RECOMBINANT AVIAN INFECTIOUS CORYZA VACCINE AND PROCESS FOR PREPARING SAME

Abstract

A recombinant avian infectious coryza vaccine and a process for preparing the same are provided. A process for preparing a recombinant avian infectious coryza vaccine which comprises step of constructing E. coli that may produce as an inclusion body a fusion peptide consisting of peptides derived from outer-membrane protein of Avibacterium paragarinarum serotype A and serotype C, step of culturing said E. coli and colleting and purifying inclusion body from culture, and step of preparing a preparation comprising said purified inclusion body, and an avian infectious coryza vaccine comprising as an active ingredient the fusion peptide. A linker sequence may be inserted between the respective peptides comprising the fusion peptide. For the peptide derived from the serotypes A and C, an amino acid sequence region of Region 2 or its vicinity responsible for protection from infection may be used.

Description

TECHNICAL FIELD

[0001] The present invention relates to a recombinant avian infectious coryza vaccine and a process for preparing the same. More particularly, the present invention relates to a recombinant avian infectious coryza vaccine comprising as an active ingredient a fusion peptide consisting of a part of an outer-membrane protein of Avibacterium paragallinarum (hereinafter also referred to as "A.pg") serotype A and a part of an outer-membrane protein of A.pg serotype C and process for preparing the same.

BACKGROUND ART

[0002] Avian infectious coryza is one of the most important respiratory diseases caused by infection with A.pg. Chicken suffering from avian infectious coryza shows cardinal symptoms of a running nose, swelling of the face and epiphora. Avian infectious coryza brings about a great economical damage since it leads to decrease in the breeding rate of chicken, retarding of egg laying, decrease in egg production or failure of egg laying.

[0003] Page et al. classified A.pg into three serotypes A, B and C (see e.g. Non-patent reference 1) and Sawata et al. classified A.pg into two serotypes 1 and 2 (see e.g. Non-patent reference 2). Thereafter, Kume et al. reported that serotype A by Page et al. corresponds to serotype 1 by Sawata et al. and serotype C by Page et al. corresponds to serotype 2 by Sawata et al. (see e.g. Non-patent references and 4). Today, it is established that main causative agents of avian infectious coryza are A.pg serotype A (hereinafter also referred to as "A.pg-A") and A.pg serotype C (hereinafter also referred to as "A.pg-C").

[0004] For prevention of avian infectious coryza, an inactivated vaccine has hitherto been used widely which is obtained by inactivating the cells of A.pg-A or A.pg-C with formalin, thimerosal and the like. However, adverse side effects caused by such an inactivated vaccine have been an issue as it has been reported that local necrotic lesions are formed in the inoculated chicken when the vaccine is administered (see e.g. Non-patent reference 5). Under the circumstances, attempting to develop a safe vaccine, a recombinant vaccine has been investigated comprising a protective antigen against infection prepared by genetic recombination technique.

[0005] For instance, Tokunaga et al. isolated and identified a gene coding for an outer-membrane protein of A.pg-A (outer-membrane protein gene) and found that a peptide obtained by expressing a part of said gene (HPG3.5 kbp, HPG4.1 kbp) in E. coli is useful as a protective antigen against infection for avian infectious coryza. Furthermore, using said DNA fragment as a probe, they obtained an outer-membrane protein gene from A.pg-C and compared nucleotide sequences of open reading frame of the outer-membrane protein gene from A.pg-A and A.pg-C. As a result, they revealed that both nucleotide sequences had homology of about 80% as a whole, that a region of 3.4 kbp at the 5'- end (hereinafter also referred to as "Region 1") and a region of about 1.2 kbp at the 3'- end (hereinafter also referred to as "Region 3") had extremely high homology and that a region of about 1.5 kbp flanked by Region 1 and Region 3 (hereinafter also referred to as "Region 2") had low homology (see Patent reference 1).

[0006] It is also reported by Noro et al. that the outer-membrane protein discovered by Tokunaga et al. is important as a protective antigen for avian infectious coryza. Noro et al. immunized chicken with peptides coded by DNA fragments of 4,801 by and 5,157 bp, which are parts of the outer-membrane protein gene from A.pg-A, to show that said peptides may induce HI antibody to A.pg-A and may have a vaccine effect (see e.g. Patent reference 2) and further reported that peptides coded by DNA fragments of about 5.1 kbp and 5.5 kbp, which are parts of the outer-membrane protein gene from A.pg-C, had similar function and effect (see e.g. Patent reference 3).

[0007] On the other hand, Yamamoto et al. employed a polypeptide coded by a DNA fragment of 2,016 bp, which comprises most of the outer-membrane protein gene from A.pg-A to show usefulness of said polypeptide (see e.g. Patent reference 4) but the nucleotide sequence of about 300 by at the 3' end of the DNA fragment reported by them was extremely different from those shown by Tokunaga et al. and Noro et al.

[0008] Patent reference 1: WO98/12331

[0009] Patent reference 2: Japanese patent No. 4001117

[0010] Patent reference 3: JP 2008-156317

[0011] Patent reference 4: JP 2004-57078

[0012] Non-patent reference 1: Am. J. Vet. Res., 23:85-95, 1962

[0013] Non-patent reference 2: Jpn. J. Vet. Sci., 40:645-652, 1978

[0014] Non-patent reference 3: m. J. Vet. Res., 41:757-760, 1980

[0015] Non-patent reference 4: Am. J. Vet.Res., 41:1901-1904, 1980

[0016] Non-patent reference 5: Avian Dis., 15:109-117, 1971

DISCLOSURE OF THE INVENTION

Technical Problem to be Solved by the Invention

[0017] As described above, it has been revealed that the outer-membrane protein or its partial peptide from A.pg-A and A.pg-C, the main causative agent of avian infectious coryza, is useful as a protective antigen against avian infectious coryza. Thus, by mixing these protective antigens against infection, immunization to avian infectious coryza may efficiently be done. However, an approach by simple mixing necessitates separate production of the two infectious protective antigens and thus is costly. In general, a vaccine for use in an animal, unlike a vaccine for use in human, would not be accepted by a stock farmer unless the vaccine is not only in high quality but also is available at a low cost. Therefore, for a vaccine for use in an animal, a process for the production with less cost for production is desired.

Means for Solving the Problems

[0018] The present inventors have assiduously investigated in order to attain the object as described above, and as a result, have revealed that peptide fragments coded by the sequence of about 1.6 kbp comprising Region 2 (the nucleotide sequence of 3,639 bp to 5,162 bp for A.pg-A and the nucleotide sequence of 4,247 bp to 5,758 bp for A.pg-C: see FIGS. 1 and 2) of the outer-membrane protein gene from A.pg-A and A.pg-C (peptides coded by a DNA sequence of from 3,558 bp to 5,192 bp for A.pg-A and by a DNA sequence of from 4,166 bp to 5,788 bp for A.pg-C: hereinafter also referred to as "AΔ5-1" and "CΔ5-1", respectively: see FIGS. 1 and 2) are useful as a protective antigen for avian infectious coryza. The present inventors have found that a fusion peptide (hereinafter also referred to as "ACΔ5-1"), which is obtained by linking together a DNA fragment coding for AΔ5-1 and a DNA fragment coding for CΔ5-1 and expressing the resultant DNA fragment, maintained immunogenicity of the respective antigens even after fusion and that the fusion peptide exhibited infection protective effect to avian infectious coryza equivalent to or more than that of AΔ5-1 or CΔ5-1, each expressed alone. Furthermore, the present inventors have found that CΔ5-1 is expressed in a soluble fraction when expressed alone whereas AΔ5-1 is expressed in an insoluble fraction by forming an inclusion body to thereby complete the present invention.

[0019] Accordingly, an object of the present invention is to provide a vaccine for avian infectious coryza comprising as an active ingredient a fusion peptide, obtained by linking to each other a peptide fragment comprising a specific region of the outer-membrane protein from A.pg-A and a peptide fragment comprising a specific region of the outer-membrane protein from A.pg-C, and a process for preparing the same.

[0020] As used herein, the outer-membrane proteins from A.pg-A and A.pg-C as isolated and identified by Tokunaga et al. (Patent reference 1) are also collectively referred to as "HMTp210 protein" and peptide fragments derived from HMTp210 protein of A.pg-A and A.pg-C are also referred to as "Peptide A" and "Peptide C", respectively.

[0021] Thus, the present invention includes the followings:

[0022] [1] A process for preparing a recombinant avian infectious coryza vaccine which comprises step of constructing a host that may produce as an inclusion body a fusion peptide consisting of a peptide fragment (Peptide A) derived from HMTp210 protein of A.pg-A and a peptide fragment (Peptide C) derived from HMTp210 protein of A.pg-C, step of culturing said host and colleting and purifying a fraction of inclusion body from culture, and step of preparing a preparation comprising said purified fraction of inclusion body.

[0023] [2] The process of [1] wherein Peptide A and Peptide C consist of 600 or less amino acid residues.

[0024] [3] The process of [1] wherein Peptide A has an amino acid sequence selected from the group consisting of SEQ ID NOs: 1, 27, 28, 29, 30, 31, 32, 33, 34 and 35 whereas Peptide C has an amino acid sequence selected from the group consisting of SEQ ID NOs: 2, 3, 4, 50, 51, 52, 53, 54, 55 and 56.

[0025] [4] The process of [3] wherein Peptide A comprises an amino acid sequence shown by SEQ ID NO: 35 whereas Peptide C comprises an amino acid sequence shown by SEQ ID NO: 56.

[0026] [5] The process of [3] or [4] wherein Peptide A or Peptide C comprises an amino acid sequence where one or several amino acids are deleted, added or replaced.

[0027] [6] The process of any one of [1] to [5] wherein a ratio of Peptide A and Peptide C in the fusion peptide is 1 to 3 of Peptide C to 1 of Peptide A.

[0028] [7] The process of any one of [1] to [6] wherein the fusion peptide comprises at least a structure where Peptide C is linked to the C-terminal of Peptide A.

[0029] [8] The process of any one of [1] to [7] wherein the fusion peptide has a linker between Peptide A and Peptide A, Peptide C and Peptide C, or Peptide A and Peptide C.

[0030] [9] The process of [3] wherein the fusion peptide has an amino acid sequence selected from the group consisting of SEQ ID NOs: 8, 9, 10, 11, 12, 13, 41, 42, 43, 44, 45, 46, 47, 48, 49, 61, 62, 63, 64, 65, 66 and 67.

[0031] [10] A recombinant avian infectious coryza vaccine comprising as an active ingredient a fusion peptide consisting of a peptide fragment (Peptide A) derived from HMTp210 protein of A.pg-A and a peptide fragment (Peptide C) derived from HMTp210 protein of A.pg-C.

[0032] [11] The vaccine of [10] wherein the fusion peptide has a property of forming an inclusion body when produced by the host.

[0033] [12] The vaccine of [10] wherein Peptide A and Peptide C consist of 600 or less amino acid residues.

[0034] [13] The vaccine of [10] wherein Peptide A has an amino acid sequence selected from the group consisting of SEQ ID NOs: 1, 27, 28, 29, 30, 31, 32, 33, 34 and 35 whereas Peptide C has an amino acid sequence selected from the group consisting of SEQ ID NOs: 2, 3, 4, 50, 51, 52, 53, 54, 55 and 56.

[0035] [14] The vaccine of [13] wherein Peptide A comprises an amino acid sequence shown by SEQ ID NO: 35 whereas Peptide C comprises an amino acid sequence shown by SEQ ID NO: 56.

[0036] [15] The vaccine of [13] or [14] wherein Peptide A or Peptide C comprises an amino acid sequence where one or several amino acids are deleted, added or replaced.

[0037] [16] The vaccine of any one of [10] to [15] wherein a ratio of Peptide A and Peptide C in the fusion peptide is 1 to 3 of Peptide C to 1 of :Peptide A.

[0038] [17] The vaccine of any one of [10] to [16] wherein the fusion peptide comprises at least a structure where Peptide C is linked to the C-terminal of Peptide.

[0039] [18] The vaccine of any one of [10] to [17] wherein the fusion peptide has a linker between Peptide A and Peptide A, Peptide C and Peptide C, or Peptide A and Peptide C.

[0040] [19] The vaccine of [13] wherein the fusion peptide has an amino acid sequence selected from the group consisting of SEQ ID NOs: 8, 9, 10, 11, 12, 13, 41, 42, 43, 44, 45, 46, 47, 48, 49, 61, 62, 63, 64, 65, 66 and 67.

[0041] [20] A recombinant avian infectious coryza vaccine comprising as an active ingredient a peptide consisting of a sequence comprising the amino acid sequence shown by SEQ ID NO: 35, said sequence being within the amino acid sequence shown by SEQ ID NO: 1 with addition of 1 to 200 amino acid residues at the N-terminal and/or C-terminal thereof.

[0042] [21] The vaccine of [20] wherein said vaccine comprises as an active ingredient a peptide consisting of the amino acid sequence shown by SEQ ID NO: 1.

[0043] [22] A recombinant avian infectious coryza vaccine comprising as an active ingredient a peptide consisting of a sequence comprising the amino acid sequence shown by SEQ ID NO: 56, said sequence being within the amino acid sequence shown by SEQ ID NO: 3 with addition of 1 to 200 amino acid residues at the N-terminal and/or C-terminal thereof.

[0044] [23] The vaccine of [22] wherein said vaccine comprises as an active ingredient a peptide consisting of the amino acid sequence shown by SEQ ID NO: 3 or 52.

[0045] [24] The vaccine of [21] or [23] wherein said peptide comprises an amino acid sequence where one or several amino acids are deleted, added or replaced.

Effects of the Invention

[0046] In accordance with the present invention, provided are an avian infectious coryza vaccine comprising as an active ingredient a fusion peptide consisting of a peptide fragment derived from HMTp210 protein of A.pg-A and a peptide fragment derived from HMTp210 protein of A.pg-C linked to each other and a process for preparing the same. The avian infectious coryza vaccine of the present invention may simultaneously provide immunization for protection from avian infectious coryza caused by A.pg-A and A.pg-C .

[0047] In accordance with the process of the present invention, it becomes possible to let CΔ5-1, which is expressed in a soluble fraction when expressed alone, form an inclusion body so as to be expressed in an insoluble fraction via expression of its fusion peptide with AΔ5-1. As a result, not only purification of said fusion peptide is facilitated but also production cost is reduced since infection protective antigens to A.pg-A and A.pg-C may be prepared with a single culture.

BRIEF DESCRIPTION OF DRAWINGS

[0048] FIG. 1 shows a position of AΔ5-1 fragment in HMTp210 gene of A.pg-A (HMTp210A gene) where the indicated nucleotide numbers correspond to those disclosed in Patent reference 1 (Tokunaga et al.).

[0049] FIG. 2 shows position of CΔ4c-1, CΔ5-1 and CΔ6b-1b fragments in HMTp210 gene of A.pg-C (HMTp210C gene) where the indicated nucleotide numbers correspond to those disclosed in Patent reference 1 (Tokunaga et al.).

[0050] FIG. 3 is a photograph showing results of SDS-PAGE performed on supernatant and precipitate fractions after centrifugation of cell debris of fusion peptide-producing E. coli. M: marker, Lane 1: AΔ5-1/CΔ4c-1 (precipitate fraction), Lane 2: AΔ5-1/CΔ4c-1 (supernatant fraction), Lane 3: ACΔ5-1 (precipitate fraction), Lane 4: ACΔ5-1 (supernatant fraction), Lane 5: AΔ5-1/CΔ6b-1b (precipitate fraction), Lane 6: AΔ5-1/CΔ6b-1b (supernatant fraction). Arrows show fusion peptides as expressed.

[0051] FIG. 4 shows a position of AΔ5-1, AΔ5-2, AΔ5-3, AΔ5-4, AΔ9-2, AΔ9-3, AΔ9-4, CΔ6-2, CΔ6-3 and CΔ6-4 fragments in HMTp210 gene of A.pg-A (HMTp210A gene) where the indicated nucleotide numbers correspond to those disclosed in Patent reference 1 (Tokunaga et al.).

[0052] FIG. 5 shows a position of CΔ5-1, CΔ5-2, CΔ5-4, CΔ9-0, CΔ9-2, CΔ9-4, CΔ6-2 and CΔ6-4 fragments in HMTp210 gene of A.pg-C (HMTp210C gene) where the indicated nucleotide numbers correspond to those disclosed in Patent reference 1 (Tokunaga et al.).

[0053] FIG. 6 is a photograph showing results of SDS-PAGE performed on precipitate fractions after centrifugation of cell debris of fusion peptide-producing E. coli. M: marker, Lane 1: ACΔ5-1 (precipitate fraction), Lane 2: AΔ5-2/CΔ5-1 (precipitate fraction), Lane 3: AΔ5-3/CΔ5-1 (precipitate fraction), Lane 4: AΔ5-4/CΔ5-1 (precipitate fraction), Lane 5: AΔ9-2/CΔ5-1 (precipitate fraction), Lane 6: AΔ9-3/CΔ5-1 (precipitate fraction), Lane 7: AΔ9-4/CΔ5-1 (precipitate fraction), Lane 8: AΔ6-2/CΔ5-1 (precipitate fraction), Lane 9: AΔ6-3/CΔ5-1 (precipitate fraction), Lane 10: AΔ6-4/CΔ5-1 (precipitate fraction), Arrows show fusion peptides as expressed.

[0054] FIG. 7 is a photograph showing results of SDS-PAGE performed on precipitate fractions after centrifugation of cell debris of fusion peptide-producing E. coli. M: marker, Lane 1: ACΔ5-1 (precipitate fraction), Lane 2: AΔ5-1/CΔ5-2 (precipitate fraction), Lane 3: AΔ5-1/CΔ5-4 (precipitate fraction), Lane 4: AΔ5-1/CΔ9-0 (precipitate fraction), Lane 5: AΔ5-1/CΔ9-2 (precipitate fraction), Lane 6: AΔ5-1/CΔ9-4 (precipitate fraction), Lane 7: AΔ5-1/CΔ6-2 (precipitate fraction), Lane 8: AΔ5-1/CΔ6-4 (precipitate fraction), Arrows show fusion peptides as expressed.

