 Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala 195 200 205 Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala Pro Glu Val Lys 210 215 220 Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile Thr Ala Met Ser 225 230 235 240 Glu Ala Gln Lys Ala Ala Lys Pro Ala Thr Glu Ala Thr Ala Thr Ala 245 250 255 Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr Ala Ala Thr Gly 260 265 270 Gly Tyr Lys Val 275 350284PRTPhleum pratense 350Ala Ala Ala Ala Val Pro Arg Arg Gly Pro Arg Gly Gly Pro Gly Arg 1 5 10 15 Ser Tyr Thr Ala Asp Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala 20 25 30 Gly Ala Ala Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu 35 40 45 Asp Ile Asn Val Gly Phe Lys Ala Ala Val Ala Ala Ala Ala Ser Val 50 55 60 Pro Ala Ala Asp Lys Phe Lys Thr Phe Glu Ala Ala Phe Thr Ser Ser 65 70 75 80 Ser Lys Ala Ala Ala Ala Lys Ala Pro Gly Leu Val Pro Lys Leu Asp 85 90 95 Ala Ala Tyr Ser Val Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu 100 105 110 Ala Lys Phe Asp Ser Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val 115 120 125 Ile Ala Gly Ala Leu Glu Val His Ala Val Lys Pro Val Thr Glu Glu 130 135 140 Pro Gly Met Ala Lys Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys 145 150 155 160 Ile Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro 165 170 175 Ala Asp Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile 180 185 190 Lys Glu Ser Thr Gly Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser 195 200 205 Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala 210 215 220 Pro Gln Val Lys Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile 225 230 235 240 Thr Ala Met Ser Glu Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala 245 250 255 Ala Thr Val Ala Ala Gly Ala Ala Thr Thr Ala Ala Gly Ala Ala Ser 260 265 270 Gly Ala Ala Thr Val Ala Ala Gly Gly Tyr Lys Val 275 280 351286PRTPhleum pratense 351Ala Asp Leu Gly Tyr Gly Pro Ala Thr Pro Ala Ala Pro Ala Ala Gly 1 5 10 15 Tyr Thr Pro Ala Thr Pro Ala Ala Pro Ala Gly Ala Asp Ala Ala Gly 20 25 30 Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Lys Ile Asn Ala Gly 35 40 45 Phe Lys Ala Ala Leu Ala Gly Ala Gly Val Gln Pro Ala Asp Lys Tyr 50 55 60 Arg Thr Phe Val Ala Thr Phe Gly Pro Ala Ser Asn Lys Ala Phe Ala 65 70 75 80 Glu Gly Leu Ser Gly Glu Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys 85 90 95 Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys 100 105 110 Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala 115 120 125 Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr Leu Glu Val His 130 135 140 Ala Val Lys Pro Ala Ala Glu Glu Val Lys Val Ile Pro Ala Gly Glu 145 150 155 160 Leu Gln Val Ile Glu Lys Val Asp Ala Ala Phe Lys Val Ala Ala Thr 165 170 175 Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys Phe Thr Val Phe Glu Ala 180 185 190 Ala Phe Asn Asp Glu Ile Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser 195

200 205 Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala 210 215 220 Ala Thr Val Ala Thr Ala Pro Glu Val Lys Tyr Thr Val Phe Glu Thr 225 230 235 240 Ala Leu Lys Lys Ala Ile Thr Ala Met Ser Glu Ala Gln Lys Ala Ala 245 250 255 Lys Pro Ala Ala Ala Ala Thr Ala Thr Ala Thr Ala Ala Val Gly Ala 260 265 270 Ala Thr Gly Ala Ala Thr Ala Ala Thr Gly Gly Tyr Lys Val 275 280 285 352287PRTPhleum pratense 352Met Ala Val Gln Lys Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Ala Gly Tyr Ala Pro 20 25 30 Ala Thr Pro Ala Ala Ala Gly Ala Glu Ala Gly Lys Ala Thr Thr Glu 35 40 45 Glu Gln Lys Leu Ile Glu Asp Ile Asn Val Gly Phe Lys Ala Ala Val 50 55 60 Ala Ala Ala Ala Ser Val Pro Ala Ala Asp Lys Phe Lys Thr Phe Glu 65 70 75 80 Ala Ala Phe Thr Ser Ser Ser Lys Ala Ala Thr Ala Lys Ala Pro Gly 85 90 95 Leu Val Pro Lys Leu Asp Ala Ala Tyr Ser Val Ser Tyr Lys Ala Ala 100 105 110 Val Gly Ala Thr Pro Glu Ala Lys Phe Asp Ser Phe Val Ala Ser Leu 115 120 125 Thr Glu Ala Leu Arg Val Ile Ala Gly Ala Leu Glu Val His Ala Val 130 135 140 Lys Pro Val Thr Glu Glu Pro Gly Met Ala Lys Ile Pro Ala Gly Glu 145 150 155 160 Leu Gln Ile Ile Asp Lys Ile Asp Ala Ala Phe Lys Val Ala Ala Thr 165 170 175 Ala Ala Ala Thr Ala Pro Ala Asp Thr Val Phe Glu Ala Ala Phe Asn 180 185 190 Lys Ala Ile Lys Glu Ser Thr Gly Gly Ala Tyr Asp Thr Tyr Lys Cys 195 200 205 Ile Pro Ser Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val 210 215 220 Ala Ala Ala Pro Gln Val Lys Tyr Ala Val Phe Glu Ala Ala Leu Thr 225 230 235 240 Lys Ala Ile Thr Ala Met Ser Glu Val Gln Lys Val Ser Gln Pro Ala 245 250 255 Thr Gly Ala Ala Thr Val Ala Ala Gly Ala Ala Thr Thr Ala Ala Gly 260 265 270 Ala Ala Ser Gly Ala Ala Thr Val Ala Ala Gly Gly Tyr Lys Val 275 280 285 353290PRTPhleum pratense 353Met Ala Val Gln Lys Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Ala Gly Tyr Ala Pro 20 25 30 Ala Thr Pro Ala Ala Ala Gly Ala Glu Ala Gly Lys Ala Thr Thr Glu 35 40 45 Glu Gln Lys Leu Ile Glu Asp Ile Asn Val Gly Phe Lys Ala Ala Val 50 55 60 Ala Ala Ala Ala Ser Val Pro Ala Ala Asp Lys Phe Lys Thr Phe Glu 65 70 75 80 Ala Ala Phe Thr Ser Ser Ser Lys Ala Ala Thr Ala Lys Ala Pro Gly 85 90 95 Leu Val Pro Lys Leu Asp Ala Ala Tyr Ser Val Ala Tyr Lys Ala Ala 100 105 110 Val Gly Ala Thr Pro Glu Ala Lys Phe Asp Ser Phe Val Ala Ser Leu 115 120 125 Thr Glu Ala Leu Arg Val Ile Ala Gly Ala Leu Glu Val His Ala Val 130 135 140 Lys Pro Val Thr Glu Asp Pro Ala Trp Pro Lys Ile Pro Ala Gly Glu 145 150 155 160 Leu Gln Ile Ile Asp Lys Ile Asp Ala Ala Phe Lys Val Ala Ala Thr 165 170 175 Ala Ala Ala Thr Ala Pro Ala Asp Asp Lys Phe Thr Val Phe Glu Ala 180 185 190 Ala Phe Asn Lys Ala Ile Lys Glu Ser Thr Gly Gly Ala Tyr Asp Thr 195 200 205 Tyr Lys Cys Ile Pro Ser Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala 210 215 220 Ala Thr Val Ala Ala Ala Pro Gln Val Lys Tyr Ala Val Phe Glu Ala 225 230 235 240 Ala Leu Thr Lys Ala Ile Thr Ala Met Ser Glu Val Gln Lys Val Ser 245 250 255 Gln Pro Ala Thr Gly Ala Ala Thr Val Ala Ala Gly Ala Ala Thr Thr 260 265 270 Ala Thr Gly Ala Ala Ser Gly Ala Ala Thr Val Ala Ala Gly Gly Tyr 275 280 285 Lys Val 290 354265PRTPhleum pratense 354Ala Asp Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala Gly Ala Glu 1 5 10 15 Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Asp Ile Asn 20 25 30 Val Gly Phe Lys Ala Ala Val Ala Ala Ala Ala Ser Val Pro Ala Ala 35 40 45 Asp Lys Phe Lys Thr Phe Glu Ala Ala Phe Thr Ser Ser Ser Lys Ala 50 55 60 Ala Thr Ala Lys Ala Pro Gly Leu Val Pro Lys Leu Asp Ala Ala Tyr 65 70 75 80 Ser Val Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu Ala Lys Phe 85 90 95 Asp Ser Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val Ile Ala Gly 100 105 110 Ala Leu Glu Val His Ala Val Lys Pro Val Thr Glu Glu Pro Gly Met 115 120 125 Ala Lys Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys Ile Asp Ala 130 135 140 Ala Phe Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro Ala Asp Asp 145 150 155 160 Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile Lys Glu Ser 165 170 175 Thr Gly Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser Leu Glu Ala 180 185 190 Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala Pro Gln Val 195 200 205 Lys Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile Thr Ala Met 210 215 220 Ser Glu Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala Ala Thr Val 225 230 235 240 Ala Ala Gly Ala Ala Thr Thr Ala Ala Gly Ala Ala Ser Gly Ala Ala 245 250 255 Thr Val Ala Ala Gly Gly Tyr Lys Val 260 265 355295PRTPhleum pratense 355Ser Val Lys Arg Ser Asn Gly Ser Ala Glu Val His Arg Gly Ala Val 1 5 10 15 Pro Arg Arg Gly Pro Arg Gly Gly Pro Gly Arg Ser Tyr Ala Ala Asp 20 25 30 Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala Gly Ala Glu Ala Gly 35 40 45 Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Asp Ile Asn Val Gly 50 55 60 Phe Lys Ala Ala Val Ala Ala Ala Ala Ser Val Pro Ala Ala Asp Lys 65 70 75 80 Phe Lys Thr Phe Glu Ala Ala Phe Thr Ser Ser Ser Lys Ala Ala Thr 85 90 95 Ala Lys Ala Pro Gly Leu Val Pro Lys Leu Asp Ala Ala Tyr Ser Val 100 105 110 Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu Ala Lys Phe Asp Ser 115 120 125 Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val Ile Ala Gly Ala Leu 130 135 140 Glu Val His Ala Val Lys Pro Val Thr Glu Glu Pro Gly Met Ala Lys 145 150 155 160 Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys Ile Asp Ala Ala Phe 165 170 175 Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro Ala Asp Asp Lys Phe 180 185 190 Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile Lys Glu Ser Thr Gly 195 200 205 Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser Leu Glu Ala Ala Val 210 215 220 Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala Pro Gln Val Lys Tyr 225 230 235 240 Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile Thr Ala Met Ser Glu 245 250 255 Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala Ala Thr Val Ala Ala 260 265 270 Gly Ala Ala Thr Thr Ala Ala Gly Ala Ala Ser Gly Ala Ala Thr Val 275 280 285 Ala Ala Gly Gly Tyr Lys Val 290 295 356312PRTPhleum pratense 356Met Ala Val His Gln Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Gly Ser Tyr Ala Ala Asp Leu Gly Tyr Gly Pro 20 25 30 Ala Thr Pro Ala Ala Pro Ala Ala Gly Tyr Thr Pro Ala Thr Pro Ala 35 40 45 Ala Pro Ala Gly Ala Glu Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln 50 55 60 Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys Ala Ala Leu Ala Ala 65 70 75 80 Ala Ala Gly Val Pro Pro Ala Asp Lys Tyr Arg Thr Phe Val Ala Thr 85 90 95 Phe Gly Ala Ala Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Gly Glu 100 105 110 Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys 115 120 125 Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr 130 135 140 Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Val Ser Glu Ala Leu 145 150 155 160 Arg Ile Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala 165 170 175 Glu Glu Val Lys Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys 180 185 190 Val Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro 195 200 205 Ala Asn Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Asp Ala Ile 210 215 220 Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala 225 230 235 240 Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala 245 250 255 Pro Glu Val Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile 260 265 270 Thr Ala Met Ser Glu Ala Gln Lys Ala Ala Lys Pro Ala Ala Ala Ala 275 280 285 Thr Ala Thr Ala Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr 290 295 300 Ala Ala Thr Gly Gly Tyr Lys Val 305 310 357276PRTPhleum pratense 357Ala Asp Leu Gly Tyr Gly Gly Pro Ala Thr Pro Ala Ala Pro Ala Glu 1 5 10 15 Ala Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu 20 25 30 Lys Ile Asn Asp Gly Phe Lys Ala Ala Leu Ala Ala Ala Ala Gly Val 35 40 45 Pro Pro Ala Asp Lys Tyr Lys Thr Phe Val Ala Thr Phe Gly Ala Ala 50 55 60 Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Ala Glu Pro Lys Gly Ala 65 70 75 80 Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala 85 90 95 Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys 100 105 110 Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala 115 120 125 Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala Glu Glu Val Lys 130 135 140 Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys Val Asp Ser Ala 145 150 155 160 Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys 165 170 175 Phe Thr Val Phe Glu Ala Ala Phe Asn Asn Ala Ile Lys Ala Ser Thr 180 185 190 Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala 195 200 205 Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala Pro Glu Val Lys 210 215 220 Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Phe Thr Ala Met Ser 225 230 235 240 Glu Ala Gln Lys Ala Ala Lys Pro Ala Thr Glu Ala Thr Ala Thr Ala 245 250 255 Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr Ala Ala Thr Gly 260 265 270 Gly Tyr Lys Val 275 358284PRTPhleum pratense 358Ala Ala Ala Ala Val Pro Arg Arg Gly Pro Arg Gly Gly Pro Gly Arg 1 5 10 15 Ser Tyr Thr Ala Asp Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala 20 25 30 Gly Ala Ala Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu 35 40 45 Asp Ile Asn Val Gly Phe Lys Ala Ala Val Ala Ala Ala Ala Ser Val 50 55 60 Pro Ala Ala Asp Lys Phe Lys Thr Phe Glu Ala Ala Phe Thr Ser Ser 65 70 75 80 Ser Lys Ala Ala Ala Ala Lys Ala Pro Gly Leu Val Pro Lys Leu Asp 85 90 95 Ala Ala Tyr Ser Val Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu 100 105 110 Ala Lys Phe Asp Ser Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val 115 120 125 Ile Ala Gly Ala Leu Glu Val His Ala Val Lys Pro Val Thr Glu Glu 130 135 140 Pro Gly Met Ala Lys Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys 145 150 155 160 Ile Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro 165 170 175 Ala Asp Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile 180 185 190 Lys Glu Ser Thr Gly Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser 195 200 205 Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala 210 215 220 Pro Gln Val Lys Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile 225 230 235 240 Thr Ala Met Ser Glu Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala 245 250 255 Ala Thr Val Ala Ala Gly Ala Ala Thr Thr Ala Ala Gly Ala Ala Ser 260 265 270 Gly Ala Ala Thr Val Ala Ala Gly Gly Tyr Lys Val 275 280 359286PRTPhleum pratense 359Ala Asp Leu Gly Tyr Gly Pro Ala Thr Pro Ala Ala Pro Ala Ala Gly 1 5 10 15 Tyr Thr Pro Ala Thr Pro Ala Ala Pro Ala Gly Ala Asp Ala Ala Gly 20 25 30 Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Lys Ile Asn Ala Gly 35 40 45 Phe Lys Ala Ala Leu Ala Gly Ala Gly Val Gln Pro Ala Asp Lys Tyr 50 55 60 Arg Thr Phe Val Ala Thr Phe Gly Pro Ala Ser Asn Lys Ala Phe Ala 65 70 75 80 Glu Gly Leu Ser Gly Glu Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys 85 90 95 Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys 100 105 110 Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala 115 120 125 Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr Leu Glu Val His 130 135 140 Ala Val Lys Pro Ala Ala Glu Glu Val Lys Val Ile Pro Ala Gly Glu 145 150 155 160 Leu Gln Val Ile Glu Lys Val Asp Ala Ala Phe Lys Val Ala Ala Thr 165 170 175 Ala Ala Asn Ala

Ala Pro Ala Asn Asp Lys Phe Thr Val Phe Glu Ala 180 185 190 Ala Phe Asn Asp Glu Ile Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser 195 200 205 Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala 210 215 220 Ala Thr Val Ala Thr Ala Pro Glu Val Lys Tyr Thr Val Phe Glu Thr 225 230 235 240 Ala Leu Lys Lys Ala Ile Thr Ala Met Ser Glu Ala Gln Lys Ala Ala 245 250 255 Lys Pro Ala Ala Ala Ala Thr Ala Thr Ala Thr Ala Ala Val Gly Ala 260 265 270 Ala Thr Gly Ala Ala Thr Ala Ala Thr Gly Gly Tyr Lys Val 275 280 285 360281PRTPhleum pratense 360Ala Val Pro Arg Arg Gly Pro Arg Gly Gly Pro Gly Arg Ser Tyr Ala 1 5 10 15 Ala Asp Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala Gly Ala Glu 20 25 30 Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Asp Ile Asn 35 40 45 Val Gly Phe Lys Ala Ala Val Ala Ala Ala Ala Ser Val Pro Ala Gly 50 55 60 Asp Lys Phe Lys Thr Phe Glu Ala Ala Phe Thr Ser Ser Ser Lys Ala 65 70 75 80 Ala Thr Ala Lys Ala Pro Gly Leu Val Pro Lys Leu Asp Ala Ala Tyr 85 90 95 Ser Val Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu Ala Lys Phe 100 105 110 Asp Ser Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val Ile Ala Gly 115 120 125 Ala Leu Glu Val His Ala Val Lys Pro Val Thr Glu Glu Pro Gly Met 130 135 140 Ala Lys Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys Ile Asp Ala 145 150 155 160 Ala Phe Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro Ala Asp Asp 165 170 175 Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile Lys Glu Ser 180 185 190 Thr Gly Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser Leu Glu Ala 195 200 205 Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala Pro Gln Val 210 215 220 Lys Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile Thr Ala Met 225 230 235 240 Ser Glu Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala Ala Thr Val 245 250 255 Ala Ala Gly Ala Ala Thr Thr Ala Thr Gly Ala Ala Ser Gly Ala Ala 260 265 270 Thr Val Ala Ala Gly Gly Tyr Lys Val 275 280 361280PRTPhleum pratense 361Met Ala Val Pro Arg Arg Gly Pro Arg Gly Gly Pro Gly Arg Ser Tyr 1 5 10 15 Thr Ala Asp Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala Gly Ala 20 25 30 Ala Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Asp Ile 35 40 45 Asn Val Gly Phe Lys Ala Ala Val Ala Ala Arg Gln Arg Pro Ala Ala 50 55 60 Asp Lys Phe Lys Thr Phe Glu Ala Ala Ser Pro Arg His Pro Arg Pro 65 70 75 80 Leu Arg Gln Gly Ala Gly Leu Val Pro Lys Leu Asp Ala Ala Tyr Ser 85 90 95 Val Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu Ala Lys Phe Asp 100 105 110 Ser Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val Ile Ala Gly Ala 115 120 125 Leu Glu Val His Ala Val Lys Pro Val Thr Glu Glu Pro Gly Met Ala 130 135 140 Lys Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys Ile Asp Ala Ala 145 150 155 160 Phe Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro Ala Asp Asp Lys 165 170 175 Phe Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile Lys Glu Ser Thr 180 185 190 Gly Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser Leu Glu Ala Ala 195 200 205 Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala Ala Glu Val Lys 210 215 220 Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile Thr Ala Met Ser 225 230 235 240 Glu Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala Ala Thr Val Ala 245 250 255 Ala Gly Ala Ala Thr Thr Ala Ala Gly Ala Ala Ser Gly Ala Ala Thr 260 265 270 Val Ala Ala Gly Gly Tyr Lys Val 275 280 362312PRTPhleum pratense 362Met Ala Val His Gln Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Leu Gly Tyr Gly Pro 20 25 30 Ala Thr Pro Ala Ala Pro Ala Ala Gly Tyr Thr Pro Ala Thr Pro Ala 35 40 45 Ala Pro Ala Glu Ala Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln 50 55 60 Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys Ala Ala Leu Ala Ala 65 70 75 80 Ala Ala Gly Val Gln Pro Ala Asp Lys Tyr Arg Thr Phe Val Ala Thr 85 90 95 Phe Gly Ala Ala Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Gly Glu 100 105 110 Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys 115 120 125 Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr 130 135 140 Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu 145 150 155 160 Arg Ile Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala 165 170 175 Glu Glu Val Lys Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys 180 185 190 Val Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro 195 200 205 Ala Asn Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Asp Ala Ile 210 215 220 Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala 225 230 235 240 Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala 245 250 255 Pro Glu Val Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile 260 265 270 Thr Ala Met Ser Glu Ala Gln Lys Ala Ala Lys Pro Ala Ala Ala Ala 275 280 285 Thr Ala Thr Ala Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr 290 295 300 Ala Ala Thr Gly Gly Tyr Lys Val 305 310 363257PRTPhleum pratense 363Glu Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu 1 5 10 15 Lys Ile Asn Ala Gly Phe Lys Ala Ala Leu Ala Arg Arg Leu Gln Pro 20 25 30 Ala Asp Lys Tyr Arg Thr Phe Val Ala Thr Phe Gly Pro Ala Ser Asn 35 40 45 Lys Ala Phe Ala Glu Gly Leu Ser Gly Glu Pro Lys Gly Ala Ala Glu 50 55 60 Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala Tyr Lys 65 70 75 80 Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys Tyr Asp 85 90 95 Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr 100 105 110 Leu Glu Val His Ala Val Lys Pro Ala Ala Glu Glu Val Lys Val Ile 115 120 125 Pro Ala Ala Glu Leu Gln Val Ile Glu Lys Val Asp Ala Ala Phe Lys 130 135 140 Val Ala Ala Thr Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys Phe Thr 145 150 155 160 Val Phe Glu Ala Ala Phe Asn Asp Glu Ile Lys Ala Ser Thr Gly Gly 165 170 175 Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala Val Lys 180 185 190 Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala Pro Glu Val Lys Tyr Thr 195 200 205 Val Phe Glu Thr Ala Leu Lys Lys Ala Ile Thr Ala Met Ser Glu Ala 210 215 220 Gln Lys Ala Ala Lys Pro Pro Pro Leu Pro Pro Pro Pro Gln Pro Pro 225 230 235 240 Pro Leu Ala Ala Thr Gly Ala Ala Thr Ala Ala Thr Gly Gly Tyr Lys 245 250 255 Val 364312PRTPhleum pratense 364Met Ala Val His Gln Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Leu Gly Tyr Gly Pro 20 25 30 Ala Thr Pro Ala Ala Pro Ala Ala Gly Tyr Thr Pro Ala Thr Pro Ala 35 40 45 Ala Pro Ala Glu Ala Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln 50 55 60 Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys Ala Ala Leu Ala Ala 65 70 75 80 Ala Ala Gly Val Gln Pro Ala Asp Lys Tyr Arg Thr Phe Val Ala Thr 85 90 95 Phe Gly Ala Ala Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Gly Glu 100 105 110 Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys 115 120 125 Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr 130 135 140 Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu 145 150 155 160 Arg Ile Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala 165 170 175 Glu Glu Val Lys Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys 180 185 190 Val Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro 195 200 205 Ala Asn Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Asp Ala Ile 210 215 220 Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala 225 230 235 240 Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala 245 250 255 Pro Glu Val Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile 260 265 270 Thr Ala Met Ser Glu Ala Gln Lys Ala Ala Lys Pro Ala Ala Ala Ala 275 280 285 Thr Ala Thr Ala Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr 290 295 300 Ala Ala Thr Gly Gly Tyr Lys Val 305 310 365280PRTPhleum pratense 365Met Ala Val Pro Arg Arg Gly Pro Arg Gly Gly Pro Gly Arg Ser Tyr 1 5 10 15 Thr Ala Asp Ala Gly Tyr Ala Pro Ala Thr Pro Ala Ala Ala Gly Ala 20 25 30 Ala Ala Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Asp Ile 35 40 45 Asn Val Gly Phe Lys Ala Ala Val Ala Ala Arg Gln Arg Pro Ala Ala 50 55 60 Asp Lys Phe Lys Thr Phe Glu Ala Ala Ser Pro Arg His Pro Arg Pro 65 70 75 80 Leu Arg Gln Gly Ala Gly Leu Val Pro Lys Leu Asp Ala