[0055] FIG. 8 is a photograph showing results of SDS-PAGE performed on supernatant and precipitate fractions after centrifugation of cell debris of peptide C-producing E. coli. M: marker, Lane 1: CΔ5-1-pQE (supernatant fraction), Lane 2: CΔ5-2-pQE (supernatant fraction), Lane 3: CΔ5-4-pQE (supernatant fraction), Lane CΔ9-0-pQE (supernatant fraction), Lane 5: CΔ9-2-pQE (supernatant fraction), Lane 6: CΔ9-4-pQE (supernatant fraction), Lane 7: CΔ6-2-pQE (precipitate fraction), Lane 8: CΔ6-4-pQE (supernatant fraction). Arrows show fusion peptides as expressed.

BEST MODE FOR CARRYING OUT THE INVENTION

[0056] The present invention is characterized by a process for preparing a recombinant avian infectious coryza vaccine comprising step of preparing an inclusion body-forming fusion peptide consisting of Peptide A derived from HMTp210 protein of Avibacterium paragarinarum (hereinafter referred to as "A.pg") serotype A and Peptide C derived from HMTp210 protein of A.pg-C. More specifically, the present invention is characterized by a process for preparing an avian infectious coryza vaccine which comprises step of constructing a host that may produce as an inclusion body a fusion peptide consisting of a peptide fragment derived from HMTp210 protein of A.pg-A and a peptide fragment derived from HMTp210 protein of A.pg-C, step of culturing said host and colleting and purifying a fraction of inclusion body from culture, and step of preparing a preparation comprising said purified fraction of inclusion body, and an avian infectious coryza vaccine comprising as an active ingredient said fusion peptide.

[0057] A DNA fragment may be obtained as described below that consists of a part of a gene (hereinafter also referred to as "HMTp210A gene") coding for an amino acid sequence of HMTp210 protein (SEQ ID NO: 25) of A.pg-A and a gene (hereinafter also referred to as "HMTp210C gene") coding for an amino acid sequence of HMTp210 protein (SEQ ID NO: 26) of A.pg-C

[0058] There are several isolated strains of A.pg-A and A.pg-C and any of these strains may be used in the present invention without limitation. Hitherto, there have been isolated, for instance, 221, O83 and W strains etc. for A.pg-A and 53-47, Modesto and HK-1 strains etc. for A.pg-C wherein mutations of substitution, deletion or addition of one or several amino acids are noted. For the present invention, any of these strains or mutants may be used.

[0059] For growth of A.pg-A and A.pg-C, a culture medium may be used that suitably contains polypeptone, glucose, casamino acid, sodium glutamate, yeast extract, sodium chloride, chicken meat infusion, nicotineamide adenine dinucleotide (β-NAD), chicken sera, and the like. A chicken broth supplemented with chicken sera was used herein, containing polypeptone S 5 g, casamino acid 1 g, sodium chloride 5 g, sodium L-glutamate 5 g, glucose 1 g, yeast extract 10 g, chicken meat infusion 175 mL, chicken sera 25 mL, β-NAD 0.025% in 1,000 mL of culture medium, for growth in a small/medium scale. Culture condition may be usually set at the temperature of 37° C. for 16 to 24 hours, which condition may suitably vary depending on purpose of use, a mode of culture, an amount of bacteria inoculated, a scale of culture, and the like.

[0060] Cells in culture may be collected by centrifugation (5,800 g, 20 min.) in a precipitate fraction. HMTp210A gene and HMTp210C gene (hereinafter also referred to collectively as "HMTp210 gene" in case that the two genes are not separately referred to) may be prepared from a genomic: DNAs extracted from the cells by genetic recombination technique according to Sambrook et al. (Molecular Cloning, A Laboratory Manual Second Edition. Cold Spring Harbor Laboratory Press, N.Y., 1989). A commercially available kit may also be used. For instance, for extraction of chromosomal DNAs, PureGene kit (Gentra Systems), SepaGene kit (Sanko Junyaku Co., Ltd.), ISOPLANT (Wako Pure Chemical Industries, Ltd.), and the like may be used.

[0061] More specifically, chromosomal DNAs may be extracted from the cells collected by centrifugation using PureGene kit: (Gentra Systems) and the like, and a genome DNA library of the cells may be prepared in accordance with Tokunaga et al. (Patent reference 1). Using the obtained DNA fragments as a template, PCR may be performed to amplify DNA fragments in desired sizes using Prime STAR HS DNA Polymerase (TAKARA BIO Inc.) in accordance with protocol attached thereto. Primers for use in PCR may be designed based on the nucleotide sequences of A.pg-A- and A.pg-C-derived HMT p210 genes as Tokunaga et al. disclosed (Patent reference 1). Primers for PCR may be readily available if asked to DNA synthesis contractor services (e.g. Sigma Genosys Japan K.K.). When designed, nucleotide sequences of appropriate restriction enzyme cleavage sites may be added at the 5'-end of upstream Primer and at the 5'-end of downstream Primer.

[0062] A DNA fragment coding for the fusion peptide of the present invention may be obtained by linking together the DNA fragment coding for HMTp210A gene and the DNA fragment coding for HMTp210C gene, as obtained above, using a DNA synthase directly or after cleavage with a restriction enzyme. A DNA fragment coding for a linker consisting of an amino acid sequence of a suitable size may optionally be added between the DNA fragment coding for HMTp210A gene and the DNA fragment coding for HMTp210C gene. For a linker, an amino acid with a lot of flexibility such as a neutral amino acid, e.g. glycine, serine, and the like may preferably be used. A linker consisting of a single sort of amino acids or two or more sorts of amino acids may be used. A linker may be in general in a size of 5 to 20 amino acids, preferably, in a size of 10 to 15 amino acids.

[0063] In accordance with the present invention, a DNA fragment of the HMTp210A gene and the HMTp210C gene coding for a fusion peptide may be used that may protect from infection of A.pg-A and A.pg-C and form an inclusion body. Such a DNA fragment includes, for instance, a DNA fragment coding for a peptide of Region 2 of an outer-membrane protein, a DNA fragment coding for a peptide of Region 2 with addition of an amino acid sequence at N-terminal and/or C-terminal thereof, DNA fragment coding for a peptide of Region 2 with addition of an amino acid sequence at N-terminal or C-terminal thereof and with deletion of an amino acid sequence at the remaining N-terminal or C-terminal thereof, and a DNA fragment coding for a peptide of Region 2 with deletion of an amino acid sequence at N-terminal and/or C-terminal thereof. The amino acid sequence to be added or deleted may be of 1 to 200, preferably 30 to 150 amino acids in length. Preferable is a DNA fragment coding for a peptide derived from HMTp210 protein of A.pg-A having an amino acid sequence selected from the group consisting of SEQ ID NOs: 1, 27, 28, 29, 30, 31, 32, 33, 34 and 35 and a peptide derived from HMTp210 protein of A.pg-C having an amino acid sequence selected from the group consisting of SEQ ID NOs: 2, 3, 4, 5, 6, 7, 50, 51, 52, 53, 54, 55 and 56. A DNA fragment coding for a mutant of the above peptide may also be used wherein one or several amino acids are deleted, added or replaced. A "mutant of the above peptide wherein one or several amino acids are deleted, added or replaced" as used herein refers to a mutant of the above peptide wherein 1, 2, 3, 4 or 5 amino acids are deleted, added or replaced. A DNA fragment coding for such a mutant peptide may be obtained by hybridization with a DNA fragment having a nucleotide sequence complementary to the nucleotide sequence of the DNA fragment coding for the above peptide under stringent condition or a method for introducing mutation such as site directed mutagenesis. These may be done by using kits commercially available.

[0064] Any combination of a DNA fragment derived from the HMTp210A gene and a DNA fragment derived from the HMTp210C gene may be used as far as a resulting peptide may form an inclusion body. For instance, a DNA fragment coding for a fusion peptide may be a DNA fragment derived from the HMTp210A gene downstream of which a DNA fragment derived from the HMTp210C gene is bound or vice versa. DNA fragments coding for a fusion peptide may also be combined to each other in tandem. Also, two or more DNA fragments derived from the HMTp210A gene may be bound to each other and downstream thereof two or more DNA fragments derived from the HMTp210C gene may further be bound. A DNA coding for fusion peptide may consists of a DNA fragment derived from the HMTp210A gene and a DNA fragment derived from the HMTp210C gene at a ratio of 1 of the former to 1 to 3 of the latter. Preferably, said ratio is 1:1. A nucleotide sequence of the obtained DNA fragment, after cloning into pBluescript II SK+ (Stratagne) or pCR2.1-TOPO (Invitrogen), may be determined with a DNA sequencer (ABI Prism 377 Applied Biosystems).

[0065] The thus obtained DNA fragments of A.pg-A and A.pg-C or the DNA fragment coding for a fusion peptide may be incorporated into an appropriate expression vector, which may then be introduced into a host for expression of each of the DNA fragments. For expression of a heterologous protein or peptide, bacteria, yeasts, animal cells, plant cells, insect cells, and the like may ordinarily be used, among which any host may be used as far as an inclusion body may be produced. For transformation of a host cell, methods known in the art may be used. For instance, calcium phosphate, DEAE dextran, approach using liposome such as lipofectin, polyethylene glycol fusion of protoplast, electroporation, heat shock, and the like may be used, as appropriately selected depending on a host cell as used. Preferably, E. coli may be used which allows for expression in a large amount.

[0066] For expression in E. coli, various expression vectors having trp promoter, T7 promoter, cspA promoter, and the like have been developed and commercially available and may be used as appropriate. Such an expression vector includes, for instance, pET-11d (Merck) and pQE30 (Quiagen). Depending on an expression vector, suitable E. coli such as BL21, HMS174, DH5a, HB101, JM109, and the like may be selected as a host. Transformation of E. coli may be conducted using commercially available competent cells in accordance with protocol attached thereto. Thus, recombinant E. coli producing the desired polypeptide may be obtained. For culture medium (e.g. LB, SOC, SOB, and the like) used for culture of E. coli, reagents used for selection of transformant (e.g. ampicillin) and reagents used for induced expression (e.g. indole acetic acid (IAA), isopropylthio-β-D-galactoside (IPTG), and the like), commercially available ones may be used. A pH of a culture medium may be within a range suitable for growth of E. coli (pH 6 to 8).

[0067] Screening of recombinant E. coli expressing a desired peptide (the object) may be carried out as described below. Cells cultured and grown in the presence of an expression inducer (IPTG was used in an expression system in the present invention) are collected by centrifugation (9,100 g, 5 minutes), suspended in a fixed volume of distilled water or PBS, disrupted by sonication or a homogenizer such as French press or Manton Golin and subject to centrifugation (e.g. 17,800 g, 15 minutes) for separation and recovery in precipitate and supernatant. To distilled water may appropriately be added a surfactant (e.g. Triton X-100), a chelating agent (e.g. EDTA), lisozyme, and the like. A fixed amount of supernatant and precipitate recovered may be subject to SDS-polyacrylamide gel electrophoresis, and after staining with Coomassie Brilliant Blue, expression of the object may be confirmed by a molecular size and stained image. For confirmation (or detection) of the object, approach based on an antigen-antibody reaction such as ELISA, Western blot, dot blot, and the like may also be used other than approach based on a molecular size as described above. All of these approaches are commonly used for detecting a heterologous protein or polypeptide expressed in E. coli and may be selected as appropriate. Thus, clones recovered in the precipitate, i.e. clones producing a fusion peptide that may form an inclusion body, may be selected.

[0068] Recovery of an inclusion body from the clones producing a fusion peptide may be carried out as described below. First, cells may be collected using centrifugation or MF membrane of a suitable size (Asahi Kasei Corporation). The collected cells may be disrupted in an appropriate manner so as to release inclusion bodies consisting of a fusion peptide out of the cells. Disruption of cells may be done by any known methods including, for instance, dissolution with a chemical substance, a surfactant, an enzyme, or physical treatment such as French press or sonication. By combining several of these, cells may be disrupted more effectively.

[0069] For instance, after the cells collected with MF membrane were diluted and concentrated with deionized water to remove the remaining culture components and the cellular metabolites, an appropriate buffer and lysozyme may be added and the resulting mixture may be left at a low temperature (4 to 15° C.) overnight to thereby dissolve the cellular membrane of the cells. The treated solution of the cells may be subject to French press (or Manton Golin) at 500 to 600 kg/cm² to disrupt the cells. A buffer may be of any kind as far as it has a buffering ability at a pH range of 7.5 to 9 at which lysozyme is active, such as Tris buffer. The buffer may be used at a concentration as commonly used as a buffer (10 to 50 mM). Lysozyme may be used at a concentration of 0.3 to 1.0 g/L. For instance, 20 mM Tris buffer at pH 8.5 may be added, lysozyme (0.6 g/L) may be added and the mixture may be left to stand at 4° C. overnight to dissolve the cell wall of the cells. After disrupting the cells with French press, dilution and concentration with a buffer or deionized water and MF membrane may be repeated to remove most of cellular components. Optionally, a surfactant such as Triton-X100 may be added. Inclusion bodies may be recovered by centrifugation of a concentrated solution containing inclusion bodies as precipitate.

[0070] The recovered inclusion bodies may be dissolved in a solution containing a denaturing agent. A denaturing agent to be used includes urea, guanidine hydrochloride, and the like with urea being preferable. Such urea and guanidine hydrochloride may be used in a range of concentration of 4 to 8 M and 2 to 6 M, respectively. For the present invention, 8M urea may preferably be used. For dissolving a denaturing agent and a reducing agent, a buffer at pH 6 to 9, preferably at pH 7 to 8, may be used. Any buffer that has a buffering ability at the above pH range may be used such as phosphate buffer, Tris buffer, glycine buffer, carbonate buffer, and the like. Dissolution may be performed at a temperature of 40° C. or less. Dissolution time may be set while observing dissolution of inclusion bodies, and usually 30 minutes to 1 hour.

[0071] Next, refolding, i.e. reconstruction of a normal steric structure, of a fusion peptide may be carried out by adding 10 to 20-fold volume of a buffer to the solution of inclusion bodies or by dialyzing the solution against a buffer. For refolding, the same kind, temperature and pH of a buffer as those used for dissolution of inclusion bodies may be employed. Refolding may be carried out at room temperature or less and by being left to stand for 1 to 7 days, preferably, for 3 to 4 days.

[0072] The solution containing fusion peptide may further be subject to purification procedure as occasion demands. For such purification procedure, a combination of the methods commonly used in the field of protein chemistry may be used such as e.g. centrifugation, salting-out, ultrafiltration, isoelectric focusing, electrophoresis, ion exchange chromatography, gel filtration chromatography, affinity chromatography, hydrophobic chromatography, hydroxyapatite chromatography, and the like. An amount of the obtained protein or polypeptide may be measured with a reagent for protein measurement such as BCA Protein Assay Reagent Kit (Pierce Biotechnology, Inc), Protein Assay Kit (BIO-RAD, Inc), and the like.

[0073] Usefulness of the fusion peptide of present invention as an avian infectious coryza vaccine may be demonstrated by immunizing chicken with a solution containing said fusion peptide and determining an antibody titer to A.pg-A and A.pg-C in sera obtained from the chicken or by challenging said immunized chicken with virulent bacteria and observing survival of the chicken and clinical symptoms such as a running nose, swelling of the face and epiphora. For immunization of chicken, an immune enhancing agent (adjuvant), as used for ordinary pharmaceutical preparation, may optionally be added. A mode of administration is not particularly restricted and administration may be done, for instance, subcutaneously, intradermally, intraperitoneally, or intranasally, oridinarily once to thrice every 2 to 4 weeks.

[0074] For preparing a pharmaceutical preparation containing the fusion peptide of the present invention as a vaccine, a solution containing said fusion peptide may be sterile filtered through membrane filter and to the filtrate may be added, as occasion demands, an immune enhancing agent (adjuvant) such as aluminum hydroxide, aluminum phosphate, mineral oil or non-mineral oil, a stabilizing agent such as Polysorbate 80, amino acids, and sugars, e.g. lactose and sucrose, and a preservative agent such as formalin, thimerosal, 2-phenoxyethanol, benzyl alcohol, benzethonium chloride and benzalkonium chloride. Also, by adding sugars effective as an excipient such as lactose or sucrose, a lyophilized preparation may be prepared. Thus, a vaccine comprising as an active ingredient the fusion peptide of the present invention may be prepared.

[0075] The obtained vaccine may be used alone as an avian infectious coryza vaccine or alternatively used as a mixed vaccine in combination with at least one vaccine selected from the group consisting of vaccines against other viruses such as avian infectious bronchitis virus, avian infectious bursal disease virus, avian encephalomyelitis virus, and egg drop syndrome virus, vaccinesropagainst bacteria such as Salmonella typhimurium, Salmonella enteritidis, and Salmonella pollorum and vaccines against protozoa such as Leucocytozoon cauleryi, Eimeria tenera, and Eimeria maxima.

[0076] The present invention is explained in more detail by means of the following Examples but is not construed to be limited thereto.

EXAMPLE 1

Construction of Plasmids for Expression of Fusion Peptides

[0077] Genome DNA libraries of A.pg-A 221 strain and A.pg-C 53-47 strain were prepared in accordance with Tokunaga et. al. (Patent reference 1). Briefly, genomic DNAs were extracted using PureGene kit (Gentra Systems) from cells collected by centrifugation (Tomy, RD-20PIV, 4,400 g, 20 min.). Using the obtained DNAs as a template, PCR was performed with Prime STAR HS DNA Polymerase (TAKARA BIO Inc.) to amplify DNA fragments of HMTp210 protein genes of A.pg-A and A.pg-C. PCR conditions were as follows: after reaction at 98° C. for 1 minute, denaturation (98° C. for seconds), annealing (55° C. for 15 seconds), and elongation reaction (72° C. for 120 seconds) for 15 cycles, followed by termination reaction (72° C. for 7 minutes).