Ala Tyr Ser 85 90 95 Val Ala Tyr Lys Ala Ala Val Gly Ala Thr Pro Glu Ala Lys Phe Asp 100 105 110 Ser Phe Val Ala Ser Leu Thr Glu Ala Leu Arg Val Ile Ala Gly Ala 115 120 125 Leu Glu Val His Ala Val Lys Pro Val Thr Glu Glu Pro Gly Met Ala 130 135 140 Lys Ile Pro Ala Gly Glu Leu Gln Ile Ile Asp Lys Ile Asp Ala Ala 145 150 155 160 Phe Lys Val Ala Ala Thr Ala Ala Ala Thr Ala Pro Ala Asp Asp Lys 165 170 175 Phe Thr Val Phe Glu Ala Ala Phe Asn Lys Ala Ile Lys Glu Ser Thr 180 185 190 Gly Gly Ala Tyr Asp Thr Tyr Lys Cys Ile Pro Ser Leu Glu Ala Ala 195 200 205 Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Ala Ala Ala Glu Val Lys 210 215 220 Tyr Ala Val Phe Glu Ala Ala Leu Thr Lys Ala Ile Thr Ala Met Ser 225 230 235 240 Glu Val Gln Lys Val Ser Gln Pro Ala Thr Gly Ala Ala Thr Val Ala 245 250 255 Ala Gly Ala Ala Thr Thr Ala Ala Gly Ala Ala Ser Gly Ala Ala Thr 260 265 270 Val Ala Ala Gly Gly Tyr Lys Val 275 280 366285PRTPhleum pratense 366Ala Asp Leu Gly Tyr Gly Pro Ala Thr Pro Ala Ala Pro Ala Ala Gly 1 5 10 15 Tyr Thr Pro Ala Thr Pro Ala Ala Pro Ala Gly Ala Asp Ala Ala Gly 20 25 30 Lys Ala Thr Thr Glu Glu Gln Lys Leu Ile Glu Lys Ile Asn Ala Gly 35 40 45 Phe Lys Ala Ala Leu Ala Gly Ala Gly Val Gln Pro Ala Asp Lys Tyr 50 55 60 Arg Thr Phe Val Ala Thr Phe Gly Pro Ala Ser Asn Lys Ala Phe Ala 65 70 75 80 Glu Gly Leu Ser Gly Glu Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys 85 90 95 Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys 100 105 110 Thr Ala Glu Gly Ala Thr Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala 115 120 125 Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr Leu Glu Val His 130 135 140 Ala Val Lys Pro Ala Ala Glu Glu Val Lys Val Ile Pro Ala Gly Glu 145 150 155 160 Leu Gln Val Ile Glu Lys Val Asp Ala Ala Phe Lys Val Ala Ala Thr 165 170 175 Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys Phe Thr Val Phe Glu Ala 180 185 190 Ala Phe Asn Asp Glu Ile Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser 195 200 205 Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala 210 215 220 Ala Thr Val Ala Thr Ala Pro Glu Val Lys Tyr Thr Val Phe Glu Thr 225 230 235 240 Ala Leu Lys Lys Ala Ile Thr Ala Met Ser Glu Ala Gln Lys Ala Ala 245 250 255 Lys Pro Pro Pro Leu Pro Pro Pro Pro Gln Pro Pro Pro Leu Ala Ala 260 265 270 Thr Gly Ala Ala Thr Ala Ala Thr Gly Gly Tyr Lys Val 275 280 285 367312PRTPhleum pratense 367Met Ala Val His Gln Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Leu Gly Tyr Gly Pro 20 25 30 Ala Thr Pro Ala Ala Pro Ala Ala Gly Tyr Thr Pro Ala Thr Pro Ala 35 40 45 Ala Pro Ala Glu Ala Ala Pro Ala Gly Lys Ala Thr Thr Glu Glu Gln 50 55 60 Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys Ala Ala Leu Ala Ala 65 70 75 80 Ala Ala Gly Val Gln Pro Ala Asp Lys Tyr Arg Thr Phe Val Ala Thr 85 90 95 Phe Gly Ala Ala Ser Asn Lys Ala Phe Ala Glu Gly Leu Ser Gly Glu 100 105 110 Pro Lys Gly Ala Ala Glu Ser Ser Ser Lys Ala Ala Leu Thr Ser Lys 115 120 125 Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys Thr Ala Glu Gly Ala Thr 130 135 140 Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu 145 150 155

160 Arg Ile Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro Ala Ala 165 170 175 Glu Glu Val Lys Val Ile Pro Ala Gly Glu Leu Gln Val Ile Glu Lys 180 185 190 Val Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro 195 200 205 Ala Asn Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Asp Ala Ile 210 215 220 Lys Ala Ser Thr Gly Gly Ala Tyr Glu Ser Tyr Lys Phe Ile Pro Ala 225 230 235 240 Leu Glu Ala Ala Val Lys Gln Ala Tyr Ala Ala Thr Val Ala Thr Ala 245 250 255 Pro Glu Val Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile 260 265 270 Thr Ala Met Ser Glu Ala Gln Lys Ala Ala Lys Pro Ala Ala Ala Ala 275 280 285 Thr Ala Thr Ala Thr Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr 290 295 300 Ala Ala Thr Gly Gly Tyr Lys Val 305 310 368138PRTPhleum pratense 368Met Ala Ala His Lys Phe Met Val Ala Met Phe Leu Ala Val Ala Val 1 5 10 15 Val Leu Gly Leu Ala Thr Ser Pro Thr Ala Glu Gly Gly Lys Ala Thr 20 25 30 Thr Glu Glu Gln Lys Leu Ile Glu Asp Val Asn Ala Ser Phe Arg Ala 35 40 45 Ala Met Ala Thr Thr Ala Asn Val Pro Pro Ala Asp Lys Tyr Lys Thr 50 55 60 Phe Glu Ala Ala Phe Thr Val Ser Ser Lys Arg Asn Leu Ala Asp Ala 65 70 75 80 Val Ser Lys Ala Pro Gln Leu Val Pro Lys Leu Asp Glu Val Tyr Asn 85 90 95 Ala Ala Tyr Asn Ala Ala Asp His Ala Ala Pro Glu Asp Lys Tyr Glu 100 105 110 Ala Phe Val Leu His Phe Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr 115 120 125 Pro Glu Val His Ala Val Lys Pro Gly Ala 130 135 36957PRTPhleum pratense 369Ser Lys Ala Pro Gln Leu Val Pro Lys Leu Asp Glu Val Tyr Asn Ala 1 5 10 15 Ala Tyr Asn Ala Ala Asp His Ala Ala Pro Glu Asp Lys Tyr Glu Ala 20 25 30 Phe Val Leu His Phe Ser Glu Ala Leu His Ile Ile Ala Gly Thr Pro 35 40 45 Glu Val His Ala Val Lys Pro Gly Ala 50 55 37080PRTPhleum pratense 370Ala Asp Lys Tyr Lys Thr Phe Glu Ala Ala Phe Thr Val Ser Ser Lys 1 5 10 15 Arg Asn Leu Ala Asp Ala Val Ser Lys Ala Pro Gln Leu Val Pro Lys 20 25 30 Leu Asp Glu Val Tyr Asn Ala Ala Tyr Asn Ala Ala Asp His Ala Ala 35 40 45 Pro Glu Asp Lys Tyr Glu Ala Phe Val Leu His Phe Ser Glu Ala Leu 50 55 60 His Ile Ile Ala Gly Thr Pro Glu Val His Ala Val Lys Pro Gly Ala 65 70 75 80 371106PRTPhleum pratense 371Thr Glu Glu Gln Lys Leu Ile Glu Asp Val Asn Ala Ser Phe Arg Ala 1 5 10 15 Ala Met Ala Thr Thr Ala Asn Val Pro Pro Ala Asp Lys Tyr Lys Thr 20 25 30 Leu Glu Ala Ala Phe Thr Val Ser Ser Lys Arg Asn Leu Ala Asp Ala 35 40 45 Val Ser Lys Ala Pro Gln Leu Val Pro Lys Leu Asp Glu Val Tyr Asn 50 55 60 Ala Ala Tyr Asn Ala Ala Asp His Ala Ala Pro Glu Asp Lys Tyr Glu 65 70 75 80 Ala Phe Val Leu His Phe Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr 85 90 95 Pro Glu Val His Ala Val Lys Pro Gly Ala 100 105 372138PRTPhleum pratense 372Met Ala Ala His Lys Phe Met Val Ala Met Phe Leu Ala Val Ala Val 1 5 10 15 Val Leu Gly Leu Ala Thr Ser Pro Thr Ala Glu Gly Gly Lys Ala Thr 20 25 30 Thr Glu Glu Gln Lys Leu Ile Glu Asp Ile Asn Ala Ser Phe Arg Ala 35 40 45 Ala Met Ala Thr Thr Ala Asn Val Pro Pro Ala Asp Lys Tyr Lys Thr 50 55 60 Phe Glu Ala Ala Phe Thr Val Ser Ser Lys Arg Asn Leu Ala Asp Ala 65 70 75 80 Val Ser Lys Ala Pro Gln Leu Val Pro Lys Leu Asp Glu Val Tyr Asn 85 90 95 Ala Ala Tyr Asn Ala Ala Asp His Ala Ala Pro Glu Asp Lys Tyr Glu 100 105 110 Ala Phe Val Leu His Phe Ser Glu Ala Leu His Ile Ile Ala Gly Thr 115 120 125 Pro Glu Val His Ala Val Lys Pro Gly Ala 130 135 373132PRTPhleum pratense 373Met Val Ala Met Phe Leu Ala Val Ala Val Val Leu Gly Leu Ala Thr 1 5 10 15 Ser Pro Thr Ala Glu Gly Gly Lys Ala Thr Thr Glu Glu Gln Lys Leu 20 25 30 Ile Glu Asp Val Asn Ala Ser Phe Arg Ala Ala Met Ala Thr Thr Ala 35 40 45 Asn Val Pro Pro Ala Asp Lys Tyr Lys Thr Phe Glu Ala Ala Phe Thr 50 55 60 Val Ser Ser Lys Arg Asn Leu Ala Asp Ala Val Ser Lys Ala Pro Gln 65 70 75 80 Leu Val Pro Lys Leu Asp Glu Val Tyr Asn Ala Ala Tyr Asn Ala Ala 85 90 95 Asp His Ala Ala Pro Glu Asp Lys Tyr Glu Ala Phe Val Leu His Phe 100 105 110 Ser Glu Ala Leu Arg Ile Ile Ala Gly Thr Pro Glu Val His Ala Val 115 120 125 Lys Pro Gly Ala 130 37478PRTPhleum pratense 374Met Ala Asp Asp Met Glu Arg Ile Phe Lys Arg Phe Asp Thr Asn Gly 1 5 10 15 Asp Gly Lys Ile Ser Leu Ser Glu Leu Thr Asp Ala Leu Arg Thr Leu 20 25 30 Gly Ser Thr Ser Ala Asp Glu Val Gln Arg Met Met Ala Glu Ile Asp 35 40 45 Thr Asp Gly Asp Gly Phe Ile Asp Phe Asn Glu Phe Ile Ser Phe Cys 50 55 60 Asn Ala Asn Pro Gly Leu Met Lys Asp Val Ala Lys Val Phe 65 70 75 375131PRTPhleum pratense 375Met Ser Trp Gln Thr Tyr Val Asp Glu His Leu Met Cys Glu Ile Glu 1 5 10 15 Gly His His Leu Ala Ser Ala Ala Ile Leu Gly His Asp Gly Thr Val 20 25 30 Trp Ala Gln Ser Ala Asp Phe Pro Gln Phe Lys Pro Glu Glu Ile Thr 35 40 45 Gly Ile Met Lys Asp Phe Asp Glu Pro Gly His Leu Ala Pro Thr Gly 50 55 60 Met Phe Val Ala Gly Ala Lys Tyr Met Val Ile Gln Gly Glu Pro Gly 65 70 75 80 Arg Val Ile Arg Gly Lys Lys Gly Ala Gly Gly Ile Thr Ile Lys Lys 85 90 95 Thr Gly Gln Ala Leu Val Val Gly Ile Tyr Asp Glu Pro Met Thr Pro 100 105 110 Gly Gln Cys Asn Met Val Val Glu Arg Leu Gly Asp Tyr Leu Val Glu 115 120 125 Gln Gly Met 130 376227PRTVespula vulgaris 376Met Glu Ile Ser Gly Leu Val Tyr Leu Ile Ile Ile Val Thr Ile Ile 1 5 10 15 Asp Leu Pro Tyr Gly Lys Ala Asn Asn Tyr Cys Lys Ile Lys Cys Leu 20 25 30 Lys Gly Gly Val His Thr Ala Cys Lys Tyr Gly Ser Leu Lys Pro Asn 35 40 45 Cys Gly Asn Lys Val Val Val Ser Tyr Gly Leu Thr Lys Gln Glu Lys 50 55 60 Gln Asp Ile Leu Lys Glu His Asn Asp Phe Arg Gln Lys Ile Ala Arg 65 70 75 80 Gly Leu Glu Thr Arg Gly Asn Pro Gly Pro Gln Pro Pro Ala Lys Asn 85 90 95 Met Lys Asn Leu Val Trp Asn Asp Glu Leu Ala Tyr Val Ala Gln Val 100 105 110 Trp Ala Asn Gln Cys Gln Tyr Gly His Asp Thr Cys Arg Asp Val Ala 115 120 125 Lys Tyr Gln Val Gly Gln Asn Val Ala Leu Thr Gly Ser Thr Ala Ala 130 135 140 Lys Tyr Asp Asp Pro Val Lys Leu Val Lys Met Trp Glu Asp Glu Val 145 150 155 160 Lys Asp Tyr Asn Pro Lys Lys Lys Phe Ser Gly Asn Asp Phe Leu Lys 165 170 175 Thr Gly His Tyr Thr Gln Met Val Trp Ala Asn Thr Lys Glu Val Gly 180 185 190 Cys Gly Ser Ile Lys Tyr Ile Gln Glu Lys Trp His Lys His Tyr Leu 195 200 205 Val Cys Asn Tyr Gly Pro Ser Gly Asn Phe Met Asn Glu Glu Leu Tyr 210 215 220 Gln Thr Lys 225 377300PRTVespula maculifrons 377Gly Pro Lys Cys Pro Phe Asn Ser Asp Thr Val Ser Ile Ile Ile Glu 1 5 10 15 Thr Arg Glu Asn Arg Asn Arg Asp Leu Tyr Thr Leu Gln Thr Leu Gln 20 25 30 Asn His Pro Glu Phe Lys Lys Lys Thr Ile Thr Arg Pro Val Val Phe 35 40 45 Ile Thr His Gly Phe Thr Ser Ser Ala Ser Glu Lys Asn Phe Ile Asn 50 55 60 Leu Ala Lys Ala Leu Val Asp Lys Asp Asn Tyr Met Val Ile Ser Ile 65 70 75 80 Asp Trp Gln Thr Ala Ala Cys Thr Asn Glu Tyr Pro Gly Leu Lys Tyr 85 90 95 Ala Tyr Tyr Pro Thr Ala Ala Ser Asn Thr Arg Leu Val Gly Gln Tyr 100 105 110 Ile Ala Thr Ile Thr Gln Lys Leu Val Lys Asp Tyr Lys Ile Ser Met 115 120 125 Ala Asn Ile Arg Leu Ile Gly His Ser Leu Gly Ala His Val Ser Gly 130 135 140 Phe Ala Gly Lys Arg Val Gln Glu Leu Lys Leu Gly Lys Tyr Ser Glu 145 150 155 160 Ile Ile Gly Leu Asp Pro Ala Arg Pro Ser Phe Asp Ser Asn His Cys 165 170 175 Ser Glu Arg Leu Cys Glu Thr Asp Ala Glu Tyr Val Gln Ile Ile His 180 185 190 Thr Ser Asn Tyr Leu Gly Thr Glu Lys Ile Leu Gly Thr Val Asp Phe 195 200 205 Tyr Met Asn Asn Gly Lys Asn Asn Pro Gly Cys Gly Arg Phe Phe Ser 210 215 220 Glu Val Cys Ser His Thr Arg Ala Val Ile Tyr Met Ala Glu Cys Ile 225 230 235 240 Lys His Glu Cys Cys Leu Ile Gly Ile Pro Arg Ser Lys Ser Ser Gln 245 250 255 Pro Ile Ser Arg Cys Thr Lys Gln Glu Cys Val Cys Val Gly Leu Asn 260 265 270 Ala Lys Lys Tyr Pro Ser Arg Gly Ser Phe Tyr Val Pro Val Glu Ser 275 280 285 Thr Ala Pro Phe Cys Asn Asn Lys Gly Lys Ile Ile 290 295 300 378336PRTVespula vulgaris 378 Met Glu Glu Asn Met Asn Leu Lys Tyr Leu Leu Leu Phe Val Tyr Phe 1 5 10 15 Val Gln Val Leu Asn Cys Cys Tyr Gly His Gly Asp Pro Leu Ser Tyr 20 25 30 Glu Leu Asp Arg Gly Pro Lys Cys Pro Phe Asn Ser Asp Thr Val Ser 35 40 45 Ile Ile Ile Glu Thr Arg Glu Asn Arg Asn Arg Asp Leu Tyr Thr Leu 50 55 60 Gln Thr Leu Gln Asn His Pro Glu Phe Lys Lys Lys Thr Ile Thr Arg 65 70 75 80 Pro Val Val Phe Ile Thr His Gly Phe Thr Ser Ser Ala Ser Glu Thr 85 90 95 Asn Phe Ile Asn Leu Ala Lys Ala Leu Val Asp Lys Asp Asn Tyr Met 100 105 110 Val Ile Ser Ile Asp Trp Gln Thr Ala Ala Cys Thr Asn Glu Ala Ala 115 120 125 Gly Leu Lys Tyr Leu Tyr Tyr Pro Thr Ala Ala Arg Asn Thr Arg Leu 130 135 140 Val Gly Gln Tyr Ile Ala Thr Ile Thr Gln Lys Leu Val Lys His Tyr 145 150 155 160 Lys Ile Ser Met Ala Asn Ile Arg Leu Ile Gly His Ser Leu Gly Ala 165 170 175 His Ala Ser Gly Phe Ala Gly Lys Lys Val Gln Glu Leu Lys Leu Gly 180 185 190 Lys Tyr Ser Glu Ile Ile Gly Leu Asp Pro Ala Arg Pro Ser Phe Asp 195 200 205 Ser Asn His Cys Ser Glu Arg Leu Cys Glu Thr Asp Ala Glu Tyr Val 210 215 220 Gln Ile Ile His Thr Ser Asn Tyr Leu Gly Thr Glu Lys Thr Leu Gly 225 230 235 240 Thr Val Asp Phe Tyr Met Asn Asn Gly Lys Asn Gln Pro Gly Cys Gly 245 250 255 Arg Phe Phe Ser Glu Val Cys Ser His Ser Arg Ala Val Ile Tyr Met 260 265 270 Ala Glu Cys Ile Lys His Glu Cys Cys Leu Ile Gly Ile Pro Lys Ser 275 280 285 Lys Ser Ser Gln Pro Ile Ser Ser Cys Thr Lys Gln Glu Cys Val Cys 290 295 300 Val Gly Leu Asn Ala Lys Lys Tyr Pro Ser Arg Gly Ser Phe Tyr Val 305 310 315 320 Pro Val Glu Ser Thr Ala Pro Phe Cys Asn Asn Lys Gly Lys Ile Ile 325 330 335 379331PRTVespula vulgaris 379Ser Glu Arg Pro Lys Arg Val Phe Asn Ile Tyr Trp Asn Val Pro Thr 1 5 10 15 Phe Met Cys His Gln Tyr Asp Leu Tyr Phe Asp Glu Val Thr Asn Phe 20 25 30 Asn Ile Lys Arg Asn Ser Lys Asp Asp Phe Gln Gly Asp Lys Ile Ala 35 40 45 Ile Phe Tyr Asp Pro Gly Glu Phe Pro Ala Leu Leu Ser Leu Lys Asp 50 55 60 Gly Lys Tyr Lys Lys Arg Asn Gly Gly Val Pro Gln Glu Gly Asn Ile 65 70 75 80 Thr Ile His Leu Gln Lys Phe Ile Glu Asn Leu Asp Lys Ile Tyr Pro 85 90 95 Asn Arg Asn Phe Ser Gly Ile Gly Val Ile Asp Phe Glu Arg Trp Arg 100 105 110 Pro Ile Phe Arg Gln Asn Trp Gly Asn Met Lys Ile His Lys Asn Phe 115 120 125 Ser Ile Asp Leu Val Arg Asn Glu His Pro Thr Trp Asn Lys Lys Met 130 135 140 Ile Glu Leu Glu Ala Ser Lys Arg Phe Glu Lys Tyr Ala Arg Phe Phe 145 150 155 160 Met Glu Glu Thr Leu Lys Leu Ala Lys Lys Thr Arg Lys Gln Ala Asp 165 170 175 Trp Gly Tyr Tyr Gly Tyr Pro Tyr Cys Phe Asn Met Ser Pro Asn Asn 180 185 190 Leu Val Pro Glu Cys Asp Val Thr Ala Met His Glu Asn Asp Lys Met 195 200 205 Ser Trp Leu Phe Asn Asn Gln Asn Val Leu Leu Pro Ser Val Tyr Val 210 215 220 Arg Gln Glu Leu Thr Pro Asp Gln Arg Ile Gly Leu Val Gln Gly Arg 225 230 235 240 Val Lys Glu Ala Val Arg Ile Ser Asn Asn Leu Lys His Ser Pro Lys 245 250 255 Val Leu Ser Tyr Trp Trp Tyr Val Tyr Gln Asp Glu Thr Asn Thr Phe 260 265 270 Leu Thr Glu Thr Asp Val Lys Lys Thr Phe Gln Glu Ile Val Ile Asn 275 280 285 Gly Gly Asp Gly Ile Ile Ile Trp Gly Ser Ser Ser Asp Val Asn Ser 290 295 300 Leu Ser Lys Cys Lys Arg Leu Gln Asp Tyr Leu Leu Thr Val Leu Gly 305 310 315 320 Pro Ile Ala Ile Asn Val Thr Glu Ala Val Asn 325 330 380206PRTVespula vidua 380Lys Val Asn Tyr Cys Lys Ile Lys Cys Leu Lys Gly Gly Val His Thr 1 5 10 15 Ala Cys Lys Tyr Gly Thr Ser Thr Lys Pro Asn Cys Gly Lys Met Val 20 25 30 Val Lys Ala Tyr Gly Leu Thr Glu Ala Glu Lys Gln Glu Ile Leu Lys 35 40 45 Val

His Asn Asp Phe Arg Gln Lys Val Ala Lys Gly Leu Glu Thr Arg 50 55 60 Gly Asn Pro Gly Pro Gln Pro Pro Ala Lys Asn Met Asn Asn Leu Val 65 70 75 80 Trp Asn Asp Glu Leu Ala Asn Ile Ala Gln Val Trp Ala Ser Gln Cys 85 90 95 Asn Tyr Gly His Asp Thr Cys Lys Asp Thr Glu Lys Tyr Pro Val Gly 100 105 110 Gln Asn Ile Ala Lys Arg Ser Thr Thr Ala Ala Leu Phe Asp Ser Pro 115 120 125 Gly Lys Leu Val Lys Met Trp Glu Asn Glu Val Lys Asp Phe Asn Pro 130 135 140 Asn Ile Glu Trp Ser Lys Asn Asn Leu Lys Lys Thr Gly His Tyr Thr 145 150 155 160 Gln Met Val Trp Ala Lys Thr Lys Glu Ile Gly Cys Gly Ser Val Lys 165 170 175 Tyr Val Lys Asp Glu Trp Tyr Thr His Tyr Leu Val Cys Asn Tyr Gly 180 185 190 Pro Ser Gly Asn Phe Arg Asn Glu Lys Leu Tyr Glu Lys Lys 195 200 205 381160PRTBetula pendula 381Met Gly Val Phe Asn Tyr Glu Thr Glu Thr Thr Ser Val Ile Pro Ala 1 5 10 15 Ala Arg Leu Phe Lys Ala Phe Ile Leu Asp Gly Asp Asn Leu Phe Pro 20 25 30 Lys Val Ala Pro Gln Ala Ile Ser Ser Val Glu Asn Ile Glu Gly Asn 35 40 45 Gly Gly Pro Gly Thr Ile Lys Lys Ile Ser Phe Pro Glu Gly Phe Pro 50 55 60 Phe Lys Tyr Val Lys Asp Arg Val Asp Glu Val Asp His Thr Asn Phe 65 70 75 80 Lys Tyr Asn Tyr Ser Val Ile Glu Gly Gly Pro Ile Gly Asp Thr Leu 85 90 95 Glu Lys Ile Ser Asn Glu Ile Lys Ile Val Ala Thr Pro Asp Gly Gly 100 105 110 Ser Ile Leu Lys Ile Ser Asn Lys Tyr His Thr Lys Gly Asp His Glu 115 120 125 Val Lys Ala Glu Gln Val Lys Ala Ser Lys Glu Met Gly Glu Thr Leu 130 135 140 Leu Arg Ala Val Glu Ser Tyr Leu Leu Ala His Ser Asp Ala Tyr Asn 145 150 155 160 382133PRTBetula pendula 382Met Ser Trp Gln Thr Tyr Val Asp Glu His Leu Met Cys Asp Ile Asp 1 5 10 15 Gly Gln Ala Ser Asn Ser Leu Ala Ser Ala Ile Val Gly His Asp Gly 20 25 30 Ser Val Trp Ala Gln Ser Ser Ser Phe Pro Gln Phe Lys Pro Gln Glu 35 40 45 Ile Thr Gly Ile Met Lys Asp Phe Glu Glu Pro Gly His Leu Ala Pro 50 55 60 Thr Gly Leu His Leu Gly Gly Ile Lys Tyr Met Val Ile Gln Gly Glu 65 70 75 80 Ala Gly Ala Val Ile Arg Gly Lys Lys Gly Ser Gly Gly Ile Thr Ile 85 90 95 Lys Lys Thr Gly Gln Ala Leu Val Phe Gly Ile Tyr Glu Glu Pro Val 100 105 110 Thr Pro Gly Gln Cys Asn Met Val Val Glu Arg Leu Gly Asp Tyr Leu 115 120 125 Ile Asp Gln Gly Leu 130 383205PRTBetula pendula 383Met Pro Cys Ser Thr Glu Ala Met Glu Lys Ala Gly His Gly His Ala 1 5 10 15 Ser Thr Pro Arg Lys Arg Ser Leu Ser Asn Ser Ser Phe Arg Leu Arg 20 25 30 Ser Glu Ser Leu Asn Thr Leu Arg Leu Arg Arg Ile Phe Asp Leu Phe 35 40 45 Asp Lys Asn Ser Asp Gly Ile Ile Thr Val Asp Glu Leu Ser Arg Ala 50 55 60 Leu Asn Leu Leu Gly Leu Glu Thr Asp Leu Ser Glu Leu Glu Ser Thr 65 70 75 80 Val Lys Ser Phe Thr Arg Glu Gly Asn Ile Gly Leu Gln Phe Glu Asp 85 90 95 Phe Ile Ser Leu His Gln Ser Leu Asn Asp Ser Tyr Phe Ala Tyr Gly 100 105 110 Gly Glu Asp Glu Asp Asp Asn Glu Glu Asp Met Arg Lys Ser Ile Leu 115 120 125 Ser Gln Glu Glu Ala Asp Ser Phe Gly Gly Phe Lys Val Phe Asp Glu 130 135 140 Asp Gly Asp Gly Tyr Ile Ser Ala Arg Glu Leu Gln Met Val Leu Gly 145 150 155 160 Lys Leu Gly Phe Ser Glu Gly Ser Glu Ile Asp Arg Val Glu Lys Met 165 170 175 Ile Val Ser Val Asp Ser Asn Arg Asp Gly Arg Val Asp Phe Phe Glu 180 185 190 Phe Lys Asp Met Met Arg Ser Val Leu Val Arg Ser Ser 195 200 205 38485PRTBetula pendula 384Met Ala Asp Asp His Pro Gln Asp Lys Ala Glu Arg Glu Arg Ile Phe 1 5 10 15 Lys Arg Phe Asp Ala Asn Gly Asp Gly Lys Ile Ser Ala Ala Glu Leu 20 25 30 Gly Glu Ala Leu Lys Thr Leu Gly Ser Ile Thr Pro Asp Glu Val Lys 35 40 45 His Met Met Ala Glu Ile Asp Thr Asp Gly Asp Gly Phe Ile Ser Phe 50 55 60 Gln Glu Phe Thr Asp Phe Gly Arg Ala Asn Arg Gly Leu Leu Lys Asp 65 70 75 80 Val Ala Lys Ile Phe 85 38524PRTQuercus albaUNSURE(5)..(5)Xaa = unknown 385Gly Val Phe Thr Xaa Glu Ser Gln Glu Thr Ser Val Ile Ala Pro Ala 1 5 10 15 Xaa Leu Phe Lys Ala Leu Phe Leu 20 38640PRTCarpinus betulusUNSURE(39)..(39)Xaa = unknown 386Gly Val Phe Asn Tyr Glu Ala Glu Thr Pro Ser Val Ile Pro Ala Ala 1 5 10 15 Arg Leu Phe Lys Ser Tyr Val Leu Asp Gly Asp Lys Leu Ile Pro Lys 20 25 30 Val Ala Pro Gln Ala Ile Xaa Lys 35 40 38744PRTAlnus glutinosa 387Gly Val Phe Asn Tyr Glu Ala Glu Thr Pro Ser Val Ile Pro Ala Ala 1 5 10 15 Arg Leu Phe Lys Ala Phe Ile Leu Asp Gly Asp Lys Leu Leu Pro Lys 20 25 30 Val Ala Pro Glu Ala Val Ser Ser Val Glu Asn Ile 35 40 388110PRTBetula pendula 388Val Gln Cys Met Gln Val Trp Pro Pro Leu Gly Leu Lys Lys Phe Glu 1 5 10 15 Thr Leu Ser Tyr Leu Pro Pro Leu Ser Ser Glu Gln Leu Ala Lys Glu 20 25 30 Val Asp Tyr Leu Leu Arg Lys Asn Leu Ile Pro Cys Leu Glu Phe Glu 35 40 45 Leu Glu His Gly Phe Val Tyr Arg Glu His Asn Arg Ser Pro Gly Tyr 50 55 60 Tyr Asp Gly Arg Tyr Trp Thr Met Trp Lys Leu Pro Met Phe Gly Cys 65 70 75 80 Asn Asp Ser Ser Gln Val Leu Lys Glu Leu Glu Glu Cys Lys Lys Ala 85 90 95 Tyr Pro Ser Ala Phe Ile Arg Ile Ile Gly Phe Asp Asp Lys 100 105 110 389626PRTArachis hypogaea 389Met Arg Gly Arg Val Ser Pro Leu Met Leu Leu Leu Gly Ile Leu Val 1 5 10 15 Leu Ala Ser Val Ser Ala Thr His Ala Lys Ser Ser Pro Tyr Gln Lys 20 25 30 Lys Thr Glu Asn Pro Cys Ala Gln Arg Cys Leu Gln Ser Cys Gln Gln 35 40 45 Glu Pro Asp Asp Leu Lys Gln Lys Ala Cys Glu Ser Arg Cys Thr Lys 50 55 60 Leu Glu Tyr Asp Pro Arg Cys Val Tyr Asp Pro Arg Gly His Thr Gly 65 70 75 80 Thr Thr Asn Gln Arg Ser Pro Pro Gly Glu Arg Thr Arg Gly Arg Gln 85 90 95 Pro Gly Asp Tyr Asp Asp Asp Arg Arg Gln Pro Arg Arg Glu Glu Gly 100 105 110 Gly Arg Trp Gly Pro Ala Gly Pro Arg Glu Arg Glu Arg Glu Glu Asp 115 120 125 Trp Arg Gln Pro Arg Glu Asp Trp Arg Arg Pro Ser His Gln Gln Pro 130 135 140 Arg Lys Ile Arg Pro Glu Gly Arg Glu Gly Glu Gln Glu Trp Gly Thr 145 150 155 160 Pro Gly Ser His Val Arg Glu Glu Thr Ser Arg Asn Asn Pro Phe Tyr 165 170 175 Phe Pro Ser Arg Arg Phe Ser Thr Arg Tyr Gly Asn Gln Asn Gly Arg 180 185 190 Ile Arg Val Leu Gln Arg Phe Asp Gln Arg Ser Arg Gln Phe Gln Asn 195 200 205 Leu Gln Asn His Arg Ile Val Gln Ile Glu Ala Lys Pro Asn Thr Leu 210 215 220 Val Leu Pro Lys His Ala Asp Ala Asp Asn Ile Leu Val Ile Gln Gln 225 230 235 240 Gly Gln Ala Thr Val Thr Val Ala Asn Gly Asn Asn Arg Lys Ser Phe 245 250 255 Asn Leu Asp Glu Gly His Ala Leu Arg Ile Pro Ser Gly Phe Ile Ser 260 265 270 Tyr Ile Leu Asn Arg His Asp Asn Gln Asn Leu Arg Val Ala Lys Ile 275 280 285 Ser Met Pro Val Asn Thr Pro Gly Gln Phe Glu Asp Phe Phe Pro Ala 290 295 300 Ser Ser Arg Asp Gln Ser Ser Tyr Leu Gln Gly Phe Ser Arg Asn Thr 305 310 315 320 Leu Glu Ala Ala Phe Asn Ala Glu Phe Asn Glu Ile Arg Arg Val Leu 325 330 335 Leu Glu Glu Asn Ala Gly Gly Glu Gln Glu Glu Arg Gly Gln Arg Arg 340 345 350 Trp Ser Thr Arg Ser Ser Glu Asn Asn Glu Gly Val Ile Val Lys Val 355 360 365 Ser Lys Glu His Val Glu Glu Leu Thr Lys His Ala Lys Ser Val Ser 370 375 380 Lys Lys Gly Ser Glu Glu Glu Gly Asp Ile Thr Asn Pro Ile Asn Leu 385 390 395 400 Arg Glu Gly Glu Pro Asp Leu Ser Asn Asn Phe Gly Lys Leu Phe Glu 405 410 415 Val Lys Pro Asp Lys Lys Asn Pro Gln Leu Gln Asp Leu Asp Met Met 420 425 430 Leu Thr Cys Val Glu Ile Lys Glu Gly Ala Leu Met Leu Pro His Phe 435 440 445 Asn Ser Lys Ala Met Val Ile Val Val Val Asn Lys Gly Thr Gly Asn 450 455 460 Leu Glu Leu Val Ala Val Arg Lys Glu Gln Gln Gln Arg Gly Arg Arg 465 470 475 480 Glu Glu Glu Glu Asp Glu Asp Glu Glu Glu Glu Gly Ser Asn Arg Glu 485 490 495 Val Arg Arg Tyr Thr Ala Arg Leu Lys Glu Gly Asp Val Phe Ile Met 500 505 510 Pro Ala Ala His Pro Val Ala Ile Asn Ala Ser Ser Glu Leu His Leu 515 520 525 Leu Gly Phe Gly Ile Asn Ala Glu Asn Asn His Arg Ile Phe Leu Ala 530 535 540 Gly Asp Lys Asp Asn Val Ile Asp Gln Ile Glu Lys Gln Ala Lys Asp 545 550 555 560 Leu Ala Phe Pro Gly Ser Gly Glu Gln Val Glu Lys Leu Ile Lys Asn 565 570 575 Gln Lys Glu Ser His Phe Val Ser Ala Arg Pro Gln Ser Gln Ser Gln 580 585 590 Ser Pro Ser Ser Pro Glu Lys Glu Ser Pro Glu Lys Glu Asp Gln Glu 595 600 605 Glu Glu Asn Gln Gly Gly Lys Gly Pro Leu Leu Ser Ile Leu Lys Ala 610 615 620 Phe Asn 625 390392PRTAmbrosia artemisiifolia 390Met Gly Ile Lys His Cys Cys Tyr Ile Leu Tyr Phe Thr Leu Ala Leu 1 5 10 15 Val Thr Leu Leu Gln Pro Val Arg Ser Ala Glu Asp Leu Gln Gln Ile 20 25 30 Leu Pro Ser Ala Asn Glu Thr Arg Ser Leu Thr Thr Cys Gly Thr Tyr 35 40 45 Asn Ile Ile Asp Gly Cys Trp Arg Gly Lys Ala Asp Trp Ala Glu Asn 50 55 60 Arg Lys Ala Leu Ala Asp Cys Ala