[0078] Table 1 shows names and Sequence ID NOs of the respective DNA fragments and PCR primers used in the amplification reaction. NcoI recognition sequence was added to the 5'-primer and BamHI recognition sequence was added to the 3'-primer used for amplification of the DNA fragments of A.pg-A and BamHI recognition sequence was added to both the 5'-primer and the 3'-primer used for amplification of the DNA fragments of A.pg-C. FIGS. 1 and 2 show relative position of the respective DNA fragments. In Table, SEQ ID NOs indicated in the column of DNA fragments denote amino acid sequences coded by the respective DNA fragments.

TABLE-US-00001 TABLE 1 DNA fragment 5'-primer 3'-primer AΔ5-1 AΔ5-1-P5 AΔ5-1-P3 (SEQ ID NO: 1) (SEQ ID NO: 14) (SEQ ID NO: 15) CΔ4c-1 CΔ4c-1-P5 CΔ4-5-P3 (SEQ ID NO: 2) (SEQ ID NO: 16) (SEQ ID NO: 17) CΔ5-1 CΔ5-1-P5 CΔ4-5-P3 (SEQ ID NO: 3) (SEQ ID NO: 18) (SEQ ID NO: 17) CΔ6b-1b CΔ6b-1b-P5 CΔ6b-1b-P3 (SEQ ID NO: 4) (SEQ ID NO: 19) (SEQ ID NO: 20)

[0079] Expression plasmids were prepared as described below. First, AΔ5-1 was digested with NcoI and BamHI and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). The obtained fragments were linked to an expression vector pET-lid (Merck) digested previously with NcoI and BamHI and the resulting plasmid was used to transform E. coli BL21(DE3) strain (Merck). From this transformant, expression plasmid (pET-11d-AΔ5-1) was extracted using Wizard Plus SV Minipreps DNA Purification System (Promega).

[0080] Next, CΔ4c-1, CΔ5-1 and CΔ6b-1b were digested with BamHI and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). The obtained fragments were linked in a forward orientation to pET-11d-AΔ5-1 digested previously with BamHI and the resulting plasmid was used to transform E. coli BL21(DE3) strain (Merck) to give expression plasmids pET-11d-AΔ5-1-CΔ4c-1, pET-11d-AΔ5-1-CΔ5-1 and pET-11d-AΔ5-1-CΔ6b-1b. In each of the constructed expression plasmids, CΔ4c-1, CΔ5-1 and CΔ6b-1b were inserted directly downstream of AΔ5-1 in a forward orientation which produce the fusion peptides as shown in Table 2.

TABLE-US-00002 TABLE 2 Plasmid Fusion peptide pET-11d-AΔ5-1-CΔ4c-1 AΔ5-1/CΔ4c-1 (SEQ ID NO: 8) pET-11d-AΔ5-1-CΔ5-1 ACΔ5-1 (SEQ ID NO: 9) pET-11d-AΔ5-1-CΔ6b-1b AΔ5-1/CΔ6b-1b (SEQ ID NO: 10)

EXAMPLE 2

Construction of Plasmids for Expression of Fusion Peptides With Addition of Linker

[0081] For addition of a linker sequence, DNA fragments of HMTp210 protein gene of A.pg were amplified as described in Example 1. Table 3 shows names and Sequence ID NOs of the respective DNA fragments and PCR primers used in the amplification reaction. The 5'-primer was added with XbaI recognition sequence and the 3'-primer was added with BamHI recognition sequence. In Table, SEQ ID NOs indicated in the column of DNA fragments denote amino acid sequences coded by the respective DNA fragments.

TABLE-US-00003 TABLE 3 DNA fragment 5'-primer 3'-primer AΔ5-1 AΔ5-1-P5 AΔ5-1-P3 (SEQ ID NO: 1) (SEQ ID NO: 14) (SEQ ID NO: 15) L-CΔ4c-1 CΔ4c-1-L-P5 CΔ4-5-P3 (SEQ ID NO: 5) (SEQ ID NO: 21) (SEQ ID NO: 17) L-CΔ5-1 CΔ5-1-L-P5 CΔ4-5-P3 (SEQ ID NO: 6) (SEQ ID NO: 22) (SEQ ID NO: 17) L-CΔ6b-1b CΔ6b-1b-L-P5 CΔ6b-1b-P3 (SEQ ID NO: 7) (SEQ ID NO: 23) (SEQ ID NO: 20)

[0082] Expression plasmids where a linker is linked directly downstream of AΔ5-1 were prepared as described below. First, AΔ5-1 obtained in Example 1 was digested with NcoI and BamHI and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). Next, to the C-terminal of the obtained fragments was added with a DNA synthetase a linker sequence consisting of a nucleotide sequence coding for ten glycine residues (Gly Linker: SEQ ID NO: 24) to give a DNA fragment (AΔ5-1-L). As a consequence of addition of the linker sequence, Bam HI recognition sequence at the C-terminal of AΔ5-1 is lost and instead thereof XbaI recognition sequence is generated.

[0083] Next, CΔ4c-1, CΔ5-1 and CΔ6b-1b were digested with XbaI and BamHI and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). The obtained fragments were ligated with AΔ5-1 and then digested with BamHI. After separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). Further, the obtained fragments were inserted into an expression vector pET-lid (Merck) previously digested with NcoI and BamHI. The resulting expression plasmid was used to transform E. coli BL21(DE3) strain (Merck) to give expression plasmids pET-11d-AΔ5-1-L-CΔ4c-1, pET-11d-AΔ5-1-L-CΔ5-1 and pET-11d-AΔ5-1-L-CΔ6b-1b. In each of the constructed expression plasmids, CΔ4c-1, CΔ5-1 and CΔ6b-1b were inserted directly downstream of the linker sequence in a forward orientation which produce the fusion peptides via glycine derived from the linker sequence as shown in Table 4.

TABLE-US-00004 TABLE 4 Plasmid Fusion peptide pET-11d-AΔ5-1-L-CΔ4c-1 AΔ5-1/L-CΔ4c-1 (SEQ ID NO: 11) pET-11d-AΔ5-1-L-CΔ5-1 ACΔ5-1-L (SEQ ID NO: 12) pET-11d-AΔ5-1-L-CΔ6b-1b AΔ5-1/L-CΔ6b-1b (SEQ ID NO: 13)

EXAMPLE 3

Construction of Plasmids for Expression of Shortened Fusion Peptides (1)

[0084] Genome DNA libraries of A.pg-A 221 strain were prepared as described in Example 1. PCR was performed to amplify the DNA fragments shown in Table 5. PCR conditions were as follows: after reaction at 98° C. for 1 minute, denaturation (98° C. for 10 seconds), annealing and elongation reactions (70° C. for 120 seconds) for 15 cycles, followed by termination reaction (72° C. for 7 minutes). Expression plasmids containing these fragments, pET-11d-AΔ5-1, pET-11d-AΔ5-2, pET-11d-AΔ5-3, pET-11d-AΔ5-4, pET-11d-AΔ9-2, pET-11d-AΔ9-3, pET-11d-AΔ9-4, pET-11d-AΔ6-2, pET-11d-AΔ6-3 and pET-11d-AΔ6-4, were extracted. Table 5 shows names and Sequence ID NOs of the respective DNA fragments and PCR primers used in the amplification reaction. The 5'-primer was added with NcoI recognition sequence and the 3'-primer was added with BamHI recognition sequence. FIG. 4 shows relative position of the respective DNA fragments. In Table, SEQ ID NOs indicated in the column of DNA fragments denote amino acid sequences coded by the respective DNA fragments.

TABLE-US-00005 TABLE 5 DNA fragment 5'-primer 3'-primer AΔ5-1 AΔ5-1-P5 AΔ5-1-P3 (SEQ ID NO: 1) (SEQ ID NO: 14) (SEQ ID NO: 15) AΔ5-2 AΔ5-1-P5 AΔ2-P3 (SEQ ID NO: 27) (SEQ ID NO: 14) (SEQ ID NO: 38) AΔ5-3 AΔ5-1-P5 AΔ3-P3 (SEQ ID NO: 28) (SEQ ID NO: 14) (SEQ ID NO: 39) AΔ5-4 AΔ5-1-P5 AΔ4-P3 (SEQ ID NO: 29) (SEQ ID NO: 14) (SEQ ID NO: 40) AΔ9-2 AΔ9-P5 AΔ2-P3 (SEQ ID NO: 30) (SEQ ID NO: 36) (SEQ ID NO: 38) AΔ9-3 AΔ9-P5 AΔ3-P3 (SEQ ID NO: 31) (SEQ ID NO: 36) (SEQ ID NO: 39) AΔ9-4 AΔ9-P5 AΔ4-P3 (SEQ ID NO: 32) (SEQ ID NO: 36) (SEQ ID NO: 40) AΔ6-2 AΔ6-P5 AΔ2-P3 (SEQ ID NO: 33) (SEQ ID NO: 37) (SEQ ID NO: 38) AΔ6-3 AΔ6-P5 AΔ3-P3 (SEQ ID NO: 34) (SEQ ID NO: 37) (SEQ ID NO: 39) AΔ6-4 AΔ6-P5 AΔ4-P3 (SEQ ID NO: 35) (SEQ ID NO: 37) (SEQ ID NO: 40)

[0085] Next, CΔ5-1 obtained in Example 1 was digested with BamHI and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). Further, the obtained fragments were linked in a forward orientation to pET-11d-AΔ5-1, pET-11d-AΔ5-2, pET-11d-AΔ5-3, pET-11d-AΔ5-4, pET-11d-AΔ9-2, pET-11d-AΔ9-3, pET-11d-AΔ9-4, pET-11d-AΔ6-2, pET-11d-AΔ6-3 and pET-11d-AΔ6-4 previously digested with BamHI. The resulting expression plasmids were used to transform E. coli BL21(DE3) strain (Merck) to give expression plasmids pET-11d-AΔ5-1-CΔ5-1, pET-11d-AΔ5-2-CΔ5-1, pET-11d-AΔ5-3-CΔ5-1, pET-11d-AΔ5-4-CΔ5-1, pET-11d-AΔ9-2-CΔ5-1, pET-11d-AΔ9-3-CΔ5-1, pET-11d-AΔ9-4-CΔ5-1, pET-11d-AΔ6-2-CΔ5-1, pET-11d-AΔ6-3-CΔ5-1 and pET-11d-AΔ6-4-CΔ5-1. In each of the constructed expression plasmids, CΔ5-1 was inserted directly downstream of the Peptide A expression gene in a forward orientation which produce the fusion peptides as shown in Table 6.

TABLE-US-00006 TABLE 6 Plasmid Fusion peptide pET-11d-AΔ5-1-CΔ5-1 ACΔ5-1 (SEQ ID NO: 9) pET-11d-AΔ5-2-CΔ5-1 AΔ5-2/CΔ5-1 (SEQ ID NO: 41) pET-11d-AΔ5-3-CΔ5-1 AΔ5-3/CΔ5-1 (SEQ ID NO: 42) pET-11d-AΔ5-4-CΔ5-1 AΔ5-4/CΔ5-1 (SEQ ID NO: 43) pET-11d-AΔ9-2-CΔ5-1 AΔ9-2/CΔ5-1 (SEQ ID NO: 44) pET-11d-AΔ9-3-CΔ5-1 AΔ9-3/CΔ5-1 (SEQ ID NO: 45) pET-11d-AΔ9-4-CΔ5-1 AΔ9-4/CΔ5-1 (SEQ ID NO: 46) pET-11d-AΔ6-2-CΔ5-1 AΔ6-2/CΔ5-1 (SEQ ID NO: 47) pET-11d-AΔ6-3-CΔ5-1 AΔ6-3/CΔ5-1 (SEQ ID NO: 48) pET-11d-AΔ6-4-CΔ5-1 AΔ6-4/CΔ5-1 (SEQ ID NO: 49)

EXAMPLE 4

Construction of Plasmids for Expression of Shortened Fusion Peptides (2)

[0086] Genome DNA libraries of A.pg-C 53-47 strain were prepared as described in Example 1 to give the DNA fragments shown in Table 7. PCR conditions were as described in Example 3. Table 7 shows names and Sequence ID NOs of the respective DNA fragments and PCR primers used in the amplification reaction. Both the 5'-primer and the 3'-primer were added with BamHI recognition sequence. FIG. 5 Shows relative position of the respective DNA fragments. In Table, SEQ ID NOs indicated in the column of DNA fragments denote amino acid sequences coded by the respective DNA fragments.

TABLE-US-00007 TABLE 7 DNA fragment 5'-primer 3'-primer CΔ5-1 CΔ5-1-P5 CΔ4-5-P3 (SEQ ID NO: 3) (SEQ ID NO: 18) (SEQ ID NO: 17) CΔ5-2 CΔ5-1-P5 CΔ2-P3 (SEQ ID NO: 50) (SEQ ID NO: 18) (SEQ ID NO: 58) CΔ5-4 CΔ5-1-P5 CΔ4-P3 (SEQ ID NO: 51) (SEQ ID NO: 18) (SEQ ID NO: 59) CΔ9-0 CΔ9-P5 CΔ0-P3 (SEQ ID NO: 52) (SEQ ID NO: 57) (SEQ ID NO: 60) CΔ9-2 CΔ9-P5 CΔ2-P3 (SEQ ID NO: 53) (SEQ ID NO: 57) (SEQ ID NO: 58) CΔ9-4 CΔ9-P5 CΔ4-P3 (SEQ ID NO: 54) (SEQ ID NO: 57) (SEQ ID NO: 59) CΔ6-2 CΔ6b-1b-P5 CΔ2-P3 (SEQ ID NO: 55) (SEQ ID NO: 19) (SEQ ID NO: 58) CΔ6-4 CΔ6b-1b-P5 CΔ4-P3 (SEQ ID NO: 56) (SEQ ID NO: 19) (SEQ ID NO: 59)

[0087] Next, as described in Example 1, CΔ5-1, CΔ5-4, CΔ9-0, CΔ9-2, C9-4, CΔ6-2 and CΔ6-4 were digested with BamHI and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). The obtained fragments were linked in a forward orientation to pET-11d-A5-1 previously digested with BamHI to give expression plasmids pET-11d-AΔ5-1-CΔ5-1, pET-11d-AΔ5-1-CΔ5-2, pET-11d-AΔ5-1-CΔ5-4, pET-11d-AΔ5-1-CΔ9-0, pET-11d-AΔ5-1-CΔ9-2, pET-11d-AΔ5-1-CΔ9-4, pET-11d-AΔ5-1-CΔ6-2 and pET-11d-AΔ5-1-CΔ-4. In each of the constructed expression plasmids, CΔ5-1, CΔ5-2, CΔ5-4, CΔ9-0, CΔ9-2, CΔ9-4, CΔ6-2 and CΔ6-4 were inserted directly downstream of AΔ5-1 in a forward orientation which produce the fusion peptides as shown in Table 8.

TABLE-US-00008 TABLE 8 Plasmid Fusion peptide pET-11d-AΔ5-1-CΔ5-1 ACΔ5-1 (SEQ ID NO: 12) pET-11d-AΔ5-1-CΔ5-2 AΔ5-1/CΔ5-2 (SEQ ID NO: 61) pET-11d-AΔ5-1-CΔ5-4 AΔ5-1/CΔ5-4 (SEQ ID NO: 62) pET-11d-AΔ5-1-CΔ9-0 AΔ5-1/CΔ9-0 (SEQ ID NO: 63) pET-11d-AΔ5-1-CΔ9-2 AΔ5-1/CΔ9-2 (SEQ ID NO: 64) pET-11d-AΔ5-1-CΔ9-4 AΔ5-1/CΔ9-4 (SEQ ID NO: 65) pET-11d-AΔ5-1-CΔ6-2 AΔ5-1/CΔ6-2 (SEQ ID NO: 66) pET-11d-AΔ5-1-CΔ6-4 AΔ5-1/CΔ6-4 (SEQ ID NO: 67)

EXAMPLE 5

Construction of Plasmids for Expression of Peptide C

[0088] Genome DNA libraries of A.pg-C 53-47 strain were prepared as described in Example 1 to give DNA fragments similar to those shown in Table 7. PCR conditions were as described in Example 3. Names and Sequence ID NOs of the respective DNA fragments and PCR primers used in the amplification reaction were the same as in Table 7 with exception that a restriction enzyme recognition sequence in the 3'-primer was changed from BamHI recognition sequence to HindIII recognition sequence so that the amplified fragments may be inserted into expression vector pQE30 (QIAGEN) more efficiently.

[0089] Next, CΔ5-1, CΔ5-2, CΔ5-4, CΔ9-0, CΔ9-2, CΔ9-4, CΔ6-2 and CΔ6-4 were digested with BamHI and HindIII and, after separation by 0.8% agarose gel electrophoresis, the DNA fragments were eluted and recovered using Wizard SV Gel and PCR Clean-Up System (Promega). The obtained fragments were linked to expression vector pQE30 digested with BamHI and HindIII. The resulting expression plasmids were used to transform E. coli JM109 strain (QIAGEN) to give plasmids expressing CΔ5-1, CΔ5-2, CΔ5-4, CΔ9-0, CΔ9-2, CΔ9-4, CΔ6-2 and CΔ6-4. The amino acid sequences of peptides obtained from these expression plasmids are those coded by the respective DNA fragments shown in Table 7 with addition at their N-terminal of histidine tag sequence (MRGSHHHHHHGS) derived from the vectors.

EXAMPLE 6

Expression of Fusion Peptide (1)

[0090] E. coli BL21 (DE3) strain (Merck) possessing the respective expression plasmids obtained in Examples 1 and 2 were inoculated to 1 to 5 mL of LB medium containing 50 μg/mL ampicillin and shake cultured while shaking at 30 to 37° C. until OD₆₀₀ of the culture fluid reached 0.5. IPTG was then added at a final concentration of 1 mM and culture was continued for 3 hours. After centrifugation (Torry, MX-300, 9,100 g, 5 minutes), supernatant was discarded, a washing buffer (PBS) was added at an amount equivalent to the amount of the initial culture fluid and the cells were suspended to uniformity. The suspension was subject to sonication under ice cooling using handy sonicater (Torry, UR-20P) at power 10 for 10 seconds for ten times and centrifuged at 17,800 g for 15 minutes. The supernatant was isolated and to the precipitate was added, a washing buffer at an amount equivalent to the amount of the sonicated solution before centrifugation and the precipitate was suspended to uniformity. To each of the isolated supernatant and the precipitate was added an equivalent amount of a sample buffer (2×SDS) and, after heating in boiled water for 5 minutes, SDS-PAGE and staining with Coomassie Brilliant Blue were performed in the conventional manner. When the fusion peptides were observed in the precipitate suspension, it was judged that said fusion peptides formed an inclusion body. FIG. 3 shows the respective expression patterns.

[0091] When expressed alone, CΔ4c-1 was expressed in a soluble fraction and fraction of CΔ5-1 expression was not constant whereas all the fusion peptides were stably expressed as an inclusion body. Regarding an expression level, it was somewhat low for AΔ5-1/CΔ4c-1 and was almost equal to each other for the remaining two fusion peptides ACΔ5-1 and AΔ5-1/CΔ6b-1b with good expression. The fusion peptides with addition of linker showed an expression level equivalent to that of the fusion peptides without addition of linker.

EXAMPLE 7

Immunogenicity of Fusion Peptide (1)

[0092] To confirm the vaccine efficacy of the fusion peptides, a challenge test was carried out using homologous virulent strain. The inclusion bodies in the precipitate suspension of ACΔ5-1 and ACΔ5-1-L obtained in Example 6 were solubilized with 8M urea and the buffer was replaced with PBS (pH 7.4) using a dialysis membrane. A vaccine prepared by emulsifying ACΔ5-1 at the amount of antigen shown in Table 9 in 0.5 mL per dose with oil adjuvant was once administered intramuscularly to the leg of SPF chickens of 8 weeks old for immunization. As a control, group administered with commercially available oil-adjuvanted vaccine with inactivated cells (OILVAX NB₂AC, Juridical Foundation The Chemo-Sero-Therapeutic Research Institute) and group with no administration were set. Four weeks after immunization, 0.2 mL of a solution containing A.pg-A 221 strain (1.0×10¹⁰ CFU/mL) or A.pg-C 53-47 strain (3.0×10⁹ CFU/mL) was administered intranasally and clinical symptoms of a running nose, swelling of the face and epiphora were observed for a week.

[0093] As a result, as shown in Table 9, chicken administered with the fusion peptides exhibited excellent protective efficacy against challenge from A.pg-A 221 strain and A.pg-C 53-47 strain and even at 0.06 μg/dose, the vaccine efficacy was more than that of 1/1,000 amount of the commercially available oil adjuvant vaccine. The peptides with addition of linker also exhibited the same protective efficacy. Thus, the fusion peptides proved to be useful as a vaccine.

TABLE-US-00009 TABLE 9 Protective rate to Amount of challenging strain Vaccine antigen A.pg-A 221 A.gp-C 53-47 ACΔ5-1 6 μg/dose 100% 100% 0.6 μg/dose 100% 100% 0.06 μg/dose 100% 100% ACΔ5-1-L 6 μg/dose 100% 100% (with linker 0.6 μg/dose 100% 100% addition) 0.06 μg/dose 100% 100% OILVAX 1/10-fold 100% 100% NB₂ AC 1/100-fold 100% 100% 1/1,000-fold 40% 20% No immunized -- 0% 0% control

EXAMPLE 8

Efficacy of Fusion Peptide to Heterologous Strain

[0094] To confirm the vaccine efficacy of the fusion peptides to the other strains (heterologous strains) than A.pg-A 221 strain and A.pg-C 53-47 strain used for preparing the fusion peptide, the challenge test was carried out as in Example 7. The procedures of Example 7 were repeated except that a different amount of antigen for immunization and different virulent strains, i.e. A.pg-A 083 strain (1.0×10⁹ CFU/mL), A.pg-A W strain (4.1×10⁹ CFU/mL) and A.pg-C Modesto strain (2.8×10⁹ CFU/mL), for challenge were used.

[0095] As a result, as shown in Table 10, chicken administered with the fusion peptides exhibited excellent protective efficacy against challenge from all the strains of A.pg-A 083, A.pg-A W and A.pg-C Modesto. Thus, the fusion peptides proved to be useful as a vaccine to other virulent strains from which the fusion peptides were not derived.

TABLE-US-00010 TABLE 10 Challenging Amount of Protection Vaccine strain antigen rate Peptide A A.pg-A 083 3 μg/dose 100% (AΔ5-1) 0.3 μg/dose 100% 0.03 μg/dose 40% A.pg-A W 3 μg/dose 100% 0.3 μg/dose 100% 0.03 μg/dose 40% Fusion A.pg-C 6 μg/dose 100% peptide Modesto 0.6 μg/dose 100% (ACΔ5-1) 0.06 μg/dose 100% OILVAX A.pg-A 083 1/10-fold 100% NB₂ AC 1/100-fold 100% 1/1,000-fold 20% A.pg-A W 1/10-fold 100% 1/100-fold 80% 1/1,000-fold 0% A.pg-A C 1/10-fold 100% Modesto 1/100-fold 80% 1/1,000-fold 20% No immunized A.pg-A 083 -- 0% control A.pg-A W -- 0% A.pg-C -- 0% Modesto

The respective strains used in the challenge test were analyzed for their nucleotide sequence of region 2. As a result, for A.pg-A, complete identity between 083 strain and W strain and 1 nucleotide mutation (A/G: glutamic acid at No. 1227 of SEQ ID NO: 25 is replaced with glycine) between 221 strain and 083 strain and between 221 strain and W strain were observed. For A.pg-C, deletion of 3 nucleotides AAG (glutamic acid at No. 1144 of SEQ ID NO: 26) was observed in Modesto strain as compared to 53-47 strain.

EXAMPLE 9

Comparison of Efficacy Between Fusion Peptide ACΔ5-1 and Respective Peptides

[0096] To compare the vaccine efficacy between the fusion peptide ACΔ5-1 and Peptide A or Peptide C before fusion, an immunization test was carried out. The vaccines were prepared as described in Example 7. A vaccine prepared by emulsifying ACΔ5-1, Peptide A or Peptide C at the amount of antigen shown in Table 11 in 0.5 mL per dose with oil adjuvant was once administered intramuscularly to the leg of SPF chickens of 4 weeks old for immunization. As a control, group with no administration was set. Four weeks after immunization, an antibody titer was determined as described by Ushijima et al. (Japanese patent application No. 2008-29589). Specifically, antibody measurement was carried out by ELISA.

[0097] The different peptides within Region 2 of A.pg-A and A.pg-C were diluted with 50 mM bicarbonate buffer to 1 μg/mL and each 50 μL of the solution was added to 96-well plate for immobilization. After adsorption at 4° C. overnight, the solution was discarded, and the plate was washed with 300 μL of PBS-T (8.1 mM disodium hydrogenphosphate, 1.5 mM potassium dihydrogenphosphate, 137 mM sodium chloride, 2.7 mM potassium chloride, 0.1% Tween 20) and added with 300 μL of PBS-T supplemented with 5% skim milk for blocking. The blocking solution was discarded. Serum was diluted with PBS-T supplemented with 10% skim milk to 100-fold and each 50 μL of the solution was added for reaction at room temperature for 1 hour. After removing the reaction solution, the plate was washed with PBS-T three times. An anti-chicken IgG-HRP-labeled antibody was diluted with PBS-T supplemented with 5% skim milk to 20,000-fold and each 50 μL of the solution was added to each well for reaction at room temperature for 30 minutes in the dark. After removing the reaction solution, the plate was washed with PBS-T three times. Each 100 μL of a substrate solution (TMB+substrate-chromogen: DAKO) was added for reaction at room temperature for 15 minutes. Each 100 μL of 3M sulfuric acid was added to stop the reaction. Absorbance at the wavelength of 450 nm was measured with 96-well plate reader (Molecular Devices Japan).

[0098] As a result, as shown in Table 11, the chicken immunized with the fusion peptide ACΔ5-1 exhibited a high antibody titer at 0.6 μg/dose and 100% of a positive conversion rate for both A.pg-A and A.pg-C. At 0.06 μg/dose of the fusion peptide, 80% and 40% of a positive conversion rate were observed for both A.pg-A _and A.pg-C, respectively. However, at 0.03 μg/dose of Peptide A or Peptide C, a positive conversion rate was 60% and 0% for A.pg-A and A.pg-C, respectively. Thus, it proved that the fusion peptide ACΔ5-1 had higher efficacy than Peptide A or Peptide C before fusion.

TABLE-US-00011 TABLE 11 Mean antibody titer Amount of (positive conversion rate) Vaccine antigen A.pg-A A.pg-C Fusion 6 μg/dose 2.152 (100%) 1.649 (100%) peptide 0.6 μg/dose 1.924 (100%) 1.177 (100%) (ACΔ5-1) 0.06 μg/dose 1.175 (80%) 0.565 (40%) 0.006 μg/dose 0.514 (60%) 0.112 (0%) Peptide A 3 μg/dose 2.051 (100%) 0.163 (0%) (AΔ5-1) 0.3 μg/dose 2.197 (100%) 0.146 (0%) 0.03 μg/dose 1.209 (60%) 0.086 (0%) 0.003 μg/dose 0.080 (0%) 0.127 (0%) Peptide C 3 μg/dose 0.153 (0%) 1.749 (100%) (CΔ5-1) 0.3 μg/dose 0.176 (0%) 1.865 (100%) 0.03 μg/dose 0.072 (0%) 0.089 (0%) 0.003 μg/dose 0.072 (0%) 0.084 (0%) No immunized -- 0.092 (0%) 0.099 (0%) control

EXAMPLE 10

Expression of Fusion Peptide (2)

[0099] E. coli BL21 (DE3) strain (Merck) possessing the respective expression plasmids obtained in Examples 3 and 4 were subject to expression as described in Example 6 and an expression level was determined. FIGS. 6 and 7 show the respective expression patterns. For Peptide A, AΔ5-4, AΔ9-2, AΔ9-4, AΔ6-2 and AΔ6-4, when expressed alone, were expressed in a soluble fraction but, upon fusion with CΔ5-1, the resulting fusion peptides stably formed an inclusion body except for AΔ6-4. AΔ6-4/CΔ5-1, though principally formed an inclusion body, may sometimes be expressed in a soluble fraction and hence its expression was instable. All the fusion peptides had the same and excellent expression level. On the other hand, Peptide C, when expressed alone, was expressed in a soluble fraction except for CΔ6-2 but, upon fusion with AΔ5-1, the resulting fusion peptides stably formed an inclusion body. All the fusion peptides had the same and excellent expression level.

EXAMPLE 11

Immunogenicity of Fusion Peptide (2)

[0100] To confirm the vaccine efficacy of the fusion peptides obtained in Example 10, a challenge test was carried out using homologous virulent strain (A.pg-A 221 strain) as described in Example 7. The procedures of Example 7 were repeated except that a different amount of antigen for immunization and different number of cells of virulent strain, i.e. A.pg-A 221 strain, 1.2×10⁹ CFU/mL, for challenge were used. As a result, as shown in Table 12, chicken immunized with the respective fusion peptides exhibited excellent protective effects against challenge from A.pg-A 221 strain where 80% protection for AΔ6-4/CΔ5-1 and 100% protection for the longer fusion peptides were confirmed.

TABLE-US-00012 TABLE 12 Amount of Protection Vaccine antigen rate ACΔ5-1 6 μg/dose 100% AΔ5-2/CΔ5-1 6 μg/dose 100% AΔ5-3/CΔ5-1 6 μg/dose 100% AΔ5-4/CΔ5-1 6 μg/dose 100% AΔ9-2/CΔ5-1 6 μg/dose 100% AΔ9-3/CΔ5-1 6 μg/dose 100% AΔ9-4/CΔ5-1 6 μg/dose 100% AΔ6-2/CΔ5-1 6 μg/dose 100% AΔ6-3/CΔ5-1 6 μg/dose 100% AΔ6-4/CΔ5-1 6 μg/dose 80% No immunized -- 0% control

EXAMPLE 12

Expression of Peptide C

[0101] E. coli JM109 (QIAGEN) possessing the respective expression plasmids obtained in Example 5 were subject to expression as described in Example 6 and an expression level for the respective cells was determined by SDS-PAGE (FIG. 8). The thus obtained peptides were named as CΔ5-1-pQE, CΔ5-2-pQE, CΔ5-4-pQE, CΔ9-0-pQE, CΔ9-2-pQE, CΔ9-4-pQE, CΔ6-2-pQ and CΔ6-4-pQE. All the peptides except for CΔ6-2-pQE were expressed in a soluble fraction with an excellent expression level.

EXAMPLE 13

Confirmation of Protective Effect of Peptide C

[0102] To confirm the vaccine effect of Peptides C obtained in Example 12, a challenge test was carried out as described in Example 7. A vaccine prepared by emulsifying Peptide C at the amount of antigen shown in Table 13 with oil adjuvant was once administered intramuscularly to the leg of SPF chickens of 4 weeks old for immunization. Four weeks after immunization, 0.2 mL of a solution containing A.pg-C 53-47 strain (5.2×10⁹ CFU/mL) was administered intranasally and clinical symptoms of a running nose, swelling of the face and epiphora were observed for a week.

[0103] As a result, as shown in Table 13, chicken administered with CΔ5-1-pQE and CΔ9-0-pQE exhibited excellent protective effects at 3 μg/dose. The protective effect of 60% was observed for the shortest CΔ6-4-pQE. From these results, it is expected that, for the protective effects to A.pg-C, a sequence at the C-terminal of non-homologous region (Region 2) in relation to A.pg-A is important and it was proved that a comparatively high protective effects were exhibited if the peptide includes at least the region of CΔ6-4. Furthermore, as shown in Example 9, it is expected that immunogenicity may be improved upon expression in fusion than expressed alone.

TABLE-US-00013 TABLE 13 Amount of Protection Vaccine antigen rate CΔ5-1-pQE 3 μg/dose 100% CΔ9-0-pQE 3 μg/dose 100% CΔ9-2-pQE 3 μg/dose 60% CΔ6-4-pQE 3 μg/dose 60% No immunized -- 0% control

INDUSTRIAL APPLICABILITY

[0104] By using the present invention, a vaccine of avian infectious coryza caused by Avibacterium paragarinarum serotypes A and C may be provided.

Sequence CWU 1

1

691549PRTAvibacterium paragallinarumtype A 1Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Ala 545 2574PRTAvibacterium paragallinarumtype C 2Arg Gly Ser Gly Ser Gln Leu Tyr Ala Thr Asn Phe Met Leu Asn Lys 1 5 10 15 Leu Ala Gln Ser Val Lys Thr Asn Phe Gly Gly Asn Ala Asn Leu Ala 20 25 30 Thr Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp 35 40 45 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu 50 55 60 Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp 65 70 75 80 Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly 85 90 95 Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr 100 105 110 Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly 115 120 125 Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser 130 135 140 Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu 145 150 155 160 Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala 165 170 175 Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn 180 185 190 Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp 195 200 205 Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala 210 215 220 Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn 225 230 235 240 Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu 245 250 255 Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp 260 265 270 Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu 275 280 285 Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu 290 295 300 Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr 305 310 315 320 Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val 325 330 335 Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala 340 345 350 Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu 355 360 365 Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn 370 375 380 Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile 385 390 395 400 Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser 405 410 415 Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys 420 425 430 Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys 435 440 445 Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val 450 455 460 Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr 465 470 475 480 Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val 485 490 495 Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile Asp 500 505 510 Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly Asp 515 520 525 Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr Ala 530 535 540 Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu Val Ser Pro Thr 545 550 555 560 Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly 565 570 3545PRTAvibacterium paragallinarumtype C 3Arg Arg Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr 1 5 10 15 Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu 20 25 30 Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala 35 40 45 Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala 50 55 60 Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser 65 70 75 80 Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe 85 90 95 Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe 100 105 110 Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser 115 120 125 Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr 130 135 140 Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala 145 150 155 160 Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn 165 170 175 Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala 180 185 190 Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys 195 200 205 Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala 210 215 220 Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly 225 230 235 240 Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly 245 250 255 Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 260 265 270 Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln 275 280 285 Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly 290 295 300 Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn 305 310 315 320 Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys 325 330 335 Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala 340 345 350 Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr 355 360 365 Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu 370 375 380 Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser 385 390 395 400 Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln 405 410 415 Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp 420 425 430 Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile 435 440 445 Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr 450 455 460 Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr 465 470 475 480 Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala 485 490 495 Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln 500 505 510 Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu Val 515 520 525 Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser Thr Gln 530 535 540 Gly 545 4387PRTAvibacterium paragallinarumtype C 4Arg Gly Ser Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr 1 5 10 15 Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser 20 25 30 Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr 35 40 45 Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser 50 55 60 Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys 65 70 75 80 Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly 85 90 95 Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu 100 105 110 Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp 115 120 125 Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr 130 135 140 Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn 145 150 155 160 Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile 165 170 175 Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys 180 185 190 Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn 195 200 205 Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr 210 215 220 Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu 225 230 235 240 Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn 245 250 255 Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu 260 265 270 Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr 275 280 285 Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val 290 295 300 Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly 305 310 315 320 Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr 325 330 335 Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro 340 345 350 Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu 355 360 365 Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala 370 375 380 Thr Gly Ile 385 5573PRTAvibacterium paragallinarumtype C 5Ser Arg Gly Ser Gln Leu Tyr Ala Thr Asn Phe Met Leu Asn Lys Leu 1 5 10 15 Ala Gln Ser Val Lys Thr Asn Phe Gly Gly Asn Ala Asn Leu Ala Thr 20 25 30 Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr 35 40 45 Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser 50 55 60 Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala 65 70 75 80 Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile 85 90 95 Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val 100 105 110 Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu 115 120 125 Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly 130 135 140 Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr 145 150 155 160 Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu 165 170 175 Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu 180 185 190 Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu 195 200 205 Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu 210 215 220