Gln Gly Phe Ala Lys Gly Thr Ile 65 70 75 80 Gly Gly Lys Asp Gly Asp Ile Tyr Thr Val Thr Ser Glu Leu Asp Asp 85 90 95 Asp Val Ala Asn Pro Lys Glu Gly Thr Leu Arg Phe Gly Ala Ala Gln 100 105 110 Asn Arg Pro Leu Trp Ile Ile Phe Ala Arg Asp Met Val Ile Arg Leu 115 120 125 Asp Arg Glu Leu Ala Ile Asn Asn Asp Lys Thr Ile Asp Gly Arg Gly 130 135 140 Ala Lys Val Glu Ile Ile Asn Ala Gly Phe Ala Ile Tyr Asn Val Lys 145 150 155 160 Asn Ile Ile Ile His Asn Ile Ile Met His Asp Ile Val Val Asn Pro 165 170 175 Gly Gly Leu Ile Lys Ser His Asp Gly Pro Pro Val Pro Arg Lys Gly 180 185 190 Ser Asp Gly Asp Ala Ile Gly Ile Ser Gly Gly Ser Gln Ile Trp Ile 195 200 205 Asp His Cys Ser Leu Ser Lys Ala Val Asp Gly Leu Ile Asp Ala Lys 210 215 220 His Gly Ser Thr His Phe Thr Val Ser Asn Cys Leu Phe Thr Gln His 225 230 235 240 Gln Tyr Leu Leu Leu Phe Trp Asp Phe Asp Glu Arg Gly Met Leu Cys 245 250 255 Thr Val Ala Phe Asn Lys Phe Thr Asp Asn Val Asp Gln Arg Met Pro 260 265 270 Asn Leu Arg His Gly Phe Val Gln Val Val Asn Asn Asn Tyr Glu Arg 275 280 285 Trp Gly Ser Tyr Ala Leu Gly Gly Ser Ala Gly Pro Thr Ile Leu Ser 290 295 300 Gln Gly Asn Arg Phe Leu Ala Ser Asp Ile Lys Lys Glu Val Val Gly 305 310 315 320 Arg Tyr Gly Glu Ser Ala Met Ser Glu Ser Ile Asn Trp Asn Trp Arg 325 330 335 Ser Tyr Met Asp Val Phe Glu Asn Gly Ala Ile Phe Val Pro Ser Gly 340 345 350 Val Asp Pro Val Leu Thr Pro Glu Gln Asn Ala Gly Met Ile Pro Ala 355 360 365 Glu Pro Gly Glu Ala Val Leu Arg Leu Thr Ser Ser Ala Gly Val Leu 370 375 380 Ser Cys Gln Pro Gly Ala Pro Cys 385 390 391397PRTAmbrosia artemisiifolia 391Met Gly Ile Lys His Cys Cys Tyr Ile Leu Tyr Phe Thr Leu Ala Leu 1 5 10 15 Val Thr Leu Val Gln Ala Gly Arg Leu Gly Glu Glu Val Asp Ile Leu 20 25 30 Pro Ser Pro Asn Asp Thr Arg Arg Ser Leu Gln Gly Cys Glu Ala His 35 40 45 Asn Ile Ile Asp Lys Cys Trp Arg Cys Lys Pro Asp Trp Ala Glu Asn 50 55 60 Arg Gln Ala Leu Gly Asn Cys Ala Gln Gly Phe Gly Lys Ala Thr His 65 70 75 80 Gly Gly Lys Trp Gly Asp Ile Tyr Met Val Thr Ser Asp Gln Asp Asp 85 90 95 Asp Val Val Asn Pro Lys Glu Gly Thr Leu Arg Phe Gly Ala Thr Gln 100 105 110 Asp Arg Pro Leu Trp Ile Ile Phe Gln Arg Asp Met Ile Ile Tyr Leu 115 120 125 Gln Gln Glu Met Val Val Thr Ser Asp Lys Thr Ile Asp Gly Arg Gly 130 135 140 Ala Lys Val Glu Leu Val Tyr Gly Gly Ile Thr Leu Met Asn Val Lys 145 150 155 160 Asn Val Ile Ile His Asn Ile Asp Ile His Asp Val Arg Val Leu Pro 165 170 175 Gly Gly Arg Ile Lys Ser Asn Gly Gly Pro Ala Ile Pro Arg His Gln 180 185 190 Ser Asp Gly Asp Ala Ile His Val Thr Gly Ser Ser Asp Ile Trp Ile 195 200 205 Asp His Cys Thr Leu Ser Lys Ser Phe Asp Gly Leu Val Asp Val Asn 210 215 220 Trp Gly Ser Thr Gly Val Thr Ile Ser Asn Cys Lys Phe Thr His His 225 230 235 240 Glu Lys Ala Val Leu Leu Gly Ala Ser Asp Thr His Phe Gln Asp Leu 245 250 255 Lys Met His Val Thr Leu Ala Tyr Asn Ile Phe Thr Asn Thr Val His 260 265 270 Glu Arg Met Pro Arg Cys Arg Phe Gly Phe Phe Gln Ile Val

Asn Asn 275 280 285 Phe Tyr Asp Arg Trp Asp Lys Tyr Ala Ile Gly Gly Ser Ser Asn Pro 290 295 300 Thr Ile Leu Ser Gln Gly Asn Lys Phe Val Ala Pro Asp Phe Ile Tyr 305 310 315 320 Lys Lys Asn Val Cys Leu Arg Thr Gly Ala Gln Glu Pro Glu Trp Met 325 330 335 Thr Trp Asn Trp Arg Thr Gln Asn Asp Val Leu Glu Asn Gly Ala Ile 340 345 350 Phe Val Ala Ser Gly Ser Asp Pro Val Leu Thr Ala Glu Gln Asn Ala 355 360 365 Gly Met Met Gln Ala Glu Pro Gly Asp Met Val Pro Gln Leu Thr Met 370 375 380 Asn Ala Gly Val Leu Thr Cys Ser Pro Gly Ala Pro Cys 385 390 395 392397PRTAmbrosia artemisiifolia 392Met Gly Ile Lys Gln Cys Cys Tyr Ile Leu Tyr Phe Thr Leu Ala Leu 1 5 10 15 Val Ala Leu Leu Gln Pro Val Arg Ser Ala Glu Gly Val Gly Glu Ile 20 25 30 Leu Pro Ser Val Asn Glu Thr Arg Ser Leu Gln Ala Cys Glu Ala Leu 35 40 45 Asn Ile Ile Asp Lys Cys Trp Arg Gly Lys Ala Asp Trp Glu Asn Asn 50 55 60 Arg Gln Ala Leu Ala Asp Cys Ala Gln Gly Phe Ala Lys Gly Thr Tyr 65 70 75 80 Gly Gly Lys Trp Gly Asp Val Tyr Thr Val Thr Ser Asn Leu Asp Asp 85 90 95 Asp Val Ala Asn Pro Lys Glu Gly Thr Leu Arg Phe Ala Ala Ala Gln 100 105 110 Asn Arg Pro Leu Trp Ile Ile Phe Lys Asn Asp Met Val Ile Asn Leu 115 120 125 Asn Gln Glu Leu Val Val Asn Ser Asp Lys Thr Ile Asp Gly Arg Gly 130 135 140 Val Lys Val Glu Ile Ile Asn Gly Gly Leu Thr Leu Met Asn Val Lys 145 150 155 160 Asn Ile Ile Ile His Asn Ile Asn Ile His Asp Val Lys Val Leu Pro 165 170 175 Gly Gly Met Ile Lys Ser Asn Asp Gly Pro Pro Ile Leu Arg Gln Ala 180 185 190 Ser Asp Gly Asp Thr Ile Asn Val Ala Gly Ser Ser Gln Ile Trp Ile 195 200 205 Asp His Cys Ser Leu Ser Lys Ser Phe Asp Gly Leu Val Asp Val Thr 210 215 220 Leu Gly Ser Thr His Val Thr Ile Ser Asn Cys Lys Phe Thr Gln Gln 225 230 235 240 Ser Lys Ala Ile Leu Leu Gly Ala Asp Asp Thr His Val Gln Asp Lys 245 250 255 Gly Met Leu Ala Thr Val Ala Phe Asn Met Phe Thr Asp Asn Val Asp 260 265 270 Gln Arg Met Pro Arg Cys Arg Phe Gly Phe Phe Gln Val Val Asn Asn 275 280 285 Asn Tyr Asp Arg Trp Gly Thr Tyr Ala Ile Gly Gly Ser Ser Ala Pro 290 295 300 Thr Ile Leu Cys Gln Gly Asn Arg Phe Leu Ala Pro Asp Asp Gln Ile 305 310 315 320 Lys Lys Asn Val Leu Ala Arg Thr Gly Thr Gly Ala Ala Glu Ser Met 325 330 335 Ala Trp Asn Trp Arg Ser Asp Lys Asp Leu Leu Glu Asn Gly Ala Ile 340 345 350 Phe Val Thr Ser Gly Ser Asp Pro Val Leu Thr Pro Val Gln Ser Ala 355 360 365 Gly Met Ile Pro Ala Glu Pro Gly Glu Ala Ala Ile Lys Leu Thr Ser 370 375 380 Ser Ala Gly Val Phe Ser Cys His Pro Gly Ala Pro Cys 385 390 395 393398PRTAmbrosia artemisiifolia 393Met Gly Ile Lys His Cys Cys Tyr Ile Leu Tyr Phe Thr Leu Ala Leu 1 5 10 15 Val Thr Leu Leu Gln Pro Val Arg Ser Ala Glu Asp Val Glu Glu Phe 20 25 30 Leu Pro Ser Ala Asn Glu Thr Arg Arg Ser Leu Lys Ala Cys Glu Ala 35 40 45 His Asn Ile Ile Asp Lys Cys Trp Arg Cys Lys Ala Asp Trp Ala Asn 50 55 60 Asn Arg Gln Ala Leu Ala Asp Cys Ala Gln Gly Phe Ala Lys Gly Thr 65 70 75 80 Tyr Gly Gly Lys His Gly Asp Val Tyr Thr Val Thr Ser Asp Lys Asp 85 90 95 Asp Asp Val Ala Asn Pro Lys Glu Gly Thr Leu Arg Phe Ala Ala Ala 100 105 110 Gln Asn Arg Pro Leu Trp Ile Ile Phe Lys Arg Asn Met Val Ile His 115 120 125 Leu Asn Gln Glu Leu Val Val Asn Ser Asp Lys Thr Ile Asp Gly Arg 130 135 140 Gly Val Lys Val Asn Ile Val Asn Ala Gly Leu Thr Leu Met Asn Val 145 150 155 160 Lys Asn Ile Ile Ile His Asn Ile Asn Ile His Asp Ile Lys Val Cys 165 170 175 Pro Gly Gly Met Ile Lys Ser Asn Asp Gly Pro Pro Ile Leu Arg Gln 180 185 190 Gln Ser Asp Gly Asp Ala Ile Asn Val Ala Gly Ser Ser Gln Ile Trp 195 200 205 Ile Asp His Cys Ser Leu Ser Lys Ala Ser Asp Gly Leu Leu Asp Ile 210 215 220 Thr Leu Gly Ser Ser His Val Thr Val Ser Asn Cys Lys Phe Thr Gln 225 230 235 240 His Gln Phe Val Leu Leu Leu Gly Ala Asp Asp Thr His Tyr Gln Asp 245 250 255 Lys Gly Met Leu Ala Thr Val Ala Phe Asn Met Phe Thr Asp His Val 260 265 270 Asp Gln Arg Met Pro Arg Cys Arg Phe Gly Phe Phe Gln Val Val Asn 275 280 285 Asn Asn Tyr Asp Arg Trp Gly Thr Tyr Ala Ile Gly Gly Ser Ser Ala 290 295 300 Pro Thr Ile Leu Ser Gln Gly Asn Arg Phe Phe Ala Pro Asp Asp Ile 305 310 315 320 Ile Lys Lys Asn Val Leu Ala Arg Thr Gly Thr Gly Asn Ala Glu Ser 325 330 335 Met Ser Trp Asn Trp Arg Thr Asp Arg Asp Leu Leu Glu Asn Gly Ala 340 345 350 Ile Phe Leu Pro Ser Gly Ser Asp Pro Val Leu Thr Pro Glu Gln Lys 355 360 365 Ala Gly Met Ile Pro Ala Glu Pro Gly Glu Ala Val Leu Arg Leu Thr 370 375 380 Ser Ser Ala Gly Val Leu Ser Cys His Gln Gly Ala Pro Cys 385 390 395 394396PRTAmbrosia artemisiifolia 394Met Gly Ile Lys His Cys Cys Tyr Ile Leu Tyr Phe Thr Leu Ala Leu 1 5 10 15 Val Thr Leu Leu Gln Pro Val Arg Ser Ala Glu Asp Leu Gln Glu Ile 20 25 30 Leu Pro Val Asn Glu Thr Arg Arg Leu Thr Thr Ser Gly Ala Tyr Asn 35 40 45 Ile Ile Asp Gly Cys Trp Arg Gly Lys Ala Asp Trp Ala Glu Asn Arg 50 55 60 Lys Ala Leu Ala Asp Cys Ala Gln Gly Phe Gly Lys Gly Thr Val Gly 65 70 75 80 Gly Lys Asp Gly Asp Ile Tyr Thr Val Thr Ser Glu Leu Asp Asp Asp 85 90 95 Val Ala Asn Pro Lys Glu Gly Thr Leu Arg Phe Gly Ala Ala Gln Asn 100 105 110 Arg Pro Leu Trp Ile Ile Phe Glu Arg Asp Met Val Ile Arg Leu Asp 115 120 125 Lys Glu Met Val Val Asn Ser Asp Lys Thr Ile Asp Gly Arg Gly Ala 130 135 140 Lys Val Glu Ile Ile Asn Ala Gly Phe Thr Leu Asn Gly Val Lys Asn 145 150 155 160 Val Ile Ile His Asn Ile Asn Met His Asp Val Lys Val Asn Pro Gly 165 170 175 Gly Leu Ile Lys Ser Asn Asp Gly Pro Ala Ala Pro Arg Ala Gly Ser 180 185 190 Asp Gly Asp Ala Ile Ser Ile Ser Gly Ser Ser Gln Ile Trp Ile Asp 195 200 205 His Cys Ser Leu Ser Lys Ser Val Asp Gly Leu Val Asp Ala Lys Leu 210 215 220 Gly Thr Thr Arg Leu Thr Val Ser Asn Ser Leu Phe Thr Gln His Gln 225 230 235 240 Phe Val Leu Leu Phe Gly Ala Gly Asp Glu Asn Ile Glu Asp Arg Gly 245 250 255 Met Leu Ala Thr Val Ala Phe Asn Thr Phe Thr Asp Asn Val Asp Gln 260 265 270 Arg Met Pro Arg Cys Arg His Gly Phe Phe Gln Val Val Asn Asn Asn 275 280 285 Tyr Asp Lys Trp Gly Ser Tyr Ala Ile Gly Gly Ser Ala Ser Pro Thr 290 295 300 Ile Leu Ser Gln Gly Asn Arg Phe Cys Ala Pro Asp Glu Arg Ser Lys 305 310 315 320 Lys Asn Val Leu Gly Arg His Gly Glu Ala Ala Ala Glu Ser Met Lys 325 330 335 Trp Asn Trp Arg Thr Asn Lys Asp Val Leu Glu Asn Gly Ala Ile Phe 340 345 350 Val Ala Ser Gly Val Asp Pro Val Leu Thr Pro Glu Gln Ser Ala Gly 355 360 365 Met Ile Pro Ala Glu Pro Gly Glu Ser Ala Leu Ser Leu Thr Ser Ser 370 375 380 Ala Gly Val Leu Ser Cys Gln Pro Gly Ala Pro Cys 385 390 395 395373PRTCryptomeria japonica 395Met Asp Ser Pro Cys Leu Val Ala Leu Leu Val Phe Ser Phe Val Ile 1 5 10 15 Gly Ser Cys Phe Ser Asp Asn Pro Ile Asp Ser Cys Trp Arg Gly Asp 20 25 30 Ser Asn Trp Ala Gln Asn Arg Met Lys Leu Ala Asp Cys Ala Val Gly 35 40 45 Phe Gly Ser Ser Thr Met Gly Gly Lys Gly Gly Asp Leu Tyr Thr Val 50 55 60 Thr Asn Ser Asp Asp Asp Pro Val Asn Pro Pro Gly Thr Leu Arg Tyr 65 70 75 80 Gly Ala Thr Arg Asp Arg Pro Leu Trp Ile Ile Phe Ser Gly Asn Met 85 90 95 Asn Ile Lys Leu Lys Met Pro Met Tyr Ile Ala Gly Tyr Lys Thr Phe 100 105 110 Asp Gly Arg Gly Ala Gln Val Tyr Ile Gly Asn Gly Gly Pro Cys Val 115 120 125 Phe Ile Lys Arg Val Ser Asn Val Ile Ile His Gly Leu Tyr Leu Tyr 130 135 140 Gly Cys Ser Thr Ser Val Leu Gly Asn Val Leu Ile Asn Glu Ser Phe 145 150 155 160 Gly Val Glu Pro Val His Pro Gln Asp Gly Asp Ala Leu Thr Leu Arg 165 170 175 Thr Ala Thr Asn Ile Trp Ile Asp His Asn Ser Phe Ser Asn Ser Ser 180 185 190 Asp Gly Leu Val Asp Val Thr Leu Thr Ser Thr Gly Val Thr Ile Ser 195 200 205 Asn Asn Leu Phe Phe Asn His His Lys Val Met Ser Leu Gly His Asp 210 215 220 Asp Ala Tyr Ser Asp Asp Lys Ser Met Lys Val Thr Val Ala Phe Asn 225 230 235 240 Gln Phe Gly Pro Asn Cys Gly Gln Arg Met Pro Arg Ala Arg Tyr Gly 245 250 255 Leu Val His Val Ala Asn Asn Asn Tyr Asp Pro Trp Thr Ile Tyr Ala 260 265 270 Ile Gly Gly Ser Ser Asn Pro Thr Ile Leu Ser Glu Gly Asn Ser Phe 275 280 285 Thr Ala Pro Asn Glu Ser Tyr Lys Lys Gln Val Thr Ile Arg Ile Gly 290 295 300 Cys Lys Thr Ser Ser Ser Cys Ser Asn Trp Val Trp Gln Ser Thr Gln 305 310 315 320 Asp Val Phe Tyr Asn Gly Ala Tyr Phe Val Ser Ser Gly Lys Tyr Glu 325 330 335 Gly Gly Asn Ile Tyr Thr Lys Lys Glu Ala Phe Asn Val Glu Asn Gly 340 345 350 Asn Ala Thr Pro His Leu Thr Gln Asn Ala Gly Val Leu Thr Cys Ser 355 360 365 Leu Ser Lys Arg Cys 370 396374PRTCryptomeria japonica 396Met Asp Ser Pro Cys Leu Val Ala Leu Leu Val Leu Ser Phe