His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr 225 230 235 240 Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala 245 250 255 Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly 260 265 270 Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg 275 280 285 Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys 290 295 300 Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp 305 310 315 320 Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys 325 330 335 Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser 340 345 350 Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr 355 360 365 Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile 370 375 380 Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val 385 390 395 400 Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly 405 410 415 Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala 420 425 430 Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu 435 440 445 Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr 450 455 460 Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala 465 470 475 480 Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val Asn 485 490 495 Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile Asp Gly 500 505 510 Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly Asp Ile 515 520 525 Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr Ala Leu 530 535 540 Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys 545 550 555 560 Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly 565 570 6543PRTAvibacterium paragallinarumtype C 6Ser Arg Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln 1 5 10 15 Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser 20 25 30 Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr 35 40 45 Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys 50 55 60 Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile 65 70 75 80 Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val 85 90 95 Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys 100 105 110 Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly 115 120 125 Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 130 135 140 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr 145 150 155 160 Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser 165 170 175 Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn 180 185 190 Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp 195 200 205 Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr 210 215 220 Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala 225 230 235 240 Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln 245 250 255 Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr 260 265 270 Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu 275 280 285 Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr 290 295 300 Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp 305 310 315 320 Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys 325 330 335 Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln 340 345 350 Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly 355 360 365 Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu 370 375 380 Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val 385 390 395 400 Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp 405 410 415 Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala 420 425 430 Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly 435 440 445 Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala 450 455 460 Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile 465 470 475 480 Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly 485 490 495 Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr 500 505 510 Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu Val Ser Pro 515 520 525 Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly 530 535 540 7386PRTAvibacterium paragallinarumtype C 7Ser Arg Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe 1 5 10 15 Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser 20 25 30 Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr 35 40 45 Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala 50 55 60 Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn 65 70 75 80 Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala 85 90 95 Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys 100 105 110 Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala 115 120 125 Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly 130 135 140 Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly 145 150 155 160 Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 165 170 175 Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln 180 185 190 Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly 195 200 205 Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn 210 215 220 Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys 225 230 235 240 Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala 245 250 255 Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr 260 265 270 Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu 275 280 285 Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser 290 295 300 Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln 305 310 315 320 Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp 325 330 335 Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile 340 345 350 Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr 355 360 365 Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr 370 375 380 Gly Ile 385 81119PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 8Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Gly Ser Gln Leu Tyr Ala Thr Asn Phe Met Leu Asn 545 550 555 560 Lys Leu Ala Gln Ser Val Lys Thr Asn Phe Gly Gly Asn Ala Asn Leu 565 570 575 Ala Thr Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln 580 585 590 Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser 595 600 605 Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr 610 615 620 Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys 625 630 635 640 Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile 645 650 655 Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val 660 665 670 Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys 675 680 685 Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly 690 695 700 Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 705 710 715 720 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr 725 730 735 Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser 740 745 750 Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn 755 760 765 Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp 770 775 780 Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr 785 790 795 800 Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala 805 810 815 Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln 820 825 830 Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr 835 840 845 Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu 850 855 860 Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr 865 870 875 880 Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp 885 890 895 Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys 900 905 910 Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln 915 920 925 Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly 930 935 940 Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu 945 950 955 960 Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val 965 970 975 Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp 980 985 990 Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala 995 1000

1005 Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn 1010 1015 1020 Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr 1025 1030 1035 Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala 1040 1045 1050 Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn 1055 1060 1065 Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr 1070 1075 1080 Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr 1085 1090 1095 Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr 1100 1105 1110 Ala Ser Ser Thr Gln Gly 1115 91089PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 9Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr 545 550 555 560 Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu 565 570 575 Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala 580 585 590 Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala 595 600 605 Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser 610 615 620 Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe 625 630 635 640 Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe 645 650 655 Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser 660 665 670 Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr 675 680 685 Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala 690 695 700 Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn 705 710 715 720 Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala 725 730 735 Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys 740 745 750 Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala 755 760 765 Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly 770 775 780 Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly 785 790 795 800 Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 805 810 815 Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln 820 825 830 Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly 835 840 845 Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn 850 855 860 Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys 865 870 875 880 Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala 885 890 895 Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr 900 905 910 Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu 915 920 925 Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser 930 935 940 Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln 945 950 955 960 Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp 965 970 975 Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile 980 985 990 Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr 995 1000 1005 Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala 1010 1015 1020 Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn 1025 1030 1035 Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr 1040 1045 1050 Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr 1055 1060 1065 Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr 1070 1075 1080 Ala Ser Ser Thr Gln Gly 1085 10932PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 10Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile 545 550 555 560 Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met 565 570 575 Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser 580 585 590 Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn 595 600 605 Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val 610 615 620 Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile 625 630 635 640 Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala 645 650 655 Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln 660 665 670 Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu 675 680 685 Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val 690 695 700 Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys 705 710 715 720 Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val 725 730 735 Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys 740 745 750 Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr 755 760 765 Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr 770 775 780 Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu 785 790 795 800 Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly 805 810 815 Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg 820 825 830 Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys 835 840 845 Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys 850 855 860 Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr 865 870 875 880 Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn 885 890 895 Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys 900 905 910 Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu 915 920 925 Ala Thr Gly Ile 930 111131PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 11Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120

125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly Ser Arg 545 550 555 560 Gly Ser Gln Leu Tyr Ala Thr Asn Phe Met Leu Asn Lys Leu Ala Gln 565 570 575 Ser Val Lys Thr Asn Phe Gly Gly Asn Ala Asn Leu Ala Thr Asp Gly 580 585 590 Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr Ile His 595 600 605 Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr 610 615 620 Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys 625 630 635 640 Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly 645 650 655 Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro 660 665 670 Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys 675 680 685 Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp 690 695 700 Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys 705 710 715 720 Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly 725 730 735 Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys 740 745 750 Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys 755 760 765 Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val 770 775 780 Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp 785 790 795 800 Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn 805 810 815 Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile 820 825 830 Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu 835 840 845 Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr 850 855 860 Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr 865 870 875 880 Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr 885 890 895 Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu 900 905 910 Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu 915 920 925 Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala 930 935 940 Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr 945 950 955 960 Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly 965 970 975 Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr 980 985 990 Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys 995 1000 1005 Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr Lys 1010 1015 1020 Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala 1025 1030 1035 Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val 1040 1045 1050 Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile 1055 1060 1065 Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp 1070 1075 1080 Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln 1085 1090 1095 Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu 1100 1105 1110 Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser 1115 1120 1125 Thr Gln Gly 1130 121101PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 12Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly Ser Arg 545 550 555 560 Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr 565 570 575 Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser 580 585 590 Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala 595 600 605 Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile 610 615 620 Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val 625 630 635 640 Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu 645 650 655 Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly 660 665 670 Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr 675 680 685 Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu 690 695 700 Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu 705 710 715 720 Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu 725 730 735 Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu 740 745 750 His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr 755 760 765 Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala 770 775 780 Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly 785 790 795 800 Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg 805 810 815 Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys 820 825 830 Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp 835 840 845 Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys 850 855 860 Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser 865 870 875 880 Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr 885 890 895 Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile 900 905 910 Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val 915 920 925 Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly 930 935 940 Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala 945 950 955 960 Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu 965 970 975 Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr 980 985 990 Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala 995 1000 1005 Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val 1010 1015 1020 Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile 1025 1030 1035 Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp 1040 1045 1050 Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln 1055 1060 1065 Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu 1070 1075 1080 Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser 1085 1090 1095 Thr Gln Gly 1100 13944PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 13Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala

Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly Ser Arg 545 550 555 560 Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys 565 570 575 Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly 580 585 590 Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 595 600 605 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr 610 615 620 Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser 625 630 635 640 Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn 645 650 655 Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp 660 665 670 Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr 675 680 685 Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala 690 695 700 Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln 705 710 715 720 Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr 725 730 735 Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu 740 745 750 Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr 755 760 765 Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp 770 775 780 Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys 785 790 795 800 Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln 805 810 815 Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly 820 825 830 Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu 835 840 845 Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val 850 855 860 Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp 865 870 875 880 Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala 885 890 895 Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly 900 905 910 Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala 915 920 925 Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile 930 935 940 1430DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 14catgccatgg atggcacaat tacatttaca 301536DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 15cgcggatcca ccttgagtgc tagatgctgt aggtgc 361639DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 16cgcggatccg gctcacagct ttatgcaacg aactttatg 391739DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 17cgcggatccc taaccttgag tgctagatgc tgtaggtgc 391833DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 18agacgcggat ccgatggcac aattacattt aca 331930DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 19cgcggatccg gcttaatgaa agacattgaa 302042DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 20cgcggatccc taaatacctg ttgccaaaat acctaccttt ga 422138DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 21gctctagagg ctcacagctt tatgcaacga actttatg 382235DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 22gctctagaga tggcacaatt acatttacaa atatt 352338DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 23gctctagagg cttaatgaaa gacattgaag gggtaaac 382430DNAArtificial SequenceDescription of Artificial Sequence Synthetic oligonucleotide 24ggcggaggtg gcggaggtgg cggaggtggc 30252042PRTAvibacterium paragallinarumtype A 25Met Asn Lys Val Phe Lys Ile Lys Tyr Ser Val Val Lys Gln Glu Met 1 5 10 15 Ile Val Val Ser Glu Leu Ala Asn Asn Lys Asp Lys Thr Ala Ser Gln 20 25 30 Lys Asn Thr His Asn Thr Ala Phe Phe Gln Pro Leu Phe Thr Lys Cys 35 40 45 Thr Tyr Leu Ala Leu Leu Ile Asn Ile Ala Leu Gly Ala Ser Leu Phe 50 55 60 Pro Gln Leu Ala Asn Ala Lys Trp Leu Glu Val Tyr Ser Ser Ser Val 65 70 75 80 Lys Leu Ser Thr Val Ser Ala Gln Ser Asn Ser Val Asn Leu Asn Pro 85 90 95 Ser Gly Ala Glu Ser Val Gly Thr Asn Ser Pro Gln Gly Val Ala Ile 100 105 110 Gly Tyr Gly Ala Thr Asn Asp Arg Ser Ala Thr Gly Ala Ile Ala Leu 115 120 125 Gly Val Gly Val Lys Asn Glu Thr Leu Ala Lys Asp Ser Ile Ala Ile 130 135 140 Gly Tyr Gly Ala Lys Asn Glu Ser Thr Ala Pro Ser Ser Val Thr Ile 145 150 155 160 Gly Lys Gln Ala Ile Asn Arg Phe Glu Lys Ser Ile Val Met Gly Leu 165 170 175 Asn Ala Tyr Thr Gln Leu Asp Pro Arg Gly Thr Ser Lys Glu Thr Arg 180 185 190 Gln Gly Ser Val Val Ile Gly Glu Asn Ala Lys Ser Ala Gly Asn Gln 195 200 205 Ser Val Ser Leu Gly Gln Asn Ser Trp Ser Lys Thr Asn Ser Ile Ser 210 215 220 Ile Gly Ala Gly Thr Phe Ala Glu Gly Lys Ser Ser Ile Ala Ile Gly 225 230 235 240 Thr Asp Lys Ile Ser Gly Thr Lys Tyr Asn Asp Lys Leu Pro Ala Thr 245 250 255 Ala Trp Asn Gly Thr Gly Thr Val Pro Lys Asn Ser Ile Trp Asp Ile 260 265 270 Phe Ser Glu Leu Tyr Met Gly Lys Gln Thr Asn Gly Arg Asp Tyr Asp 275 280 285 Thr Thr Thr Arg Asp Pro Asn Lys Pro Glu Ala Phe Tyr Lys Phe Ser 290 295 300 Asp Phe Lys Gly Lys Tyr Val Asn Thr Pro Thr Ala Ser Pro Thr Tyr 305 310 315 320 Ala Gly Lys Leu Gly Ala Ile Ala Leu Gly Ser Arg Thr Ile Ala Ala 325 330 335 Gly Glu Met Ser Thr Ala Val Gly Ser Leu Ala Phe Ala Leu Ala Asp 340 345 350 Arg Ser Thr Ala Met Gly Leu Arg Ser Phe Val Ala Lys Asp Ala Val 355 360 365 Gly Gly Thr Ala Ile Gly Glu Glu Ser Arg Thr Phe Ala Lys Asp Ser 370 375 380 Val Ala Ile Gly Asn Lys Thr Glu Ala Ser Asn Ala Gly Ser Met Ala 385 390 395 400 Tyr Gly Tyr Lys Ala Lys Ala Val Gly Ala Gly Ala Ile Ala Ile Gly 405 410 415 Thr Glu Val Ala Ala Gly Ala Lys Phe Asn Ser His Gln Thr Gly Asn 420 425 430 Leu Leu Gln Asp Asn Asn Ala Tyr Ala Thr Leu Lys Asn Ala Asp Lys 435 440 445 Ser Asp Asp Thr Lys Thr Gly Asn Ala Ile Thr Val Phe Thr Gln Ser 450 455 460 Phe Asp Asn Met Leu Thr Asn Gly Leu Pro Leu Val Ser Glu Asn Glu 465 470 475 480 Thr Tyr Leu Thr Thr Ser Ala Gly Ala Ile Lys Lys Thr Ala Thr Thr 485 490 495 Asp Ser Ser Ala Gly Gly Gly Lys Asn Ala Ile Ala Ile Gly Ser Lys 500 505 510 Thr Phe Ala Ser Lys Ala Asn Ser Val Ala Leu Gly Ser Tyr Ala Leu 515 520 525 Ala Asp Ala Gln Asn Ala Phe Ala Leu Gly Ser Tyr Ser Phe Val Glu 530 535 540 Ser Ser Ala Thr Asn Thr Ile Thr Ile Gly Val Gly Ser Tyr Ala Lys 545 550 555 560 Gly Lys Asn Ser Phe Leu Gly Gly Thr Trp Ala Ser Thr Leu Ser Asp 565 570 575 Arg Thr Val Val Leu Gly Asn Ser Thr Ser Ile Ser Ser Gly Ser Gln 580 585 590 Asn Ala Leu Ala Ile Gly Val Asn Val Phe Ile Gly Asn Asp Ser Ala 595 600 605 Ser Ser Leu Ala Leu Gly Met Gly Ser Thr Ile Ala Lys Ser Ala Lys 610 615 620 Ser Pro Asp Ser Leu Ala Ile Gly Lys Glu Ala Arg Ile Asp Ala Lys 625 630 635 640 Asp Thr Asp Asn Gly Thr Leu Tyr Gln Pro Gln Val Tyr Asp Glu Thr 645 650 655 Thr Arg Ala Phe Arg Asn Phe Asn Glu Ser Ser Asp Tyr Met Arg Gln 660 665 670 Ala Met Ala Leu Gly Phe Asn Ala Lys Val Ser Arg Gly Val Gly Lys 675 680 685 Met Glu Thr Gly Ile Asn Ser Met Ala Ile Gly Ala Tyr Ala Gln Ala 690 695 700 Thr Leu Gln Asn Ser Thr Ala Leu Gly Val Gly Ser Lys Thr Asp Tyr 705 710 715 720 Thr Trp Glu Gln Leu Glu Thr Asp Pro Trp Val Ser Glu Gly Ala Ile 725 730 735 Ser Ile Pro Thr Ser Gly Lys Thr Gly Val Ile Ser Val Gly Ser Lys 740 745 750 Gly Ser Glu Arg Arg Ile Val Asn Leu Ala Ser Gly Ser Ser Asp Thr 755 760 765 Asp Ala Val Asn Val Ala Gln Leu Lys Thr Val Glu Glu Arg Phe Leu 770 775 780 Ser Glu Ile Asn Leu Leu Gln Asn Gly Gly Gly Val Lys Tyr Leu Ser 785 790 795 800 Val Glu Lys Thr Asn Ile Asn Gly Gln Ser Gly Arg Val Ala Ser Gln 805 810 815 Ile Arg Lys Gly Glu Asn Tyr Glu Arg Tyr Val Lys Leu Lys Thr Gln 820 825 830 Leu Leu Tyr Leu Asp Ala Arg Gly Lys Leu Asn Gly Glu Lys Phe Asp 835 840 845 Gln Asn Ser Leu Asn Lys Ile Arg Ala Val Val Gln Glu Leu Glu Ala 850 855 860 Glu Tyr Ser Gly Glu Leu Lys Thr Thr Ala Ser Ala Leu Asn Gln Val 865 870 875 880 Ala Thr Gln Leu Glu Gln Glu Val Thr Thr Asn Asn Phe Asp Lys Phe 885 890 895 Asn Gln Tyr Lys Thr Gln Ile Glu Asn Ala Ser Asn Ala Asp Ser Ala 900 905 910 Arg Asn Val Gly Gly Leu Thr Pro Gln Ala Ile Ala Gln Leu Lys Ala 915 920 925 Asn Asn Asn Tyr Leu Asn Asp Gly Ala Lys Gly Gln Asp Ser Ile Ala 930 935 940 Phe Gly Trp Gln Ala Lys Thr Ser Gly Ala Asn Asn Gly Leu Ala Gly 945 950 955 960 Lys Gln Ala Ile Ala Ile Gly Phe Gln Ala Asn Ser Ser Ala Glu Asn 965 970 975 Ala Ile Ser Ile Gly Thr Asn Ser Asp Thr Ser Met Thr Gly Ala Val 980 985 990 Ala Ile Gly Lys Gly Ala Thr Val Thr Ala Gly Gly Lys Pro Ser Ile 995 1000 1005 Ala Leu Gly Gln Asp Ser Thr Val Ala Asn Ser Ala Ile Ser Arg 1010 1015 1020 Thr Ser Ser Pro Met Ile Asn Gly Leu Ile Phe Asn Asn Phe Ala 1025 1030 1035 Gly Ser Pro Glu Thr Leu Gly Val Leu Ser Ile Gly Thr Ala Gly 1040 1045 1050 Arg Glu Arg Lys Ile Val Asn Val Ala Ala Gly Asp Val Ser Gln 1055 1060 1065 Ala Ser Thr Glu Ala Ile Asn Gly Ser Gln Leu Tyr Ala Thr Asn 1070 1075 1080 Phe Met Leu Ser Lys Val Ala Gln Ser Val Lys Ser Asn Phe Gly 1085 1090 1095 Gly Asn Val Asn Leu Gly Thr Asp Gly Thr Ile Thr Phe Thr Asn 1100 1105 1110 Ile Gly Gly Thr Gly Gln Ala Thr Ile His Asp Ala Ile Asn Asn 1115 1120 1125 Val Leu Thr Lys Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro 1130 1135 1140 Thr Gly Asn Gln Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr 1145 1150 1155 Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys 1160 1165 1170 Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn Gly Thr Ile Leu 1175 1180 1185 Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile Thr Ala Gly 1190 1195 1200 Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu Asn 1205 1210 1215 Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 1220 1225 1230 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 1235 1240 1245 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser 1250 1255 1260 Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys 1265 1270 1275 Gln Val

Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile 1280 1285 1290 Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr 1295 1300 1305 Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 1310 1315 1320 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile 1325 1330 1335 Thr Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn 1340 1345 1350 Lys Ile Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu 1355 1360 1365 Ser Gly Lys Asn Ala Ile Thr Gly Leu Val Asp Val Val Lys Lys 1370 1375 1380 Thr Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Ser Asn Lys 1385 1390 1395 Lys Lys Thr Phe Thr Val Gly Val Asp Phe Thr Asp Thr Ile Thr 1400 1405 1410 Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr Thr Ser Lys Ser 1415 1420 1425 Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe Ser Thr Asp 1430 1435 1440 Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr Ala Asn 1445 1450 1455 Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile Lys 1460 1465 1470 Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 1475 1480 1485 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu 1490 1495 1500 Ser Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe 1505 1510 1515 Ala Lys Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu 1520 1525 1530 Lys Trp Arg Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp 1535 1540 1545 Ala Glu Ile Gln Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly 1550 1555 1560 Leu Ile Phe Ala Thr Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly 1565 1570 1575 Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly Asp 1580 1585 1590 Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr 1595 1600 1605 Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu Val Ser 1610 1615 1620 Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Asn Ala Asn Pro Thr 1625 1630 1635 Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly Trp Ala Thr 1640 1645 1650 Thr Ala Asn Thr Ala Gly Gly Val Ala Pro Ala Gly Asn Val Ala 1655 1660 1665 Thr Gly Asp Ile Ala Pro Thr Gln Pro Thr Leu Pro Glu Met Asn 1670 1675 1680 Thr Ala Leu Val Asp Asp His Leu Ala Val Pro Leu Gly Gly Ser 1685 1690 1695 Leu Lys Ile His Gly Asp His Asn Val Lys Thr Thr Ile Ser Ala 1700 1705 1710 Asp Asn Gln Val Gly Ile Ser Leu Gln Pro Asn Ile Ser Ile Glu 1715 1720 1725 Asn Asn Leu Val Ile Gly Ser Asn Asp Pro Glu Lys Ala Lys Leu 1730 1735 1740 Ala Ala Gln Glu Gly Asn Ala Leu Val Ile Thr Asn Lys Asp Asp 1745 1750 1755 Gly Asn Ala Ala Met Val Phe Asn Asn Glu Lys Asn Met Leu Val 1760 1765 1770 Leu Ser Asp Lys Glu Ala Lys Pro Arg Val Leu Leu Asp Gly Gln 1775 1780 1785 Asn Gly Ala Leu Thr Leu Val Gly Asn Asp Asp Ser Gln Val Thr 1790 1795 1800 Leu Ser Ser Lys Lys Gly Lys Asp Ile Asp Gly Asn Asp Leu Ser 1805 1810 1815 Arg Leu Ser Val Thr Thr Glu Arg Thr Asn Ala Asp Gly Gln Leu 1820 1825 1830 Glu Lys Val Glu Thr Ser Phe Ala Thr Met Asp Asp Gly Leu Lys 1835 1840 1845 Phe Lys Ala Asp Gly Asp Lys Val Ile Asn Lys Lys Leu Asn Glu 1850 1855 1860 Thr Val Glu Ile Val Gly Asp Glu Asn Val Thr Thr Ser Ile Thr 1865 1870 1875 Asp Asp Asn Lys Val Lys Val Ser Leu Asn Lys Lys Ile Ala Ile 1880 1885 1890 Asp Glu Val Lys Ile Pro Asn Thr Asp Pro Asp Ala Gln Lys Gly 1895 1900 1905 Asp Ser Ile Val Ile Asn Asn Gly Gly Ile His Ala Gly Asn Lys 1910 1915 1920 Val Ile Thr Gly Val Lys Ala Ser Asp Asp Pro Thr Ser Ala Val 1925 1930 1935 Asn Arg Gly Gln Leu Asn Thr Val Ile Asp Asn Val Gln Asn Asn 1940 1945 1950 Phe Asn Gln Val Asn Gln Arg Ile Gly Asp Leu Thr Arg Glu Ser 1955 1960 1965 Arg Ala Gly Ile Ala Gly Ala Met Ala Thr Ala Ser Leu Gln Asn 1970 1975 1980 Val Ala Leu Pro Gly Lys Thr Thr Ile Ser Val Gly Thr Ala Thr 1985 1990 1995 Phe Lys Gly Glu Asn Ala Val Ala Ile Gly Met Ser Arg Leu Ser 2000 2005 2010 Asp Asn Gly Lys Val Gly Ile Arg Leu Ser Gly Met Ser Thr Ser 2015 2020 2025 Asn Gly Asp Lys Gly Ala Ala Met Ser Val Gly Phe Ser Phe 2030 2035 2040 262039PRTAvibacterium paragallinarumtype C 26Met Asn Lys Val Phe Lys Ile Lys Tyr Ser Val Val Lys Gln Glu Met 1 5 10 15 Ile Val Val Ser Glu Leu Ala Asn Asn Lys Asp Lys Thr Ala Ser Gln 20 25 30 Lys Asn Thr His Asn Thr Ala Phe Phe Gln Pro Leu Phe Thr Lys Cys 35 40 45 Thr Tyr Leu Ala Leu Leu Ile Asn Ile Ala Leu Gly Thr Ser Leu Phe 50 55 60 Pro Gln Leu Ala Asn Ala Lys Phe Leu Glu Val Tyr Asn Ser Ser Val 65 70 75 80 Lys Leu Gln His Val Asn Ser Gly Val Pro Ser Asp Ser Val Asn Leu 85 90 95 Asn Pro Ser Gly Gly Glu Asn Val Gly Met Asn Ser Asn Gln Gly Val 100 105 110 Ala Ile Gly Arg Gly Ala Val Asn Asn Tyr Ser Ala Thr Gly Ser Ile 115 120 125 Ala Ile Gly Gln Gly Ala Lys Asn Asp Asn Trp Ala Thr Arg Ser Ile 130 135 140 Ala Ile Gly Gln Gly Ala Lys Asn Glu Ser Ile Ala Ser Asp Ser Val 145 150 155 160 Ala Ile Ser Asn Ala Ile Asn Arg Phe Lys Lys Ser Ile Val Ile Gly 165 170 175 Leu Asn Thr Tyr Thr Gln Leu Asp Pro Arg Arg Ala Pro Glu Ser Arg 180 185 190 Gln Gly Ser Val Val Ile Gly Glu Asn Ala Lys Ser Ala Gly Asn Gln 195 200 205 Ser Val Ser Leu Gly Gln Asn Ala Trp Ser Lys Thr Asn Ser Ile Ser 210 215 220 Ile Gly Ala Gly Thr Phe Ala Glu Gly Lys Ser Thr Ile Ala Ile Gly 225 230 235 240 Thr Asp Lys Ile Leu Gly Thr Asn Tyr Asn Asp Lys Leu Pro Ala Pro 245 250 255 Ser Trp Asp Gly Arg Thr Gly Lys Ala Pro Thr Asn Ser Ile Trp Asp 260 265 270 Ile Phe Ser Glu Leu Tyr Met Gly Lys Lys Thr Asn Gly Thr Asp Tyr 275 280 285 Asp Ala Lys Lys Asn Asp Arg Asp Pro Asn Lys Pro Glu Ala Phe Tyr 290 295 300 Thr Tyr Ser Asp Phe Lys Ser Arg Tyr Val Asn Asn Pro Ser Thr Ser 305 310 315 320 Pro Thr Tyr Ala Ala Lys Leu Gly Ala Ile Ala Leu Gly Ser Arg Thr 325 330 335 Ile Ala Ala Gly Glu Met Ser Thr Ala Val Gly Ser Leu Ala Phe Ala 340 345 350 Leu Ala Asp Lys Ser Thr Ala Met Gly Leu Arg Ser Phe Val Ala Lys 355 360 365 Asp Ala Val Gly Gly Thr Ala Ile Gly Glu Glu Ser Arg Thr Phe Ala 370 375 380 Lys Asp Ser Val Ala Ile Gly Asn Lys Thr Glu Ala Ser Asn Ala Gly 385 390 395 400 Ser Met Ala Tyr Gly Tyr Lys Ala Lys Ala Val Gly Ala Gly Ala Ile 405 410 415 Ala Ile Gly Ala Glu Val Ala Ala Gly Ala Glu Phe Asp Ser Ser Gln 420 425 430 Ala Gly Asn Leu Leu Leu Asn Arg Gly Ala Tyr Ala Thr Leu Lys Ser 435 440 445 Ala Asp Lys Ser Asp Asp Ile Lys Ala Gly Asp Ala Ile Asn Val Phe 450 455 460 Thr Gln Phe Phe Asp Asn Met Leu Thr Gln Gly Ser His Leu Thr Tyr 465 470 475 480 Glu Asn Thr Thr Tyr Leu Thr Thr Ser Ala Gly Asp Ile Lys Lys Thr 485 490 495 Leu Ala Ala Val Gly Asp Gly Gly Lys Asn Ala Ile Ala Ile Gly Asn 500 505 510 Lys Thr Phe Ala Ser Lys Ala Asn Ser Val Ala Leu Gly Ser Tyr Ala 515 520 525 Leu Ala Ser Ala Gln Asn Ala Phe Ala Leu Gly Ser Tyr Ser Leu Val 530 535 540 Ser Pro Leu Ala Ala Asn Thr Ile Val Ile Gly Val Gly Gly Tyr Ala 545 550 555 560 Thr Gly Ser Asn Ser Phe Val Gly Gly Ser Trp Val Ser Thr Leu Ser 565 570 575 Ala Arg Thr Val Val Leu Gly Tyr Ser Ala Ser Ile Ser Ser Asp Ser 580 585 590 His Asp Ser Leu Ala Met Gly Val Asn Ala Phe Ile Gly Asn Gly Ser 595 600 605 Asn Ser Ser Leu Ala Leu Gly Thr Gly Ser Thr Ile Ala Lys Asn Ala 610 615 620 Lys Ser Pro Asp Ser Leu Ala Ile Gly Lys Asp Ser Arg Ile Asp Ala 625 630 635 640 Lys Asp Thr Asp Asn Gly Val Leu Tyr Thr Pro Gln Val Tyr Asp Glu 645 650 655 Thr Thr Arg Ala Phe Arg Thr Phe Asp Glu Asn Lys Asp Tyr Met Arg 660 665 670 Gln Ala Met Ala Leu Gly Phe Asn Ala Lys Val Ser Arg Gly Lys Gly 675 680 685 Lys Met Glu Thr Gly Ile Asn Ser Met Ala Ile Gly Ala Arg Ser Gln 690 695 700 Ala Thr Leu Gln Asn Ser Thr Ala Leu Gly Val Asn Ala Lys Thr Asp 705 710 715 720 Tyr Thr Trp Glu Gln Leu Glu Ala Asp Pro Trp Val Ser Lys Gly Ala 725 730 735 Ile Ser Ile Pro Thr Ser Gly Lys Ile Gly Val Ile Ser Val Gly Ser 740 745 750 Lys Gly Ser Glu Arg Arg Ile Val Asn Val Ala Ser Gly Ser Leu Asp 755 760 765 Thr Asp Ala Val Asn Val Ala Gln Leu Lys Thr Ile Glu Glu Arg Phe 770 775 780 Gln Ser Glu Ile Asp Leu Leu Gln Asn Gly Gly Gly Val Gln Tyr Leu 785 790 795 800 Ser Val Glu Lys Thr Asn Ile Asn Gly Glu Ala Gly Arg Val Ala Ser 805 810 815 Gln Ile Arg Lys Gly Glu Ser Tyr Lys Arg Tyr Val Lys Leu Lys Thr 820 825 830 Gln Leu Leu Tyr Leu Asp Ala Arg Lys Lys Leu Asn Gly Glu Lys Phe 835 840 845 Asp Gln Thr Ser Leu Asp Lys Ile Ser Lys Ala Val Gln Glu Leu Glu 850 855 860 Ala Glu Tyr Ser Gly Glu Leu Lys Thr Thr Ala Ser Glu Leu Asn Arg 865 870 875 880 Val Ala Met Gln Leu Asn Ala Glu Thr Thr Val Asn Asp Phe Gly Lys 885 890 895 Phe Asn Gln Tyr Lys Thr Gln Ile Glu Asn Ala Thr Asn Ala Asp Ser 900 905 910 Glu Lys Asn Val Gly Gly Leu Ser Pro Gln Val Ile Ala Gln Leu Lys 915 920 925 Ala Asn Asn Asn Tyr Leu Asn Asp Gly Ala Lys Gly Gln Asp Ser Ile 930 935 940 Ala Phe Gly Trp Gln Ala Lys Thr Ser Glu Ala Asn Asn Gly Leu Ala 945 950 955 960 Gly Lys Gln Ala Ile Ala Ile Gly Phe Gln Ala Asn Ser Ser Ala Glu 965 970 975 Asn Ala Ile Ser Ile Gly Thr Asn Ser Asp Thr Ser Met Thr Gly Ala 980 985 990 Val Ala Ile Gly Lys Gly Ala Thr Val Thr Ala Gly Gly Lys Pro Ser 995 1000 1005 Ile Ala Leu Gly Gln Asp Ser Thr Val Ala Asn Ser Ala Ile Ser 1010 1015 1020 Arg Thr Ser Ser Val Met Ile Asn Gly Leu Thr Phe Asn Asn Phe 1025 1030 1035 Ala Gly Ser Pro Glu Thr Leu Gly Val Leu Ser Ile Gly Thr Ala 1040 1045 1050 Gly Lys Glu Arg Lys Ile Val Asn Val Ala Ala Gly Asp Ile Ser 1055 1060 1065 Gln Thr Ser Thr Glu Ala Ile Asn Gly Ser Gln Leu Tyr Ala Thr 1070 1075 1080 Asn Phe Met Leu Asn Lys Leu Ala Gln Ser Val Lys Thr Asn Phe 1085 1090 1095 Gly Gly Asn Ala Asn Leu Ala Thr Asp Gly Thr Ile Thr Phe Thr 1100 1105 1110 Asn Ile Gly Gly Thr Gly Gln Asp Thr Ile His Asp Ala Ile Asn 1115 1120 1125 Asn Val Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu 1130 1135 1140 Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala 1145 1150 1155 Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu 1160 1165 1170 Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro 1175 1180 1185 Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu Met 1190 1195 1200 Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly 1205 1210 1215 Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu 1220 1225 1230 Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 1235 1240 1245 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln 1250 1255 1260 Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn 1265 1270 1275 Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly 1280 1285 1290 Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala 1295 1300 1305 Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala 1310 1315 1320 Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile 1325 1330 1335 Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys 1340 1345 1350 Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp 1355 1360 1365 Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu 1370 1375 1380 Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala 1385 1390 1395 Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp 1400 1405 1410 Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu 1415 1420 1425 Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly 1430 1435 1440 Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile 1445 1450 1455 Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile 1460 1465 1470 Val Leu

Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu 1475 1480 1485 Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly 1490 1495 1500 Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln 1505 1510 1515 Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr 1520 1525 1530 Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn 1535 1540 1545 Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp 1550 1555 1560 Lys Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly 1565 1570 1575 Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys 1580 1585 1590 Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 1595 1600 1605 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile 1610 1615 1620 Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr 1625 1630 1635 Ala Pro Thr Ala Ser Ser Thr Gln Gly Gly Ala Thr Thr Ala Asn 1640 1645 1650 Thr Ala Gly Gly Val Ala Pro Ala Gly Asn Val Ala Thr Gly Asp 1655 1660 1665 Ile Ala Pro Thr Gln Pro Ala Leu Pro Glu Met Lys Thr Ala Leu 1670 1675 1680 Val Gly Asp His Leu Ala Val Pro Leu Gly Gly Ser Leu Lys Ile 1685 1690 1695 His Gly Asp His Asn Val Lys Thr Thr Ile Ser Ala Gly Asn Gln 1700 1705 1710 Val Gly Ile Ser Leu Gln Pro Asn Ile Ser Ile Glu Asn Asn Leu 1715 1720 1725 Val Ile Gly Ser Asn Lys Pro Glu Lys Ala Lys Leu Ala Ala Gln 1730 1735 1740 Glu Gly Asn Ala Leu Val Ile Thr Asn Lys Asp Asp Gly Asn Ala 1745 1750 1755 Ala Met Val Phe Asn Asn Glu Lys Asn Met Leu Val Leu Ser Asp 1760 1765 1770 Lys Lys Ala Lys Pro Arg Ala Val Leu Asp Gly Gln Asn Gly Ala 1775 1780 1785 Leu Thr Leu Val Gly Asn Asp Asp Ser Gln Val Thr Leu Ser Ser 1790 1795 1800 Lys Lys Gly Lys Asp Ile Asp Gly Asn Asp Leu Ser Arg Leu Ser 1805 1810 1815 Val Thr Thr Glu Arg Thr Asn Ala Asp Gly Gln Leu Glu Lys Val 1820 1825 1830 Glu Thr Ser Phe Ala Thr Met Asp Asp Gly Leu Lys Phe Lys Ala 1835 1840 1845 Asp Gly Asp Lys Val Ile Asn Lys Lys Leu Asn Glu Thr Val Glu 1850 1855 1860 Ile Val Gly Asp Glu Asn Val Thr Thr Ser Ile Thr Asp Asp Asn 1865 1870 1875 Lys Val Lys Val Ser Leu Asn Lys Lys Ile Ala Ile Asp Glu Val 1880 1885 1890 Lys Ile Pro Asn Thr Asp Pro Asp Ala Gln Lys Gly Asp Ser Ile 1895 1900 1905 Val Ile Asn Asn Gly Gly Ile His Ala Gly Asn Lys Val Ile Thr 1910 1915 1920 Gly Val Lys Ala Ser Asp Asp Pro Thr Ser Ala Val Asn Arg Gly 1925 1930 1935 Gln Leu Asn Thr Val Ile Asp Asn Val Gln Asn Asn Phe Asn Gln 1940 1945 1950 Val Asn Gln Arg Ile Gly Asp Leu Thr Arg Glu Ser Arg Ala Gly 1955 1960 1965 Ile Ala Gly Ala Met Ala Thr Ala Ser Leu Gln Asn Val Ala Leu 1970 1975 1980 Pro Gly Lys Thr Thr Ile Ser Val Gly Thr Ala Thr Phe Lys Gly 1985 1990 1995 Glu Asn Ala Val Ala Ile Gly Met Ser Arg Leu Ser Asp Asn Gly 2000 2005 2010 Lys Val Gly Ile Arg Leu Ser Gly Met Ser Thr Ser Asn Gly Asp 2015 2020 2025 Lys Gly Ala Ala Met Ser Val Gly Phe Thr Phe 2030 2035 27484PRTAvibacterium paragallinarumtype A 27Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn 28406PRTAvibacterium paragallinarumtype A 28Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu 405 29267PRTAvibacterium paragallinarumtype A 29Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 260 265 30457PRTAvibacterium paragallinarumtype A 30Met Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln 1 5 10 15 Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn 20 25 30 Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr 35 40 45 Tyr Asn Ser Gln Asn Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro 50 55 60 Ser Val Lys Gln Ile Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala 65 70 75 80 Asn Asn Lys Asn Gln Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu 85 90 95 Ala Thr Gly Ile Thr Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe 100 105 110 Ser Leu Gly Ala Asp Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr 115 120 125 Val Lys Leu Ser Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala 130 135 140 Thr Leu Lys Gln Val Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn 145 150 155 160 Asp Ile Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr 165 170 175 Tyr Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 180 185 190 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr 195 200 205 Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile 210 215 220 Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 225 230 235 240 Asn Ala Ile Thr Gly Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro 245 250 255 Ile Thr Val Glu Pro Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr 260 265 270 Val Gly Val Asp Phe Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp 275 280 285 Asp Lys Lys Leu Thr Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn 290 295 300 Lys Leu Ala Asn Phe Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser 305 310 315 320 Gly Asn Ala Thr Thr Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser 325 330 335 Asp Gly Phe Thr Ile Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln 340 345 350 Tyr Asn Gly Ser Asp Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly 355 360 365 Val Phe Lys Leu Ser Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala 370 375 380 Asn Thr Phe Ala Lys Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn 385 390 395 400 Lys Glu Lys Trp Arg Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val 405 410 415 Asp Ala Glu Ile Gln Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly 420 425 430 Leu Ile Phe Ala Thr Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile 435 440 445 Asp Ala Gly Asn Lys Lys Ile Ser Asn 450 455 31379PRTAvibacterium paragallinarumtype A 31Met Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln 1 5 10 15 Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn 20 25 30 Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr 35 40 45 Tyr Asn Ser Gln Asn Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro 50 55 60 Ser Val Lys Gln Ile Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala 65