Val Ile 1 5 10 15 Gly Ser Cys Phe Ser Asp Asn Pro Ile Asp Ser Cys Trp Arg Gly Asp 20 25 30 Ser Asn Trp Ala Gln Asn Arg Met Lys Leu Ala Asp Cys Ala Val Gly 35 40 45 Phe Gly Ser Ser Thr Met Gly Gly Lys Gly Gly Asp Leu Tyr Thr Val 50 55 60 Thr Asn Ser Asp Asp Asp Pro Val Asn Pro Ala Pro Gly Thr Leu Arg 65 70 75 80 Tyr Gly Ala Thr Arg Asp Arg Pro Leu Trp Ile Ile Phe Ser Gly Asn 85 90 95 Met Asn Ile Lys Leu Lys Met Pro Met Tyr Ile Ala Gly Tyr Lys Thr 100 105 110 Phe Asp Gly Arg Gly Ala Gln Val Tyr Ile Gly Asn Gly Gly Pro Cys 115 120 125 Val Phe Ile Lys Arg Val Ser Asn Val Ile Ile His Gly Leu His Leu 130 135 140 Tyr Gly Cys Ser Thr Ser Val Leu Gly Asn Val Leu Ile Asn Glu Ser 145 150 155 160 Phe Gly Val Glu Pro Val His Pro Gln Asp Gly Asp Ala Leu Thr Leu 165 170 175 Arg Thr Ala Thr Asn Ile Trp Ile Asp His Asn Ser Phe Ser Asn Ser 180 185 190 Ser Asp Gly Leu Val Asp Val Thr Leu Ser Ser Thr Gly Val Thr Ile 195 200 205 Ser Asn Asn Leu Phe Phe Asn His His Lys Val Met Leu Leu Gly His 210 215 220 Asp Asp Ala Tyr Ser Asp Asp Lys Ser Met Lys Val Thr Val Ala Phe 225 230 235 240 Asn Gln Phe Gly Pro Asn Cys Gly Gln Arg Met Pro Arg Ala Arg Tyr 245 250 255 Gly Leu Val His Val Ala Asn Asn Asn Tyr Asp Pro Trp Thr Ile Tyr 260 265 270 Ala Ile Gly Gly Ser Ser Asn Pro Thr Ile Leu Ser Glu Gly Asn Ser 275 280 285 Phe Thr Ala Pro Asn Glu Ser Tyr Lys Lys Gln Val Thr Ile Arg Ile 290 295 300 Gly Cys Lys Thr Ser Ser Ser Cys Ser Asn Trp Val Trp Gln Ser Thr 305 310 315 320 Gln Asp Val Phe Tyr Asn Gly Ala Tyr Phe Val Ser Ser Gly Lys Tyr 325 330 335 Glu Gly Gly Asn Ile Tyr Thr Lys Lys Glu Ala Phe Asn Val Glu Asn 340 345 350 Gly Asn Ala Thr Pro Gln Leu Thr Lys Asn Ala Gly Val Leu Thr Cys 355 360 365 Ser Leu Ser Lys Arg Cys 370 397514PRTCryptomeria japonica 397 Met Ala Met Lys Leu Ile Ala Pro Met Ala Phe Leu Ala Met Gln Leu 1 5 10 15 Ile Ile Met Ala Ala Ala Glu Asp Gln Ser Ala Gln Ile Met Leu Asp 20 25 30 Ser Val Val Glu Lys Tyr Leu Arg Ser Asn Arg Ser Leu Arg Lys Val 35 40 45 Glu His Ser Arg His Asp Ala Ile Asn Ile Phe Asn Val Glu Lys Tyr 50 55 60 Gly Ala Val Gly Asp Gly Lys His Asp Cys Thr Glu Ala Phe Ser Thr 65 70 75 80 Ala Trp Gln Ala Ala Cys Lys Asn Pro Ser Ala Met Leu Leu Val Pro 85 90 95 Gly Ser Lys Lys Phe Val Val Asn Asn Leu Phe Phe Asn Gly Pro Cys 100 105 110 Gln Pro His Phe Thr Phe Lys Val Asp Gly Ile Ile Ala Ala Tyr Gln 115 120 125 Asn Pro Ala Ser Trp Lys Asn Asn Arg Ile Trp Leu Gln Phe Ala Lys 130 135 140 Leu Thr Gly Phe Thr Leu Met Gly Lys Gly Val Ile Asp Gly Gln Gly 145 150 155 160 Lys Gln Trp Trp Ala Gly Gln Cys Lys Trp Val Asn Gly Arg Glu Ile 165 170 175 Cys Asn Asp Arg Asp Arg Pro Thr Ala Ile Lys Phe Asp Phe Ser Thr 180 185 190 Gly Leu Ile Ile Gln Gly Leu Lys Leu Met Asn Ser Pro Glu Phe His 195 200 205 Leu Val Phe Gly Asn Cys Glu Gly Val Lys Ile Ile Gly Ile Ser Ile 210 215 220

Thr Ala Pro Arg Asp Ser Pro Asn Thr Asp Gly Ile Asp Ile Phe Ala 225 230 235 240 Ser Lys Asn Phe His Leu Gln Lys Asn Thr Ile Gly Thr Gly Asp Asp 245 250 255 Cys Val Ala Ile Gly Thr Gly Ser Ser Asn Ile Val Ile Glu Asp Leu 260 265 270 Ile Cys Gly Pro Gly His Gly Ile Ser Ile Gly Ser Leu Gly Arg Glu 275 280 285 Asn Ser Arg Ala Glu Val Ser Tyr Val His Val Asn Gly Ala Lys Phe 290 295 300 Ile Asp Thr Gln Asn Gly Leu Arg Ile Lys Thr Trp Gln Gly Gly Ser 305 310 315 320 Gly Met Ala Ser His Ile Ile Tyr Glu Asn Val Glu Met Ile Asn Ser 325 330 335 Glu Asn Pro Ile Leu Ile Asn Gln Phe Tyr Cys Thr Ser Ala Ser Ala 340 345 350 Cys Gln Asn Gln Arg Ser Ala Val Gln Ile Gln Asp Val Thr Tyr Lys 355 360 365 Asn Ile Arg Gly Thr Ser Ala Thr Ala Ala Ala Ile Gln Leu Lys Cys 370 375 380 Ser Asp Ser Met Pro Cys Lys Asp Ile Lys Leu Ser Asp Ile Ser Leu 385 390 395 400 Lys Leu Thr Ser Gly Lys Ile Ala Ser Cys Leu Asn Asp Asn Ala Asn 405 410 415 Gly Tyr Phe Ser Gly His Val Ile Pro Ala Cys Lys Asn Leu Ser Pro 420 425 430 Ser Ala Lys Arg Lys Glu Ser Lys Ser His Lys His Pro Lys Thr Val 435 440 445 Met Val Glu Asn Met Arg Ala Tyr Asp Lys Gly Asn Arg Thr Arg Ile 450 455 460 Leu Leu Gly Ser Arg Pro Pro Asn Cys Thr Asn Lys Cys His Gly Cys 465 470 475 480 Ser Pro Cys Lys Ala Lys Leu Val Ile Val His Arg Ile Met Pro Gln 485 490 495 Glu Tyr Tyr Pro Gln Arg Trp Ile Cys Ser Cys His Gly Lys Ile Tyr 500 505 510 His Pro 398514PRTCryptomeria japonica 398Met Ala Met Lys Phe Ile Ala Pro Met Ala Phe Val Ala Met Gln Leu 1 5 10 15 Ile Ile Met Ala Ala Ala Glu Asp Gln Ser Ala Gln Ile Met Leu Asp 20 25 30 Ser Asp Ile Glu Gln Tyr Leu Arg Ser Asn Arg Ser Leu Arg Lys Val 35 40 45 Glu His Ser Arg His Asp Ala Ile Asn Ile Phe Asn Val Glu Lys Tyr 50 55 60 Gly Ala Val Gly Asp Gly Lys His Asp Cys Thr Glu Ala Phe Ser Thr 65 70 75 80 Ala Trp Gln Ala Ala Cys Lys Lys Pro Ser Ala Met Leu Leu Val Pro 85 90 95 Gly Asn Lys Lys Phe Val Val Asn Asn Leu Phe Phe Asn Gly Pro Cys 100 105 110 Gln Pro His Phe Thr Phe Lys Val Asp Gly Ile Ile Ala Ala Tyr Gln 115 120 125 Asn Pro Ala Ser Trp Lys Asn Asn Arg Ile Trp Leu Gln Phe Ala Lys 130 135 140 Leu Thr Gly Phe Thr Leu Met Gly Lys Gly Val Ile Asp Gly Gln Gly 145 150 155 160 Lys Gln Trp Trp Ala Gly Gln Cys Lys Trp Val Asn Gly Arg Glu Ile 165 170 175 Cys Asn Asp Arg Asp Arg Pro Thr Ala Ile Lys Phe Asp Phe Ser Thr 180 185 190 Gly Leu Ile Ile Gln Gly Leu Lys Leu Met Asn Ser Pro Glu Phe His 195 200 205 Leu Val Phe Gly Asn Cys Glu Gly Val Lys Ile Ile Gly Ile Ser Ile 210 215 220 Thr Ala Pro Arg Asp Ser Pro Asn Thr Asp Gly Ile Asp Ile Phe Ala 225 230 235 240 Ser Lys Asn Phe His Leu Gln Lys Asn Thr Ile Gly Thr Gly Asp Asp 245 250 255 Cys Val Ala Ile Gly Thr Gly Ser Ser Asn Ile Val Ile Glu Asp Leu 260 265 270 Ile Cys Gly Pro Gly His Gly Ile Ser Ile Gly Ser Leu Gly Arg Glu 275 280 285 Asn Ser Arg Ala Glu Val Ser Tyr Val His Val Asn Gly Ala Lys Phe 290 295 300 Ile Asp Thr Gln Asn Gly Leu Arg Ile Lys Thr Trp Gln Gly Gly Ser 305 310 315 320 Gly Met Ala Ser His Ile Ile Tyr Glu Asn Val Glu Met Ile Asn Ser 325 330 335 Glu Asn Pro Ile Leu Ile Asn Gln Phe Tyr Cys Thr Ser Ala Ser Ala 340 345 350 Cys Gln Asn Gln Arg Ser Ala Val Gln Ile Gln Asp Val Thr Tyr Lys 355 360 365 Asn Ile Arg Gly Thr Ser Ala Thr Ala Ala Ala Ile Gln Leu Lys Cys 370 375 380 Ser Asp Ser Met Pro Cys Lys Asp Ile Lys Leu Ser Asp Ile Ser Leu 385 390 395 400 Lys Leu Thr Ser Gly Lys Ile Ala Ser Cys Leu Asn Asp Asn Ala Asn 405 410 415 Gly Tyr Phe Ser Gly His Val Ile Pro Ala Cys Lys Asn Leu Ser Pro 420 425 430 Ser Ala Lys Arg Lys Glu Ser Lys Ser His Lys His Pro Lys Thr Val 435 440 445 Met Val Lys Asn Met Gly Ala Tyr Asp Lys Gly Asn Arg Thr Arg Ile 450 455 460 Leu Leu Gly Ser Arg Pro Pro Asn Cys Thr Asn Lys Cys His Gly Cys 465 470 475 480 Ser Pro Cys Lys Ala Lys Leu Val Ile Val His Arg Ile Met Pro Gln 485 490 495 Glu Tyr Tyr Pro Gln Arg Trp Met Cys Ser Arg His Gly Lys Ile Tyr 500 505 510 His Pro 399373PRTCryptomeria japonica 399Met Asp Ser Pro Cys Leu Val Ala Leu Leu Val Leu Ser Phe Val Ile 1 5 10 15 Gly Ser Cys Phe Ser Asp Asn Pro Ile Asp Ser Cys Trp Arg Gly Asp 20 25 30 Ser Asn Trp Ala Gln Asn Arg Met Lys Leu Ala Asp Cys Ala Val Gly 35 40 45 Phe Gly Ser Ser Thr Met Gly Gly Lys Gly Gly Asp Leu Tyr Thr Val 50 55 60 Thr Asn Ser Asp Asp Asp Pro Val Asn Pro Pro Gly Thr Leu Arg Tyr 65 70 75 80 Gly Ala Thr Arg Asp Arg Pro Leu Trp Ile Ile Phe Ser Gly Asn Met 85 90 95 Asn Ile Lys Leu Lys Met Pro Met Tyr Ile Ala Gly Tyr Lys Thr Phe 100 105 110 Asp Gly Arg Gly Ala Gln Val Tyr Ile Gly Asn Gly Gly Pro Cys Val 115 120 125 Phe Ile Lys Arg Val Ser Asn Val Ile Ile His Gly Leu His Leu Tyr 130 135 140 Gly Cys Ser Thr Ser Val Leu Gly Asn Val Leu Ile Asn Glu Ser Phe 145 150 155 160 Gly Val Glu Pro Val His Pro Gln Asp Gly Asp Ala Leu Thr Leu Arg 165 170 175 Thr Ala Thr Asn Ile Trp Ile Asp His Asn Ser Phe Ser Asn Ser Ser 180 185 190 Asp Gly Leu Val Asp Val Thr Leu Ser Ser Thr Gly Val Thr Ile Ser 195 200 205 Asn Asn Leu Phe Phe Asn His His Lys Val Met Leu Leu Gly His Asp 210 215 220 Asp Ala Tyr Ser Asp Asp Lys Ser Met Lys Val Thr Val Ala Phe Asn 225 230 235 240 Gln Phe Gly Pro Asn Cys Gly Gln Arg Met Pro Arg Ala Arg Tyr Gly 245 250 255 Leu Val His Val Ala Asn Asn Asn Tyr Asp Pro Trp Thr Ile Tyr Ala 260 265 270 Ile Gly Gly Ser Ser Asn Pro Thr Ile Leu Ser Glu Gly Asn Ser Phe 275 280 285 Thr Ala Pro Asn Glu Ser Tyr Lys Lys Gln Val Thr Ile Arg Ile Gly 290 295 300 Cys Lys Thr Ser Ser Ser Cys Ser Asn Trp Val Trp Gln Ser Thr Gln 305 310 315 320 Asp Val Phe Tyr Asn Gly Ala Tyr Phe Val Ser Ser Gly Lys Tyr Glu 325 330 335 Gly Gly Asn Ile Tyr Thr Lys Lys Glu Ala Phe Asn Val Glu Asn Gly 340 345 350 Asn Ala Thr Pro Gln Leu Thr Lys Asn Ala Gly Val Leu Thr Cys Ser 355 360 365 Leu Ser Lys Arg Cys 370 400374PRTCryptomeria japonica 400Met Asp Ser Pro Cys Leu Val Ala Leu Leu Val Phe Ser Phe Val Ile 1 5 10 15 Gly Ser Cys Phe Ser Asp Asn Pro Ile Asp Ser Cys Trp Arg Gly Asp 20 25 30 Ser Asn Trp Ala Gln Asn Arg Met Lys Leu Ala Asp Cys Ala Val Gly 35 40 45 Phe Gly Ser Ser Thr Met Gly Gly Lys Gly Gly Asp Leu Tyr Thr Val 50 55 60 Thr Asn Ser Asp Asp Asp Pro Val Asn Pro Ala Pro Gly Thr Leu Arg 65 70 75 80 Tyr Gly Ala Thr Arg Asp Arg Pro Leu Trp Ile Ile Phe Ser Gly Asn 85 90 95 Met Asn Ile Lys Leu Lys Met Pro Met Tyr Ile Ala Gly Tyr Lys Thr 100 105 110 Phe Asp Gly Arg Gly Ala Gln Val Tyr Ile Gly Asn Gly Gly Pro Cys 115 120 125 Val Phe Ile Lys Arg Val Ser Asn Val Ile Ile His Gly Leu Tyr Leu 130 135 140 Tyr Gly Cys Ser Thr Ser Val Leu Gly Asn Val Leu Ile Asn Glu Ser 145 150 155 160 Phe Gly Val Glu Pro Val His Pro Gln Asp Gly Asp Ala Leu Thr Leu 165 170 175 Arg Thr Ala Thr Asn Ile Trp Ile Asp His Asn Ser Phe Ser Asn Ser 180 185 190 Ser Asp Gly Leu Val Asp Val Thr Leu Thr Ser Thr Gly Val Thr Ile 195 200 205 Ser Asn Asn Leu Phe Phe Asn His His Lys Val Met Ser Leu Gly His 210 215 220 Asp Asp Ala Tyr Ser Asp Asp Lys Ser Met Lys Val Thr Val Ala Phe 225 230 235 240 Asn Gln Phe Gly Pro Asn Cys Gly Gln Arg Met Pro Arg Ala Arg Tyr 245 250 255 Gly Leu Val His Val Ala Asn Asn Asn Tyr Asp Pro Trp Thr Ile Tyr 260 265 270 Ala Ile Gly Gly Ser Ser Asn Pro Thr Ile Leu Ser Glu Gly Asn Ser 275 280 285 Phe Thr Ala Pro Asn Glu Ser Tyr Lys Lys Gln Val Thr Ile Arg Ile 290 295 300 Gly Cys Lys Thr Ser Ser Ser Cys Ser Asn Trp Val Trp Gln Ser Thr 305 310 315 320 Gln Asp Val Phe Tyr Asn Gly Ala Tyr Phe Val Ser Ser Gly Lys Tyr 325 330 335 Glu Gly Gly Asn Ile Tyr Thr Lys Lys Glu Ala Phe Asn Val Glu Asn 340 345 350 Gly Asn Ala Thr Pro His Leu Thr Gln Asn Ala Gly Val Leu Thr Cys 355 360 365 Ser Leu Ser Lys Arg Cys 370 401174PRTCanis familiaris 401Met Lys Thr Leu Leu Leu Thr Ile Gly Phe Ser Leu Ile Ala Ile Leu 1 5 10 15 Gln Ala Gln Asp Thr Pro Ala Leu Gly Lys Asp Thr Val Ala Val Ser 20 25 30 Gly Lys Trp Tyr Leu Lys Ala Met Thr Ala Asp Gln Glu Val Pro Glu 35 40 45 Lys Pro Asp Ser Val Thr Pro Met Ile Leu Lys Ala Gln Lys Gly Gly 50 55 60 Asn Leu Glu Ala Lys Ile Thr Met Leu Thr Asn Gly Gln Cys Gln Asn 65 70 75 80 Ile Thr Val Val Leu His Lys Thr Ser Glu Pro Gly Lys Tyr Thr Ala 85 90 95 Tyr Glu Gly Gln Arg Val Val Phe Ile Gln Pro Ser Pro Val Arg Asp 100 105 110 His Tyr Ile Leu Tyr Cys Glu Gly Glu Leu His Gly Arg Gln Ile Arg 115 120 125 Met Ala Lys Leu Leu Gly Arg Asp Pro Glu Gln Ser Gln Glu Ala Leu 130 135 140 Glu Asp Phe Arg Glu Phe Ser Arg Ala Lys Gly Leu Asn Gln Glu Ile 145 150 155 160 Leu Glu Leu Ala Gln Ser Glu Thr Cys Ser Pro Gly Gly