70 75 80 Asn Asn Lys Asn Gln Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu 85 90 95 Ala Thr Gly Ile Thr Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe 100 105 110 Ser Leu Gly Ala Asp Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr 115 120 125 Val Lys Leu Ser Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala 130 135 140 Thr Leu Lys Gln Val Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn 145 150 155 160 Asp Ile Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr 165 170 175 Tyr Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 180 185 190 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr 195 200 205 Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile 210 215 220 Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 225 230 235 240 Asn Ala Ile Thr Gly Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro 245 250 255 Ile Thr Val Glu Pro Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr 260 265 270 Val Gly Val Asp Phe Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp 275 280 285 Asp Lys Lys Leu Thr Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn 290 295 300 Lys Leu Ala Asn Phe Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser 305 310 315 320 Gly Asn Ala Thr Thr Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser 325 330 335 Asp Gly Phe Thr Ile Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln 340 345 350 Tyr Asn Gly Ser Asp Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly 355 360 365 Val Phe Lys Leu Ser Leu Asn Met Thr Ala Leu 370 375 32240PRTAvibacterium paragallinarumtype A 32Met Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln 1 5 10 15 Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn 20 25 30 Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr 35 40 45 Tyr Asn Ser Gln Asn Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro 50 55 60 Ser Val Lys Gln Ile Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala 65 70 75 80 Asn Asn Lys Asn Gln Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu 85 90 95 Ala Thr Gly Ile Thr Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe 100 105 110 Ser Leu Gly Ala Asp Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr 115 120 125 Val Lys Leu Ser Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala 130 135 140 Thr Leu Lys Gln Val Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn 145 150 155 160 Asp Ile Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr 165 170 175 Tyr Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 180 185 190 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr 195 200 205 Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile 210 215 220 Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 225 230 235 240 33387PRTAvibacterium paragallinarumtype A 33Met Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu 1 5 10 15 Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 20 25 30 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp Ser 35 40 45 Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly Val 50 55 60 Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val Lys 65 70 75 80 Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala Asp 85 90 95 Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu Asn 100 105 110 Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys Thr 115 120 125 Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr Ile 130 135 140 Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp Gln 145 150 155 160 Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly Leu 165 170 175 Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro Ser 180 185 190 Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe Thr 195 200 205 Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr Thr 210 215 220 Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe Ser 225 230 235 240 Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr Ala 245 250 255 Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile Lys 260 265 270 Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp Ser 275 280 285 Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser Leu 290 295 300 Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys Leu 305 310 315 320 Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg Thr 325 330 335 Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln Lys 340 345 350 Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr Lys 355 360 365 Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys Lys 370 375 380 Ile Ser Asn 385 34309PRTAvibacterium paragallinarumtype A 34Met Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu 1 5 10 15 Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 20 25 30 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp Ser 35 40 45 Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly Val 50 55 60 Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val Lys 65 70 75 80 Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala Asp 85 90 95 Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu Asn 100 105 110 Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys Thr 115 120 125 Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr Ile 130 135 140 Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp Gln 145 150 155 160 Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly Leu 165 170 175 Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro Ser 180 185 190 Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe Thr 195 200 205 Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr Thr 210 215 220 Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe Ser 225 230 235 240 Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr Ala 245 250 255 Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile Lys 260 265 270 Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp Ser 275 280 285 Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser Leu 290 295 300 Asn Met Thr Ala Leu 305 35170PRTAvibacterium paragallinarumtype A 35Met Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu 1 5 10 15 Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 20 25 30 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp Ser 35 40 45 Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly Val 50 55 60 Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val Lys 65 70 75 80 Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala Asp 85 90 95 Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu Asn 100 105 110 Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys Thr 115 120 125 Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr Ile 130 135 140 Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp Gln 145 150 155 160 Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 165 170 3625DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 36catgccatgg ggatctacct taaag 253733DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 37catgccatgg gaacctataa tacaacgggt gat 333833DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 38cgcggatcca ttactaattt tcttattccc agc 333930DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 39cgcggatcca agtgcggtca tatttaggct 304030DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 40cgcggatcct ttgccacttt cactgaggtt 30411027PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 41Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly 485 490 495 Gly Thr Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr 500 505 510 Lys Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly 515 520 525 Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala 530 535 540 Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala 545 550 555 560 Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys 565 570 575 Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile 580 585 590 Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met 595 600 605 Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser 610 615 620 Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn 625 630 635 640 Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val 645 650 655 Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile 660 665 670 Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala 675 680 685 Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln 690 695 700 Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu 705 710 715 720 Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val 725 730 735 Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys 740 745 750 Ile Gly Gly Thr Glu Lys Thr Thr Ile

Ser Glu Ala Ile Ser Asp Val 755 760 765 Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys 770 775 780 Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr 785 790 795 800 Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr 805 810 815 Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu 820 825 830 Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly 835 840 845 Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg 850 855 860 Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys 865 870 875 880 Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys 885 890 895 Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr 900 905 910 Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn 915 920 925 Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys 930 935 940 Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu 945 950 955 960 Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn 965 970 975 Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly 980 985 990 Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp 995 1000 1005 Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser 1010 1015 1020 Ser Thr Gln Gly 1025 42949PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 42Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn 405 410 415 Ile Gly Gly Thr Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val 420 425 430 Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val 435 440 445 Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val 450 455 460 Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys 465 470 475 480 Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys 485 490 495 Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn 500 505 510 Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly 515 520 525 Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn 530 535 540 Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr 545 550 555 560 Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe 565 570 575 Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu 580 585 590 Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly 595 600 605 Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu 610 615 620 Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile 625 630 635 640 Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp 645 650 655 Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly 660 665 670 Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser 675 680 685 Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp 690 695 700 Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr 705 710 715 720 Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys 725 730 735 Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu 740 745 750 Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val 755 760 765 Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn 770 775 780 Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly 785 790 795 800 Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val 805 810 815 Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu 820 825 830 Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile 835 840 845 Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val 850 855 860 Asp Lys Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly 865 870 875 880 Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile 885 890 895 Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val 900 905 910 Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr 915 920 925 Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala 930 935 940 Ser Ser Thr Gln Gly 945 43810PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 43Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Gly Ser Asp Gly Thr 260 265 270 Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr Ile His Asp 275 280 285 Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu 290 295 300 Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly 305 310 315 320 Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu 325 330 335 Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser 340 345 350 Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp 355 360 365 Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu 370 375 380 Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys 385 390 395 400 Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu 405 410 415 Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val 420 425 430 Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu 435 440 445 Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu 450 455 460 Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys 465 470 475 480 Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala 485 490 495 Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr 500 505 510 Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu 515 520 525 Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile 530 535 540 Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu 545 550 555 560 Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp 565 570 575 Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp 580 585 590 Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys 595 600 605 Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly 610 615 620 Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys 625 630 635 640 Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn 645 650 655 Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala 660 665 670 Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala 675 680 685 Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro 690 695 700 Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr 705 710 715 720 Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val Asn Thr Gly Trp 725 730 735 Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala 740 745 750 Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr 755 760 765 Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys 770 775 780 Gly Ile Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr 785 790 795 800 Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly 805 810 441000PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 44Met Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln 1 5 10 15 Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn 20 25 30 Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr 35 40 45 Tyr Asn Ser Gln Asn Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro 50 55 60 Ser Val Lys Gln Ile Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala 65 70 75 80 Asn Asn Lys Asn Gln Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu 85 90 95 Ala Thr Gly Ile Thr Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe 100 105 110 Ser Leu Gly Ala Asp Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr 115 120 125 Val Lys Leu Ser Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala 130 135 140 Thr Leu Lys Gln Val Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn 145 150 155 160 Asp Ile Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr 165 170 175 Tyr Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 180 185 190 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr 195 200 205 Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile 210 215 220 Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 225 230 235

240 Asn Ala Ile Thr Gly Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro 245 250 255 Ile Thr Val Glu Pro Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr 260 265 270 Val Gly Val Asp Phe Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp 275 280 285 Asp Lys Lys Leu Thr Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn 290 295 300 Lys Leu Ala Asn Phe Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser 305 310 315 320 Gly Asn Ala Thr Thr Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser 325 330 335 Asp Gly Phe Thr Ile Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln 340 345 350 Tyr Asn Gly Ser Asp Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly 355 360 365 Val Phe Lys Leu Ser Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala 370 375 380 Asn Thr Phe Ala Lys Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn 385 390 395 400 Lys Glu Lys Trp Arg Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val 405 410 415 Asp Ala Glu Ile Gln Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly 420 425 430 Leu Ile Phe Ala Thr Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile 435 440 445 Asp Ala Gly Asn Lys Lys Ile Ser Asn Gly Ser Asp Gly Thr Ile Thr 450 455 460 Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr Ile His Asp Ala Ile 465 470 475 480 Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu 485 490 495 Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys 500 505 510 Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp 515 520 525 Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp 530 535 540 Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu 545 550 555 560 Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln 565 570 575 Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp 580 585 590 Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile 595 600 605 Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg 610 615 620 Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser 625 630 635 640 Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu Val Thr 645 650 655 Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser 660 665 670 Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly 675 680 685 Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn 690 695 700 Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val 705 710 715 720 Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu 725 730 735 Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr 740 745 750 Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu 755 760 765 Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly 770 775 780 Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile 785 790 795 800 Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr 805 810 815 Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly 820 825 830 Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala 835 840 845 Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr 850 855 860 Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn 865 870 875 880 Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln 885 890 895 Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys 900 905 910 Asp Ala Val Asp Lys Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser 915 920 925 Lys Val Gly Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn 930 935 940 Lys Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly 945 950 955 960 Asp Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile 965 970 975 Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala 980 985 990 Pro Thr Ala Ser Ser Thr Gln Gly 995 1000 45922PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 45Met Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln 1 5 10 15 Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn 20 25 30 Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr 35 40 45 Tyr Asn Ser Gln Asn Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro 50 55 60 Ser Val Lys Gln Ile Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala 65 70 75 80 Asn Asn Lys Asn Gln Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu 85 90 95 Ala Thr Gly Ile Thr Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe 100 105 110 Ser Leu Gly Ala Asp Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr 115 120 125 Val Lys Leu Ser Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala 130 135 140 Thr Leu Lys Gln Val Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn 145 150 155 160 Asp Ile Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr 165 170 175 Tyr Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 180 185 190 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr 195 200 205 Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile 210 215 220 Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 225 230 235 240 Asn Ala Ile Thr Gly Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro 245 250 255 Ile Thr Val Glu Pro Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr 260 265 270 Val Gly Val Asp Phe Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp 275 280 285 Asp Lys Lys Leu Thr Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn 290 295 300 Lys Leu Ala Asn Phe Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser 305 310 315 320 Gly Asn Ala Thr Thr Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser 325 330 335 Asp Gly Phe Thr Ile Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln 340 345 350 Tyr Asn Gly Ser Asp Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly 355 360 365 Val Phe Lys Leu Ser Leu Asn Met Thr Ala Leu Gly Ser Asp Gly Thr 370 375 380 Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr Ile His Asp 385 390 395 400 Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu 405 410 415 Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly 420 425 430 Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu 435 440 445 Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser 450 455 460 Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp 465 470 475 480 Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu 485 490 495 Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys 500 505 510 Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu 515 520 525 Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val 530 535 540 Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu 545 550 555 560 Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu 565 570 575 Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys 580 585 590 Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala 595 600 605 Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr 610 615 620 Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu 625 630 635 640 Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile 645 650 655 Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu 660 665 670 Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp 675 680 685 Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp 690 695 700 Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys 705 710 715 720 Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly 725 730 735 Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys 740 745 750 Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn 755 760 765 Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala 770 775 780 Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala 785 790 795 800 Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro 805 810 815 Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr 820 825 830 Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val Asn Thr Gly Trp 835 840 845 Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala 850 855 860 Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr 865 870 875 880 Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys 885 890 895 Gly Ile Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr 900 905 910 Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly 915 920 46783PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 46Met Gly Ile Tyr Leu Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln 1 5 10 15 Gly Gln Lys Val Glu Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn 20 25 30 Gln Trp Ala Asn Asn Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr 35 40 45 Tyr Asn Ser Gln Asn Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro 50 55 60 Ser Val Lys Gln Ile Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala 65 70 75 80 Asn Asn Lys Asn Gln Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu 85 90 95 Ala Thr Gly Ile Thr Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe 100 105 110 Ser Leu Gly Ala Asp Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr 115 120 125 Val Lys Leu Ser Gly Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala 130 135 140 Thr Leu Lys Gln Val Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn 145 150 155 160 Asp Ile Thr Ala Ala Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr 165 170 175 Tyr Asn Leu Ser Leu Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys 180 185 190 Val Val Ser Gly Lys Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr 195 200 205 Gly Asn Ile Phe Thr Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile 210 215 220 Asn Asn Pro Ala Asp Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys 225 230 235 240 Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln 245 250 255 Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser 260 265 270 Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr 275 280 285 Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys 290 295 300 Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile 305 310 315 320 Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val 325 330 335 Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys 340 345 350 Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly 355 360 365 Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 370 375 380 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr 385 390 395 400 Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser 405 410 415 Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn 420 425 430 Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp 435 440 445 Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr 450 455 460 Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala 465 470 475 480 Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln 485 490 495 Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr 500 505 510 Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu 515 520 525 Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr 530 535 540 Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp 545 550 555 560 Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys 565 570 575 Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln 580 585 590 Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu

Thr Glu Gly 595 600 605 Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu 610 615 620 Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val 625 630 635 640 Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp 645 650 655 Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala 660 665 670 Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly 675 680 685 Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala 690 695 700 Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala Thr Gly Ile 705 710 715 720 Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val Ala Asp Gly 725 730 735 Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg Gln Leu Tyr 740 745 750 Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu Val Ser Pro 755 760 765 Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser Thr Gln Gly 770 775 780 47930PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 47Met Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu 1 5 10 15 Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 20 25 30 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp Ser 35 40 45 Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly Val 50 55 60 Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val Lys 65 70 75 80 Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala Asp 85 90 95 Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu Asn 100 105 110 Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys Thr 115 120 125 Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr Ile 130 135 140 Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp Gln 145 150 155 160 Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly Leu 165 170 175 Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro Ser 180 185 190 Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe Thr 195 200 205 Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr Thr 210 215 220 Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe Ser 225 230 235 240 Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr Ala 245 250 255 Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile Lys 260 265 270 Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp Ser 275 280 285 Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser Leu 290 295 300 Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys Leu 305 310 315 320 Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg Thr 325 330 335 Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln Lys 340 345 350 Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr Lys 355 360 365 Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys Lys 370 375 380 Ile Ser Asn Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly 385 390 395 400 Thr Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys 405 410 415 Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu 420 425 430 Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu 435 440 445 Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn 450 455 460 Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr 465 470 475 480 Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr 485 490 495 Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser 500 505 510 Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr 515 520 525 Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser 530 535 540 Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys 545 550 555 560 Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly 565 570 575 Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu 580 585 590 Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp 595 600 605 Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr 610 615 620 Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn 625 630 635 640 Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile 645 650 655 Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys 660 665 670 Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn 675 680 685 Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr 690 695 700 Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu 705 710 715 720 Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn 725 730 735 Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu 740 745 750 Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr 755 760 765 Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val 770 775 780 Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly 785 790 795 800 Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr 805 810 815 Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro 820 825 830 Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu 835 840 845 Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala 850 855 860 Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val 865 870 875 880 Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg 885 890 895 Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu 900 905 910 Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser Ser Thr 915 920 925 Gln Gly 930 48852PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 48Met Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu 1 5 10 15 Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 20 25 30 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp Ser 35 40 45 Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly Val 50 55 60 Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val Lys 65 70 75 80 Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala Asp 85 90 95 Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu Asn 100 105 110 Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys Thr 115 120 125 Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr Ile 130 135 140 Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp Gln 145 150 155 160 Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly Leu 165 170 175 Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro Ser 180 185 190 Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe Thr 195 200 205 Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr Thr 210 215 220 Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe Ser 225 230 235 240 Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr Ala 245 250 255 Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile Lys 260 265 270 Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp Ser 275 280 285 Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser Leu 290 295 300 Asn Met Thr Ala Leu Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile 305 310 315 320 Gly Gly Thr Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu 325 330 335 Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser 340 345 350 Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser 355 360 365 Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys 370 375 380 Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys 385 390 395 400 Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser 405 410 415 Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg 420 425 430 Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly 435 440 445 Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr 450 455 460 Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser 465 470 475 480 Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser 485 490 495 Ile Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile 500 505 510 Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala 515 520 525 Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys 530 535 540 Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala 545 550 555 560 Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala 565 570 575 Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp 580 585 590 Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn 595 600 605 Lys Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser 610 615 620 Thr Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe 625 630 635 640 Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser 645 650 655 Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly 660 665 670 Gly Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp 675 680 685 Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile 690 695 700 Lys Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn 705 710 715 720 Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly 725 730 735 Thr Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe 740 745 750 Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp 755 760 765 Lys Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile 770 775 780 Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser 785 790 795 800 Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr 805 810 815 Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly 820 825 830 Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro Thr Ala Ser 835 840 845 Ser Thr Gln Gly 850 49713PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 49Met Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln Leu 1 5 10 15 Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr Ser 20 25 30 Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp Ser 35 40 45 Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly Val 50 55 60 Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val Lys 65 70 75 80 Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala Asp 85 90 95 Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu Asn 100 105 110 Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys Thr 115 120 125 Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr Ile 130 135 140 Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp Gln 145 150 155 160 Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Gly Ser Asp Gly Thr Ile 165 170 175 Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr Ile His Asp Ala 180 185 190 Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser Ala Thr Glu Glu 195 200 205 Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala 210 215 220 Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val 225 230 235 240 Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr 245 250 255 Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile 260 265 270 Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn 275 280 285 Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly 290 295