Gln 165 170 40224PRTCanis familiaris 402Glu Ala Tyr Lys Ser Glu Ile Ala His Arg Tyr Asn Asp Leu Gly Glu 1 5 10 15 Glu His Phe Arg Gly Leu Val Leu 20 403265PRTCanis familiaris 403Leu Ser Ser Ala Lys Glu Arg Phe Lys Cys Ala Ser Leu Gln Lys Phe 1 5 10 15 Gly Asp Arg Ala Phe Lys Ala Trp Ser Val Ala Arg Leu Ser Gln Arg 20 25 30 Phe Pro Lys Ala Asp Phe Ala Glu Ile Ser Lys Val Val Thr Asp Leu 35 40 45 Thr Lys Val His Lys Glu Cys Cys His Gly Asp Leu Leu Glu Cys Ala 50 55 60 Asp Asp Arg Ala Asp Leu Ala Lys Tyr Met Cys Glu Asn Gln Asp Ser 65 70 75 80 Ile Ser Thr Lys Leu Lys Glu Cys Cys Asp Lys Pro Val Leu Glu Lys 85 90 95 Ser Gln Cys Leu Ala Glu Val Glu Arg Asp Glu Leu Pro Gly Asp Leu 100 105 110 Pro Ser Leu Ala Ala Asp Phe Val Glu Asp Lys Glu Val Cys Lys Asn 115 120 125 Tyr Gln Glu Ala Lys Asp Val Phe Leu Gly Thr Phe Leu Tyr Glu Tyr 130 135 140 Ser Arg Arg His Pro Glu Tyr Ser Val Ser Leu Leu Leu Arg Leu Ala 145 150 155 160 Lys Glu Tyr Glu Ala Thr Leu Glu Lys Cys Cys Ala Thr Asp Asp Pro 165 170 175 Pro Thr Cys Tyr Ala Lys Val Leu Asp Glu Phe Lys Pro Leu Val Asp 180 185 190 Glu Pro Gln Asn Leu Val Lys Thr Asn Cys Glu Leu Phe Glu Lys Leu 195 200 205 Gly Glu Tyr Gly Phe Gln Asn Ala Leu Leu Val Arg Tyr Thr Lys Lys 210 215 220 Ala Pro Gln Val Ser Thr Pro Thr Leu Val Val Glu Val Ser Arg Lys 225 230 235 240 Leu Gly Lys Val Gly Thr Lys Cys Cys Lys Lys Pro Glu Ser Glu Arg 245 250 255 Met Ser Cys Ala Asp Asp Phe Leu Ser 260 265 404180PRTCanis familiaris 404Met Gln Leu Leu Leu Leu Thr Val Gly Leu Ala Leu Ile Cys Gly Leu 1 5 10 15 Gln Ala Gln Glu Gly Asn His Glu Glu Pro Gln Gly Gly Leu Glu Glu 20 25 30 Leu Ser Gly Arg Trp His Ser Val Ala Leu Ala Ser Asn Lys Ser Asp 35 40 45 Leu Ile Lys Pro Trp Gly His Phe Arg Val Phe Ile His Ser Met Ser 50 55 60 Ala Lys Asp Gly Asn Leu His Gly Asp Ile Leu Ile Pro Gln Asp Gly 65 70 75 80 Gln Cys Glu Lys Val Ser Leu Thr Ala Phe Lys Thr Ala Thr Ser Asn 85 90 95 Lys Phe Asp Leu Glu Tyr Trp Gly His Asn Asp Leu Tyr Leu Ala Glu 100 105 110 Val Asp Pro Lys Ser Tyr Leu Ile Leu Tyr Met Ile Asn Gln Tyr Asn 115 120 125 Asp Asp Thr Ser Leu Val Ala His Leu Met Val Arg Asp Leu Ser Arg 130 135 140 Gln Gln Asp Phe Leu Pro Ala Phe Glu Ser Val Cys Glu Asp Ile Gly 145 150 155 160 Leu His Lys Asp Gln Ile Val Val Leu Ser Asp Asp Asp Arg Cys Gln 165 170 175 Gly Ser Arg Asp 180 405187PRTEquus caballus 405Met Lys Leu Leu Leu Leu Cys Leu Gly Leu Ile Leu Val Cys Ala Gln 1 5 10 15 Gln Glu Glu Asn Ser Asp Val Ala Ile Arg Asn Phe Asp Ile Ser Lys 20 25 30 Ile Ser Gly Glu Trp Tyr Ser Ile Phe Leu Ala Ser Asp Val Lys Glu 35 40 45 Lys Ile Glu Glu Asn Gly Ser Met Arg Val Phe Val Asp Val Ile Arg 50 55 60 Ala Leu Asp Asn Ser Ser Leu Tyr Ala Glu Tyr Gln Thr Lys Val Asn 65 70 75

80 Gly Glu Cys Thr Glu Phe Pro Met Val Phe Asp Lys Thr Glu Glu Asp 85 90 95 Gly Val Tyr Ser Leu Asn Tyr Asp Gly Tyr Asn Val Phe Arg Ile Ser 100 105 110 Glu Phe Glu Asn Asp Glu His Ile Ile Leu Tyr Leu Val Asn Phe Asp 115 120 125 Lys Asp Arg Pro Phe Gln Leu Phe Glu Phe Tyr Ala Arg Glu Pro Asp 130 135 140 Val Ser Pro Glu Ile Lys Glu Glu Phe Val Lys Ile Val Gln Lys Arg 145 150 155 160 Gly Ile Val Lys Glu Asn Ile Ile Asp Leu Thr Lys Ile Asp Arg Cys 165 170 175 Phe Gln Leu Arg Gly Asn Gly Val Ala Gln Ala 180 185 40629PRTEquus caballusUNSURE(3)..(3)Xaa = unknown 406Ser Gln Xaa Pro Gln Ser Glu Thr Asp Tyr Ser Gln Leu Ser Gly Glu 1 5 10 15 Trp Asn Thr Ile Tyr Gly Ala Ala Ser Asn Ile Xaa Lys 20 25 407211PRTEuroglyphus maynei 407Thr Tyr Ala Cys Ser Ile Asn Ser Val Ser Leu Pro Ser Glu Leu Asp 1 5 10 15 Leu Arg Ser Leu Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly Cys 20 25 30 Gly Ser Cys Trp Ala Phe Ser Gly Val Ala Ser Thr Glu Ser Ala Tyr 35 40 45 Leu Ala Tyr Arg Asn Met Ser Leu Asp Leu Ala Glu Gln Glu Leu Val 50 55 60 Asp Cys Ala Ser Gln Asn Gly Cys His Gly Asp Thr Ile Pro Arg Gly 65 70 75 80 Ile Glu Tyr Ile Gln Gln Asn Gly Val Val Gln Glu His Tyr Tyr Pro 85 90 95 Tyr Val Ala Arg Glu Gln Ser Cys His Arg Pro Asn Ala Gln Arg Tyr 100 105 110 Gly Leu Lys Asn Tyr Cys Gln Ile Ser Pro Pro Asp Ser Asn Lys Ile 115 120 125 Arg Gln Ala Leu Thr Gln Thr His Thr Ala Val Ala Val Ile Ile Gly 130 135 140 Ile Lys Asp Leu Asn Ala Phe Arg His Tyr Asp Gly Arg Thr Ile Met 145 150 155 160 Gln His Asp Asn Gly Tyr Gln Pro Asn Tyr His Ala Val Asn Ile Val 165 170 175 Gly Tyr Gly Asn Thr Gln Gly Val Asp Tyr Trp Ile Val Arg Asn Ser 180 185 190 Trp Asp Thr Thr Trp Gly Asp Asn Gly Tyr Gly Tyr Phe Ala Ala Asn 195 200 205 Ile Asn Leu 210 408211PRTEuroglyphus maynei 408Thr Tyr Ala Cys Ser Ile Asn Ser Val Ser Leu Pro Ser Glu Leu Asp 1 5 10 15 Leu Arg Ser Leu Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly Cys 20 25 30 Gly Ser Cys Trp Ala Phe Ser Gly Val Ala Ser Thr Glu Ser Ala Tyr 35 40 45 Leu Ala Tyr Arg Asn Met Ser Leu Asp Leu Ala Glu Gln Glu Leu Val 50 55 60 Asp Cys Ala Ser Gln Asn Gly Cys His Gly Asp Thr Ile Pro Arg Gly 65 70 75 80 Ile Glu Tyr Ile Gln Gln Asn Gly Val Val Gln Glu His Tyr Tyr Pro 85 90 95 Tyr Val Ala Arg Glu Gln Ser Cys His Arg Pro Asn Ala Gln Arg Tyr 100 105 110 Gly Leu Lys Asn Tyr Cys Gln Ile Ser Pro Pro Asp Ser Asn Lys Ile 115 120 125 Arg Gln Ala Leu Thr Gln Thr His Thr Ala Val Ala Val Ile Ile Gly 130 135 140 Ile Lys Asp Leu Asn Ala Phe Arg His Tyr Asp Gly Arg Thr Ile Met 145 150 155 160 Gln His Asp Asn Gly Tyr Gln Pro Asn Tyr His Ala Val Asn Ile Val 165 170 175 Gly Tyr Gly Asn Thr Gln Gly Val Asp Tyr Trp Ile Val Arg Asn Ser 180 185 190 Trp Asp Thr Thr Trp Gly Asp Asn Gly Tyr Gly Tyr Phe Ala Ala Asn 195 200 205 Ile Asn Leu 210 409211PRTEuroglyphus maynei 409 Glu Thr Asn Ala Cys Ser Ile Asn Gly Asn Ala Pro Ala Glu Ile Asp 1 5 10 15 Leu Arg Gln Met Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly Cys 20 25 30 Gly Ser Cys Trp Ala Phe Ser Gly Val Ala Ala Thr Glu Ser Ala Tyr 35 40 45 Leu Ala Tyr Arg Asn Gln Ser Leu Asp Leu Ala Glu Gln Glu Leu Val 50 55 60 Asp Cys Ala Ser Gln His Gly Cys His Gly Asp Thr Ile Pro Arg Gly 65 70 75 80 Ile Glu Tyr Ile Gln His Asn Gly Val Val Gln Glu Ser Tyr Tyr Arg 85 90 95 Tyr Val Ala Arg Glu Gln Ser Cys Arg Arg Pro Asn Ala Gln Arg Phe 100 105 110 Gly Ile Ser Asn Tyr Cys Gln Ile Tyr Pro Pro Asn Ala Asn Lys Ile 115 120 125 Arg Glu Ala Leu Ala Gln Thr His Ser Ala Ile Ala Val Ile Ile Gly 130 135 140 Ile Lys Asp Leu Asp Ala Phe Arg His Tyr Asp Gly Arg Thr Ile Ile 145 150 155 160 Gln Arg Asp Asn Gly Tyr Gln Pro Asn Tyr His Ala Val Asn Ile Val 165 170 175 Gly Tyr Ser Asn Ala Gln Gly Val Asp Tyr Trp Ile Val Arg Asn Ser 180 185 190 Trp Asp Thr Asn Trp Gly Asp Asn Gly Tyr Gly Tyr Phe Ala Ala Asn 195 200 205 Ile Asp Leu 210 410212PRTEuroglyphus maynei 410Glu Thr Ser Ala Cys Arg Ile Asn Ser Val Asn Val Pro Ser Glu Leu 1 5 10 15 Asp Leu Arg Ser Leu Arg Thr Val Thr Pro Ile Arg Met Gln Gly Gly 20 25 30 Cys Gly Ser Cys Trp Ala Phe Ser Gly Val Ala Ala Thr Glu Ser Ala 35 40 45 Tyr Leu Ala Tyr Arg Asn Thr Ser Leu Asp Leu Ser Glu Gln Glu Leu 50 55 60 Val Asp Cys Ala Ser Gln His Gly Cys His Gly Asp Thr Ile Pro Arg 65 70 75 80 Gly Ile Glu Tyr Ile Gln Gln Asn Gly Val Val Glu Glu Arg Ser Tyr 85 90 95 Pro Tyr Val Ala Arg Glu Gln Gln Cys Arg Arg Pro Asn Ser Gln His 100 105 110 Tyr Gly Ile Ser Asn Tyr Cys Gln Ile Tyr Pro Pro Asp Val Lys Gln 115 120 125 Ile Arg Glu Ala Leu Thr Gln Thr His Thr Ala Ile Ala Val Ile Ile 130 135 140 Gly Ile Lys Asp Leu Arg Ala Phe Gln His Tyr Asp Gly Arg Thr Ile 145 150 155 160 Ile Gln His Asp Asn Gly Tyr Gln Pro Asn Tyr His Ala Val Asn Ile 165 170 175 Val Gly Tyr Gly Ser Thr Gln Gly Val Asp Tyr Trp Ile Val Arg Asn 180 185 190 Ser Trp Asp Thr Thr Trp Gly Asp Ser Gly Tyr Gly Tyr Phe Gln Ala 195 200 205 Gly Asn Asn Leu 210 411307PRTPoa pratensis 411 Met Ala Val Gln Lys Tyr Thr Val Ala Leu Phe Leu Val Ala Leu Val 1 5 10 15 Val Gly Pro Ala Ala Ser Tyr Ala Ala Asp Leu Ser Tyr Gly Ala Pro 20 25 30 Ala Thr Pro Ala Ala Pro Ala Ala Gly Tyr Thr Pro Ala Ala Pro Ala 35 40 45 Gly Ala Ala Pro Lys Ala Thr Thr Asp Glu Gln Lys Met Ile Glu Lys 50 55 60 Ile Asn Val Gly Phe Lys Ala Ala Val Ala Ala Ala Gly Gly Val Pro 65 70 75 80 Ala Ala Asn Lys Tyr Lys Thr Phe Val Ala Thr Phe Gly Ala Ala Ser 85 90 95 Asn Lys Ala Phe Ala Glu Ala Leu Ser Thr Glu Pro Lys Gly Ala Ala 100 105 110 Val Asp Ser Ser Lys Ala Ala Leu Thr Ser Lys Leu Asp Ala Ala Tyr 115 120 125 Lys Leu Ala Tyr Lys Ser Ala Glu Gly Ala Thr Pro Glu Ala Lys Tyr 130 135 140 Asp Asp Tyr Val Ala Thr Leu Ser Glu Ala Leu Arg Ile Ile Ala Gly 145 150 155 160 Thr Leu Glu Val His Gly Val Lys Pro Ala Ala Glu Glu Val Lys Ala 165 170 175 Thr Pro Ala Gly Glu Leu Gln Val Ile Asp Lys Val Asp Ala Ala Phe 180 185 190 Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro Ala Asn Asp Lys Phe 195 200 205 Thr Val Phe Glu Ala Ala Phe Asn Asp Ala Ile Lys Ala Ser Thr Gly 210 215 220 Gly Ala Tyr Gln Ser Tyr Lys Phe Ile Pro Ala Leu Glu Ala Ala Val 225 230 235 240 Lys Gln Ser Tyr Ala Ala Thr Val Ala Thr Ala Pro Ala Val Lys Tyr 245 250 255 Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile Thr Ala Met Ser Gln 260 265 270 Ala Gln Lys Ala Ala Lys Pro Ala Ala Ala Ala Thr Gly Thr Ala Thr 275 280 285 Ala Ala Val Gly Ala Ala Thr Gly Ala Ala Thr Ala Ala Ala Gly Gly 290 295 300 Tyr Lys Val 305 412333PRTPoa pratensis 412Met Ala Val His Gln Tyr Thr Val Ala Leu Phe Leu Ala Val Ala Leu 1 5 10 15 Val Ala Gly Pro Ala Ala Ser Tyr Ala Ala Asp Val Gly Tyr Gly Ala 20 25 30 Pro Ala Thr Leu Ala Thr Pro Ala Thr Pro Ala Ala Pro Ala Ala Gly 35 40 45 Tyr Thr Pro Ala Ala Pro Ala Gly Ala Ala Pro Lys Ala Thr Thr Asp 50 55 60 Glu Gln Lys Leu Ile Glu Lys Ile Asn Ala Gly Phe Lys Ala Ala Val 65 70 75 80 Ala Ala Ala Ala Gly Val Pro Ala Val Asp Lys Tyr Lys Thr Phe Val 85 90 95 Ala Thr Phe Gly Thr Ala Ser Asn Lys Ala Phe Ala Glu Ala Leu Ser 100 105 110 Thr Glu Pro Lys Gly Ala Ala Ala Ala Ser Ser Asn Ala Val Leu Thr 115 120 125 Ser Lys Leu Asp Ala Ala Tyr Lys Leu Ala Tyr Lys Ser Ala Glu Gly 130 135 140 Ala Thr Pro Glu Ala Lys Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu 145 150 155 160 Ala Leu Arg Ile Ile Ala Gly Thr Leu Glu Val His Ala Val Lys Pro 165 170 175 Ala Gly Glu Glu Val Lys Ala Ile Pro Ala Gly Glu Leu Gln Val Ile 180 185 190 Asp Lys Val Asp Ala Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala 195 200 205 Ala Pro Ala Asn Asp Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Asp 210 215 220 Ala Ile Lys Ala Ser Thr Gly Gly Ala Tyr Gln Ser Tyr Lys Phe Ile 225 230 235 240 Pro Ala Leu Glu Ala Ala Val Lys Gln Ser Tyr Ala Ala Thr Val Ala 245 250 255 Thr Ala Pro Ala Val Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys 260 265 270 Ala Ile Thr Ala Met Ser Gln Ala Gln Lys Ala Ala Lys Pro Ala Ala 275 280 285 Ala Val Thr Ala Thr Ala Thr Gly Ala Val Gly Ala Ala Thr Gly Ala 290 295 300 Val Gly Ala Ala Thr Gly Ala Ala Thr Ala Ala Ala Gly Gly Tyr Lys 305 310 315 320 Thr Gly Ala Ala Thr Pro Thr Ala Gly Gly Tyr Lys Val 325 330 413373PRTPoa pratensis 413Met Asp Lys Ala Asn Gly Ala Tyr Lys Thr Ala Leu Lys Ala Ala Ser 1 5 10 15 Ala Val Ala Pro Ala Glu Lys Phe Pro Val Phe Gln Ala Thr Phe Asp 20 25 30 Lys Asn Leu Lys Glu Gly Leu Ser Gly Pro Asp Ala Val Gly Phe Ala 35 40 45 Lys Lys Leu Asp Ala Phe Ile Gln Thr Ser Tyr Leu Ser Thr Lys Ala 50 55 60 Ala Glu Pro Lys Glu Lys Phe Asp Leu Phe Val Leu Ser Leu Thr Glu 65 70 75 80 Val Leu Arg Phe Met Ala Gly Ala Val Lys Ala Pro Pro Ala Ser Lys 85 90 95 Phe Pro Ala Lys Pro Ala Pro Lys Val Ala Ala Tyr Thr Pro Ala Ala 100 105 110 Pro Ala Gly Ala Ala Pro Lys Ala Thr Thr Asp Glu Gln Lys Leu Ile 115 120 125 Glu Lys Ile Asn Val Gly Phe Lys Ala Ala Val Ala Ala Ala Ala Gly 130 135 140 Val Pro Ala Ala Ser Lys Tyr Lys Thr Phe Val Ala Thr Phe Gly Ala 145 150 155 160 Ala Ser Asn Lys Ala Phe Ala Glu Ala Leu Ser Thr Glu Pro Lys Gly 165 170 175 Ala Ala Val Ala Ser Ser Lys Ala Val Leu Thr Ser Lys Leu Asp Ala 180 185 190 Ala Tyr Lys Leu Ala Tyr Lys Ser Ala Glu Gly Ala Thr Pro Glu Ala 195 200 205 Lys Tyr Asp Ala Tyr Val Ala Thr Leu Ser Glu Ala Leu Arg Ile Ile 210 215 220 Ala Gly Thr Leu Glu Val His Gly Val Lys Pro Ala Ala Glu Glu Val 225 230 235 240 Lys Ala Ile Pro Ala Gly Glu Leu Gln Val Ile Asp Lys Val Asp Ala 245 250 255 Ala Phe Lys Val Ala Ala Thr Ala Ala Asn Ala Ala Pro Ala Asn Asp 260 265 270 Lys Phe Thr Val Phe Glu Ala Ala Phe Asn Asp Ala Ile Lys Ala Ser 275 280 285 Thr Gly Gly Ala Tyr Gln Ser Tyr Lys Phe Ile Pro Ala Leu Glu Ala 290 295 300 Ala Val Lys Gln Ser Tyr Ala Ala Thr Val Ala Thr Ala Pro Ala Val 305 310 315 320 Lys Tyr Thr Val Phe Glu Thr Ala Leu Lys Lys Ala Ile Thr Ala Met 325 330 335 Ser Gln Ala Gln Lys Ala Ala Lys Pro Ala Ala Ala Val Thr Gly Thr 340 345 350 Ala Thr Ser Ala Val Gly Ala Ala Thr Gly Ala Ala Thr Ala Ala Ala 355 360 365 Gly Gly Tyr Lys Val 370 414685PRTPeriplaneta americana 414 Met Lys Thr Ala Leu Val Phe Ala Ala Val Val Ala Phe Val Ala Ala 1 5 10 15 Arg Phe Pro Asp His Lys Asp Tyr Lys Gln Leu Ala Asp Lys Gln Phe 20 25 30 Leu Ala Lys Gln Arg Asp Val Leu Arg Leu Phe His Arg Val His Gln 35 40 45 His Asn Ile Leu Asn Asp Gln Val Glu Val Gly Ile Pro Met Thr Ser 50 55 60 Lys Gln Thr Ser Ala Thr Thr Val Pro Pro Ser Gly Glu Ala Val His 65 70 75 80 Gly Val Leu Gln Glu Gly His Ala Arg Pro Arg Gly Glu Pro Phe Ser 85 90 95 Val Asn Tyr Glu Lys His Arg Glu Gln Ala Ile Met Leu Tyr Asp Leu 100 105 110 Leu Tyr Phe Ala Asn Asp Tyr Asp Thr Phe Tyr Lys Thr Ala Cys Trp 115 120 125 Ala Arg Asp Arg Val Asn Glu Gly Met Phe Met Tyr Ser Phe Ser Ile 130 135 140 Ala Val Phe His Arg Asp Asp Met Gln Gly Val Met Leu Pro Pro Pro 145 150 155 160 Tyr Glu Val Tyr Pro Tyr Leu Phe Val Asp His Asp Val Ile His Met 165 170 175 Ala Gln Lys Tyr Trp Met Lys Asn Ala Gly Ser Gly Glu His His Ser 180 185 190 His Val Ile Pro Val Asn Phe Thr Leu Arg Thr Gln Asp His Leu Leu 195 200 205 Ala Tyr Phe Thr Ser Asp Val Asn Leu Asn Ala Phe Asn Thr Tyr Tyr 210 215 220 Arg Tyr Tyr Tyr Pro Ser Trp Tyr Asn Thr Thr Leu Tyr Gly His Asn 225 230 235 240 Ile Asp Arg Arg Gly Glu Gln Phe Tyr Tyr Thr Tyr Lys Gln Ile Tyr 245 250 255 Ala Arg Tyr Phe Leu Glu Arg Leu Ser Asn Asp Leu Pro Asp Val Tyr 260 265

270 Pro Phe Tyr Tyr Ser Lys Pro Val Lys Ser Ala Tyr Asn Pro Asn Leu 275 280 285 Arg Tyr His Asn Gly Glu Glu Met Pro Val Arg Pro Ser Asn Met Tyr 290 295 300 Val Thr Asn Phe Asp Leu Tyr Tyr Ile Ala Asp Ile Lys Asn Tyr Glu 305 310 315 320 Lys Arg Val Glu Asp Ala Ile Asp Phe Gly Tyr Ala Phe Asp Glu His 325 330 335 Met Lys Pro His Ser Leu Tyr His Asp Val His Gly Met Glu Tyr Leu 340 345 350 Ala Asp Met Ile Glu Gly Asn Met Asp Ser Pro Asn Phe Tyr Phe Tyr 355 360 365 Gly Ser Ile Tyr His Met Tyr His Ser Met Ile Gly His Ile Val Asp 370 375 380 Pro Tyr His Lys Met Gly Leu Ala Pro Ser Leu Glu His Pro Glu Thr 385 390 395 400 Val Leu Arg Asp Pro Val Phe Tyr Gln Leu Trp Lys Arg Val Asp His 405 410 415 Leu Phe Gln Lys Tyr Lys Asn Arg Leu Pro Arg Tyr Thr His Asp Glu 420 425 430 Leu Ala Phe Glu Gly Val Lys Val Glu Asn Val Asp Val Gly Lys Leu 435 440 445 Tyr Thr Tyr Phe Glu Gln Tyr Asp Met Ser Leu Asp Met Ala Val Tyr 450 455 460 Val Asn Asn Val Asp Gln Ile Ser Asn Val Asp Val Gln Leu Ala Val 465 470 475 480 Arg Leu Asn His Lys Pro Phe Thr Tyr Asn Ile Glu Val Ser Ser Asp 485 490 495 Lys Ala Gln Asp Val Tyr Val Ala Val Phe Leu Gly Pro Lys Tyr Asp 500 505 510 Tyr Leu Gly Arg Glu Tyr Asp Leu Asn Asp Arg Arg His Tyr Phe Val 515 520 525 Glu Met Asp Arg Phe Pro Tyr His Val Gly Ala Gly Lys Thr Val Ile 530 535 540 Glu Arg Asn Ser His Asp Ser Asn Ile Ile Ala Pro Glu Arg Asp Ser 545 550 555 560 Tyr Arg Thr Phe Tyr Lys Lys Val Gln Glu Ala Tyr Glu Gly Lys Ser 565 570 575 Gln Tyr Tyr Val Asp Lys Gly His Asn Tyr Cys Gly Tyr Pro Glu Asn 580 585 590 Leu Leu Ile Pro Lys Gly Lys Lys Gly Gly Gln Ala Tyr Thr Phe Tyr 595 600 605 Val Ile Val Thr Pro Tyr Val Lys Gln Asp Glu His Asp Phe Glu Pro 610 615 620 Tyr Asn Tyr Lys Ala Phe Ser Tyr Cys Gly Val Gly Ser Glu Arg Lys 625 630 635 640 Tyr Pro Asp Asn Lys Pro Leu Gly Tyr Pro Phe Asp Arg Lys Ile Tyr 645 650 655 Ser Asn Asp Phe Tyr Thr Pro Asn Met Tyr Phe Lys Asp Val Ile Ile 660 665 670 Phe His Lys Lys Tyr Asp Glu Val Gly Val Gln Gly His 675 680 685 415446PRTPeriplaneta americana 415Ile Asn Glu Ile His Ser Ile Ile Gly Leu Pro Pro Phe Val Pro Pro 1 5 10 15 Ser Arg Arg His Ala Arg Arg Gly Val Gly Ile Asn Gly Leu Ile Asp 20 25 30 Asp Val Ile Ala Ile Leu Pro Val Asp Glu Leu Lys Ala Leu Phe Gln 35 40 45 Glu Lys Leu Glu Thr Ser Pro Asp Phe Lys Ala Leu Tyr Asp Ala Ile 50 55 60 Arg Ser Pro Glu Phe Gln Ser Ile Ile Ser Thr Leu Asn Ala Met Gln 65 70 75 80 Arg Ser Glu His His Gln Asn Leu Arg Asp Lys Gly Val Asp Val Asp 85 90 95 His Phe Ile Gln Leu Ile Arg Ala Leu Phe Gly Leu Ser Arg Ala Ala 100 105 110 Arg Asn Leu Gln Asp Asp Leu Asn Asp Phe Leu His Ser Leu Glu Pro 115 120 125 Ile Ser Pro Arg His Arg His Gly Leu Pro Arg Gln Arg Arg Arg Ser 130 135 140 Ala Arg Val Ser Ala Tyr Leu His Ala Asp Asp Phe His Lys Ile Ile 145 150 155 160 Thr Thr Ile Glu Ala Leu Pro Glu Phe Ala Asn Phe Tyr Asn Phe Leu 165 170 175 Lys Glu His Gly Leu Asp Val Val Asp Tyr Ile Asn Glu Ile His Ser 180 185 190 Ile Ile Gly Leu Pro Pro Phe Val Pro Pro Ser Arg Arg His Ala Arg 195 200 205 Arg Gly Val Gly Ile Asn Gly Leu Ile Asp Asp Val Ile Ala Ile Leu 210 215 220 Pro Val Asp Glu Leu Lys Ala Leu Phe Gln Glu Lys Leu Glu Thr Ser 225 230 235 240 Pro Asp Phe Lys Ala Leu Tyr Asp Ala Ile Arg Ser Pro Glu Phe Gln 245 250 255 Ser Ile Ile Ser Thr Leu Asn Ala Met Pro Glu Tyr Gln Glu Leu Leu 260 265 270 Gln Asn Leu Arg Asp Lys Gly Val Asp Val Asp His Phe Ile Arg Val 275 280 285 Asp Gln Gly Thr Leu Arg Thr Leu Ser Ser Gly Gln Arg Asn Leu Gln 290 295 300 Asp Asp Leu Asn Asp Phe Leu Ala Leu Ile Pro Thr Asp Gln Ile Leu 305 310 315 320 Ala Ile Ala Met Asp Tyr Leu Ala Asn Asp Ala Glu Val Gln Glu Leu 325 330 335 Val Ala Tyr Leu Gln Ser Asp Asp Phe His Lys Ile Ile Thr Thr Ile 340 345 350 Glu Ala Leu Pro Glu Phe Ala Asn Phe Tyr Asn Phe Leu Lys Glu His 355 360 365 Gly Leu Asp Val Val Asp Tyr Ile Asn Glu Ile His Ser Ile Ile Gly 370 375 380 Leu Pro Pro Phe Val Pro Pro Ser Gln Arg His Ala Arg Arg Gly Val 385 390 395 400 Gly Ile Asn Gly Leu Ile Asp Asp Val Ile Ala Ile Leu Pro Val Asp 405 410 415 Glu Leu Lys Ala Leu Phe Gln Glu Lys Leu Glu Thr Ser Pro Asp Phe 420 425 430 Lys Ala Leu Tyr Asp Ala Ile Asp Leu Arg Ser Ser Arg Ala 435 440 445 416352PRTBlattella germanica 416Met Ile Gly Leu Lys Leu Val Thr Val Leu Phe Ala Val Ala Thr Ile 1 5 10 15 Thr His Ala Ala Glu Leu Gln Arg Val Pro Leu Tyr Lys Leu Val His 20 25 30 Val Phe Ile Asn Thr Gln Tyr Ala Gly Ile Thr Lys Ile Gly Asn Gln 35 40 45 Asn Phe Leu Thr Val Phe Asp Ser Thr Ser Cys Asn Val Val Val Ala 50 55 60 Ser Gln Glu Cys Val Gly Gly Ala Cys Val Cys Pro Asn Leu Gln Lys 65 70 75 80 Tyr Glu Lys Leu Lys Pro Lys Tyr Ile Ser Asp Gly Asn Val Gln Val 85 90 95 Lys Phe Phe Asp Thr Gly Ser Ala Val Gly Arg Gly Ile Glu Asp Ser 100 105 110 Leu Thr Ile Ser Asn Leu Thr Thr Ser Gln Gln Asp Ile Val Leu Ala 115 120 125 Asp Glu Leu Ser Gln Glu Val Cys Ile Leu Ser Ala Asp Val Val Val 130 135 140 Gly Ile Ala Ala Pro Gly Cys Pro Asn Ala Leu Lys Gly Lys Thr Val 145 150 155 160 Leu Glu Asn Phe Val Glu Glu Asn Leu Ile Ala Pro Val Phe Ser Ile 165 170 175 His His Ala Arg Phe Gln Asp Gly Glu His Phe Gly Glu Ile Ile Phe 180 185 190 Gly Gly Ser Asp Trp Lys Tyr Val Asp Gly Glu Phe Thr Tyr Val Pro 195 200 205 Leu Val Gly Asp Asp Ser Trp Lys Phe Arg Leu Asp Gly Val Lys Ile 210 215 220 Gly Asp Thr Thr Val Ala Pro Ala Gly Thr Gln Ala Ile Ile Asp Thr 225 230 235 240 Ser Lys Ala Ile Ile Val Gly Pro Lys Ala Tyr Val Asn Pro Ile Asn 245 250 255 Glu Ala Ile Gly Cys Val Val Glu Lys Thr Thr Thr Arg Arg Ile Cys 260 265 270 Lys Leu Asp Cys Ser Lys Ile Pro Ser Leu Pro Asp Val Thr Phe Val 275 280 285 Ile Asn Gly Arg Asn Phe Asn Ile Ser Ser Gln Tyr Tyr Ile Gln Gln 290 295 300 Asn Gly Asn Leu Cys Tyr Ser Gly Phe Gln Pro Cys Gly His Ser Asp 305 310 315 320 His Phe Phe Ile Gly Asp Phe Phe Val Asp His Tyr Tyr Ser Glu Phe 325 330 335 Asn Trp Glu Asn Lys Thr Met Gly Phe Gly Arg Ser Val Glu Ser Val 340 345 350 417182PRTBlattella germanica 417Ala Val Leu Ala Leu Cys Ala Thr Asp Thr Leu Ala Asn Glu Asp Cys 1 5 10 15 Phe Arg His Glu Ser Leu Val Pro Asn Leu Asp Tyr Glu Arg Phe Arg 20 25 30 Gly Ser Trp Ile Ile Ala Ala Gly Thr Ser Glu Ala Leu Thr Gln Tyr 35 40 45 Lys Cys Trp Ile Asp Arg Phe Ser Tyr Asp Asp Ala Leu Val Ser Lys 50 55 60 Tyr Thr Asp Ser Gln Gly Lys Asn Arg Thr Thr Ile Arg Gly Arg Thr 65 70 75 80 Lys Phe Glu Gly Asn Lys Phe Thr Ile Asp Tyr Asn Asp Lys Gly Lys 85 90 95 Ala Phe Ser Ala Pro Tyr Ser Val Leu Ala Thr Asp Tyr Glu Asn Tyr 100 105 110 Ala Ile Val Glu Gly Cys Pro Ala Ala Ala Asn Gly His Val Ile Tyr 115 120 125 Val Gln Ile Arg Phe Ser Val Arg Arg Phe His Pro Lys Leu Gly Asp 130 135 140 Lys Glu Met Ile Gln His Tyr Thr Leu Asp Gln Val Asn Gln His Lys 145 150 155 160 Lys Ala Ile Glu Glu Asp Leu Lys His Phe Asn Leu Lys Tyr Glu Asp 165 170 175 Leu His Ser Thr Cys His 180 418200PRTBlattella germanica 418Tyr Lys Leu Thr Tyr Cys Pro Val Lys Ala Leu Gly Glu Pro Ile Arg 1 5 10 15 Phe Leu Leu Ser Tyr Gly Glu Lys Asp Phe Glu Asp Tyr Arg Phe Gln 20 25 30 Glu Gly Asp Trp Pro Asn Leu Lys Pro Ser Met Pro Phe Gly Lys Thr 35 40 45 Pro Val Leu Glu Ile Asp Gly Lys Gln Thr His Gln Ser Val Ala Ile 50 55 60 Ser Arg Tyr Leu Gly Lys Gln Phe Gly Leu Ser Gly Lys Asp Asp Trp 65 70 75 80 Glu Asn Leu Glu Ile Asp Met Ile Val Asp Thr Ile Ser Asp Phe Arg 85 90 95 Ala Ala Ile Ala Asn Tyr His Tyr Asp Ala Asp Glu Asn Ser Lys Gln 100 105 110 Lys Lys Trp Asp Pro Leu Lys Lys Glu Thr Ile Pro Tyr Tyr Thr Lys 115 120 125 Lys Phe Asp Glu Val Val Lys Ala Asn Gly Gly Tyr Leu Ala Ala Gly 130 135 140 Lys Leu Thr Trp Ala Asp Phe Tyr Phe Val Ala Ile Leu Asp Tyr Leu 145 150 155 160 Asn His Met Ala Lys Glu Asp Leu Val Ala Asn Gln Pro Asn Leu Lys 165 170 175 Ala Leu Arg Glu Lys Val Leu Gly Leu Pro Ala Ile Lys Ala Trp Val 180 185 190 Ala Lys Arg Pro Pro Thr Asp Leu 195 200 41915PRTAlternaria alternata 419Glu Val Tyr Gln Lys Leu Lys Ala Leu Ala Lys Lys Thr Tyr Gly1 5 10 1542017PRTAlternaria alternata 420Ala Glu Val Tyr Gln Lys Leu Lys Ala Leu Ala Lys Lys Thr Tyr Gly Gln1 5 10 15

Claims

1. (canceled)

2. A composition comprising a peptide which has a length of 10 to 25 amino acids and which comprises a region having the sequence of SEQ ID NO: 60 or SEQ ID NO: 81.

3. A composition according to claim 2 which additionally comprises a pharmaceutically acceptable carrier and an adjuvant.

4. A composition according to claim 2 which additionally comprises an effective amount of a preservative and a pharmaceutically acceptable carrier.

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