300 Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr 305 310 315 320 Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser 325 330 335 Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala 340 345 350 Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu Val 355 360 365 Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser 370 375 380 Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr 385 390 395 400 Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val 405 410 415 Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly 420 425 430 Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser 435 440 445 Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala 450 455 460 Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp Gly 465 470 475 480 Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp Asn 485 490 495 Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr 500 505 510 Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly 515 520 525 Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys Ser 530 535 540 Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala 545 550 555 560 Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala Asp 565 570 575 Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile 580 585 590 Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro Asn 595 600 605 Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe 610 615 620 Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val Asn Thr Gly Trp Gly 625 630 635 640 Ser Lys Val Gly Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly 645 650 655 Asn Lys Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser 660 665 670 Gly Asp Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly 675 680 685 Ile Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr 690 695 700 Ala Pro Thr Ala Ser Ser Thr Gln Gly 705 710 50469PRTAvibacterium paragallinarumtype C 50Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr 1 5 10 15 Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser 20 25 30 Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala 35 40 45 Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile 50 55 60 Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val 65 70 75 80 Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu 85 90 95 Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly 100 105 110 Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr 115 120 125 Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu 130 135 140 Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu 145 150 155 160 Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu 165 170 175 Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu 180 185 190 His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr 195 200 205 Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala 210 215 220 Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly 225 230 235 240 Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg 245 250 255 Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr Glu Lys 260 265 270 Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu Thr Asp 275 280 285 Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr Val Lys 290 295 300 Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp Ala Ser 305 310 315 320 Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys Leu Thr 325 330 335 Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln Asn Ile 340 345 350 Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly Ile Val 355 360 365 Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu Ser Gly 370 375 380 Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val Lys Ala 385 390 395 400 Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp Lys Leu 405 410 415 Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala Val Thr 420 425 430 Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly Thr Ala 435 440 445 Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala Val Asn 450 455 460 Thr Gly Trp Gly Ser 465 51268PRTAvibacterium paragallinarumtype C 51Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Asp Thr 1 5 10 15 Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu Ile Ser Leu Ser 20 25 30 Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala Val Tyr Asp Ala 35 40 45 Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala Asn Lys Gly Ile 50 55 60 Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser Pro Ile Thr Val 65 70 75 80 Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe Thr Val Gly Leu 85 90 95 Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys Ser Gly 100 105 110 Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly Leu Thr 115 120 125 Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe Ala Glu 130 135 140 Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr Asn Leu 145 150 155 160 Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser Asp Glu 165 170 175 Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn Ala Glu 180 185 190 His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp Asn Thr 195 200 205 Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr Leu Ala 210 215 220 Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala Asp Gly 225 230 235 240 Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln Leu Arg 245 250 255 Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 260 265 52504PRTAvibacterium paragallinarumtype C 52Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu 1 5 10 15 Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu 20 25 30 Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn 35 40 45 Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr 50 55 60 Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr 65 70 75 80 Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser 85 90 95 Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr 100 105 110 Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser 115 120 125 Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys 130 135 140 Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly 145 150 155 160 Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu 165 170 175 Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp 180 185 190 Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr 195 200 205 Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn 210 215 220 Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile 225 230 235 240 Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys 245 250 255 Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn 260 265 270 Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr 275 280 285 Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu 290 295 300 Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn 305 310 315 320 Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu 325 330 335 Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr 340 345 350 Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val 355 360 365 Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly 370 375 380 Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr 385 390 395 400 Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro 405 410 415 Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu 420 425 430 Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val Gly Ile Leu Ala 435 440 445 Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys Ile Ser Asn Val 450 455 460 Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp Val Val Thr Gly Arg 465 470 475 480 Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg Val Tyr Gly Asp Glu 485 490 495 Val Ser Pro Thr Lys Thr Gln Thr 500 53442PRTAvibacterium paragallinarumtype C 53Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu 1 5 10 15 Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu 20 25 30 Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn 35 40 45 Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr 50 55 60 Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr 65 70 75 80 Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser 85 90 95 Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr 100 105 110 Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser 115 120 125 Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys 130 135 140 Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly 145 150 155 160 Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu 165 170 175 Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp 180 185 190 Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr 195 200 205 Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn 210 215 220 Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile 225 230 235 240 Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys 245 250 255 Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn 260 265 270 Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr 275 280 285 Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu 290 295 300 Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn 305 310 315 320 Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu 325 330 335 Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr 340 345 350 Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val 355 360 365 Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly 370 375 380 Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr 385 390 395 400 Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro 405 410 415 Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu 420 425 430 Thr Thr Ala Val Asn Thr Gly Trp Gly Ser 435 440 54241PRTAvibacterium paragallinarumtype C 54Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu 1 5 10 15 Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu 20 25 30 Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn 35 40 45 Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr 50 55 60 Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr 65 70 75 80 Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser 85 90 95 Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr 100 105 110 Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser 115 120 125 Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys 130 135 140 Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly 145 150 155 160 Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu 165 170 175 Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser

Ile Thr Leu Ala Gln Asp 180 185 190 Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr 195 200 205 Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn 210 215 220 Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile 225 230 235 240 Gly 55375PRTAvibacterium paragallinarumtype C 55Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys 1 5 10 15 Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly 20 25 30 Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 35 40 45 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr 50 55 60 Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser 65 70 75 80 Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn 85 90 95 Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp 100 105 110 Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr 115 120 125 Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala 130 135 140 Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln 145 150 155 160 Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly Gly Thr 165 170 175 Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln Ala Leu 180 185 190 Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly Lys Thr 195 200 205 Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn Ile Asp 210 215 220 Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys Asp Lys 225 230 235 240 Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala Ser Gln 245 250 255 Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr Glu Gly 260 265 270 Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu Ser Leu 275 280 285 Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser Gly Val 290 295 300 Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln Leu Asp 305 310 315 320 Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp Leu Ala 325 330 335 Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile Asn Gly 340 345 350 Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr Thr Ala 355 360 365 Val Asn Thr Gly Trp Gly Ser 370 375 56174PRTAvibacterium paragallinarumtype C 56Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe Asp Lys 1 5 10 15 Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser Ala Gly 20 25 30 Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr Thr Phe 35 40 45 Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala Gln Thr 50 55 60 Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn Gly Ser 65 70 75 80 Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala Glu Asn 85 90 95 Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys Ala Asp 100 105 110 Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala Ile Thr 115 120 125 Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly Val Ala 130 135 140 Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly Gly Gln 145 150 155 160 Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 165 170 5732DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 57cgcggatcct tgatctcgct ttcggcaaca ga 325833DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 58cgcggatccc tatgatcccc aacctgtatt cac 335933DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 59cgcggatccc tagccaattt tagccccgct atc 336033DNAArtificial SequenceDescription of Artificial Sequence Synthetic primer 60cgcggatccc tatgtttgag tcttcgttgg act 33611017PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 61Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr 545 550 555 560 Gly Gln Asp Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Leu 565 570 575 Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala 580 585 590 Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala 595 600 605 Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser 610 615 620 Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe 625 630 635 640 Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe 645 650 655 Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser 660 665 670 Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr 675 680 685 Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala 690 695 700 Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn 705 710 715 720 Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala 725 730 735 Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys 740 745 750 Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala 755 760 765 Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly 770 775 780 Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly 785 790 795 800 Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 805 810 815 Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val Lys Gln 820 825 830 Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys Asn Gly 835 840 845 Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr Thr Asn 850 855 860 Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr Leu Lys 865 870 875 880 Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu Asn Ala 885 890 895 Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly Glu Thr 900 905 910 Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg Thr Leu 915 920 925 Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys Val Ser 930 935 940 Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys Gly Gln 945 950 955 960 Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr Thr Asp 965 970 975 Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn Pro Ile 980 985 990 Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys Leu Thr 995 1000 1005 Thr Ala Val Asn Thr Gly Trp Gly Ser 1010 1015 62816PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 62Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr 545 550 555 560 Gly Gln Asp Thr Ile His Asp Ala Ile

Asn Asn Val Leu Thr Lys Leu 565 570 575 Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val Val Ser Gly Glu Ala 580 585 590 Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr Val Ser Ala Glu Ala 595 600 605 Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val Lys Lys Ala Asn Ser 610 615 620 Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn Lys Lys Lys Thr Phe 625 630 635 640 Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile Thr Phe 645 650 655 Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met Ser Ser 660 665 670 Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser Thr Thr 675 680 685 Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn Ser Ala 690 695 700 Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val Lys Asn 705 710 715 720 Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile Gly Ala 725 730 735 Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala Leu Lys 740 745 750 Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln Asp Ala 755 760 765 Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu Thr Gly 770 775 780 Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val Asn Gly 785 790 795 800 Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys Ile Gly 805 810 815 631052PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 63Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val 545 550 555 560 Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr 565 570 575 Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val 580 585 590 Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn 595 600 605 Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val 610 615 620 Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr 625 630 635 640 Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr 645 650 655 Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser 660 665 670 Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly 675 680 685 Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys 690 695 700 Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser 705 710 715 720 Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr 725 730 735 Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala 740 745 750 Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys 755 760 765 Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser 770 775 780 Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile 785 790 795 800 Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala 805 810 815 Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe 820 825 830 Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val 835 840 845 Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr 850 855 860 Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr 865 870 875 880 Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly 885 890 895 Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp 900 905 910 Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala 915 920 925 Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala 930 935 940 Leu Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser 945 950 955 960 Ile Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala 965 970 975 Val Asp Lys Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser Lys Val 980 985 990 Gly Ile Leu Ala Thr Gly Ile Asp Gly Ile Asp Ala Gly Asn Lys Lys 995 1000 1005 Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 1010 1015 1020 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile 1025 1030 1035 Arg Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr 1040 1045 1050 64990PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 64Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val 545 550 555 560 Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr 565 570 575 Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val 580 585 590 Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn 595 600 605 Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val 610 615 620 Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr 625 630 635 640 Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr 645 650 655 Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser 660 665 670 Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly 675 680 685 Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys 690 695 700 Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser 705 710 715 720 Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr 725 730 735 Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala 740 745 750 Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys 755 760 765 Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser 770 775 780 Gly Ala Lys Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile 785 790 795 800 Ser Asp Val Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala 805 810 815 Asp Asn Lys Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe 820 825 830 Thr Ser Thr Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val 835 840 845 Lys Phe Thr Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr 850 855 860 Glu Ser Leu Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr 865 870 875 880 Val Gly Gly Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly 885 890 895 Asn Asp Arg Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp 900 905 910 Gly Ile Lys Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala 915 920 925 Val Asn Lys Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala 930 935 940 Leu Gly Thr Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser 945 950 955 960 Ile Phe Asn Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala 965 970 975 Val Asp Lys

Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser 980 985 990 65789PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 65Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Leu Ile Ser Leu Ser Ala Thr Glu Glu Glu Glu Val 545 550 555 560 Val Ser Gly Glu Ala Val Tyr Asp Ala Leu Lys Gly Ala Lys Pro Thr 565 570 575 Val Ser Ala Glu Ala Asn Lys Gly Ile Thr Gly Leu Val Asp Val Val 580 585 590 Lys Lys Ala Asn Ser Pro Ile Thr Val Glu Pro Ser Thr Asp Asn Asn 595 600 605 Lys Lys Lys Thr Phe Thr Val Gly Leu Met Lys Asp Ile Glu Gly Val 610 615 620 Asn Ser Ile Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr 625 630 635 640 Gly Arg Met Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr 645 650 655 Asn Gly Ser Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser 660 665 670 Thr Thr Asn Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly 675 680 685 Phe Ser Val Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys 690 695 700 Leu Ser Ile Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser 705 710 715 720 Gly Ile Ala Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr 725 730 735 Leu Ala Gln Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala 740 745 750 Ile Lys Leu Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys 755 760 765 Asp Ala Val Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser 770 775 780 Gly Ala Lys Ile Gly 785 66923PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 66Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile 545 550 555 560 Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met 565 570 575 Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser 580 585 590 Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn 595 600 605 Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val 610 615 620 Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile 625 630 635 640 Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala 645 650 655 Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln 660 665 670 Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu 675 680 685 Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val 690 695 700 Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys 705 710 715 720 Ile Gly Gly Thr Glu Lys Thr Thr Ile Ser Glu Ala Ile Ser Asp Val 725 730 735 Lys Gln Ala Leu Thr Asp Ala Thr Leu Ala Tyr Lys Ala Asp Asn Lys 740 745 750 Asn Gly Lys Thr Val Lys Leu Thr Asp Gly Leu Asn Phe Thr Ser Thr 755 760 765 Thr Asn Ile Asp Ala Ser Val Glu Asp Asn Gly Val Val Lys Phe Thr 770 775 780 Leu Lys Asp Lys Leu Thr Gly Leu Lys Thr Ile Ala Thr Glu Ser Leu 785 790 795 800 Asn Ala Ser Gln Asn Ile Ile Ala Gly Gly Thr Val Thr Val Gly Gly 805 810 815 Glu Thr Glu Gly Ile Val Leu Thr Lys Ser Gly Ser Gly Asn Asp Arg 820 825 830 Thr Leu Ser Leu Ser Gly Ala Gly Asn Ala Ala Thr Asp Gly Ile Lys 835 840 845 Val Ser Gly Val Lys Ala Gly Thr Ala Asp Thr Asp Ala Val Asn Lys 850 855 860 Gly Gln Leu Asp Lys Leu Phe Lys Ala Ile Asn Asp Ala Leu Gly Thr 865 870 875 880 Thr Asp Leu Ala Val Thr Lys Asn Pro Asn Gln Thr Ser Ile Phe Asn 885 890 895 Pro Ile Asn Gly Thr Ala Pro Thr Thr Phe Lys Asp Ala Val Asp Lys 900 905 910 Leu Thr Thr Ala Val Asn Thr Gly Trp Gly Ser 915 920 67722PRTArtificial SequenceDescription of Artificial Sequence Synthetic polypeptide 67Met Asp Gly Thr Ile Thr Phe Thr Asn Ile Gly Gly Thr Gly Gln Ala 1 5 10 15 Thr Ile His Asp Ala Ile Asn Asn Val Leu Thr Lys Gly Ile Tyr Leu 20 25 30 Lys Ala Asp Gln Asn Asp Pro Thr Gly Asn Gln Gly Gln Lys Val Glu 35 40 45 Leu Gly Asn Ala Ile Thr Leu Ser Ala Thr Asn Gln Trp Ala Asn Asn 50 55 60 Gly Val Asn Tyr Lys Thr Asn Asn Leu Thr Thr Tyr Asn Ser Gln Asn 65 70 75 80 Gly Thr Ile Leu Phe Gly Met Arg Glu Asp Pro Ser Val Lys Gln Ile 85 90 95 Thr Ala Gly Thr Tyr Asn Thr Thr Gly Asp Ala Asn Asn Lys Asn Gln 100 105 110 Leu Asn Asn Thr Leu Gln Gln Thr Thr Leu Glu Ala Thr Gly Ile Thr 115 120 125 Ser Ser Val Gly Ser Thr Asn Tyr Ala Gly Phe Ser Leu Gly Ala Asp 130 135 140 Ser Val Thr Phe Ser Lys Gly Gly Ala Gly Thr Val Lys Leu Ser Gly 145 150 155 160 Val Ser Asp Ala Thr Ala Asp Thr Asp Ala Ala Thr Leu Lys Gln Val 165 170 175 Lys Glu Tyr Arg Thr Thr Leu Val Gly Asp Asn Asp Ile Thr Ala Ala 180 185 190 Asp Arg Ser Gly Gly Thr Ser Asn Gly Ile Thr Tyr Asn Leu Ser Leu 195 200 205 Asn Lys Gly Thr Val Ser Ala Thr Glu Glu Lys Val Val Ser Gly Lys 210 215 220 Thr Val Tyr Glu Ala Ile Arg Asn Ala Ile Thr Gly Asn Ile Phe Thr 225 230 235 240 Ile Gly Leu Asp Asp Thr Thr Leu Asn Lys Ile Asn Asn Pro Ala Asp 245 250 255 Gln Asp Leu Ser Asn Leu Ser Glu Ser Gly Lys Asn Ala Ile Thr Gly 260 265 270 Leu Val Asp Val Val Lys Lys Thr Asn Ser Pro Ile Thr Val Glu Pro 275 280 285 Ser Thr Asp Ser Asn Lys Lys Lys Thr Phe Thr Val Gly Val Asp Phe 290 295 300 Thr Asp Thr Ile Thr Glu Gly Asp Ala Thr Asp Asp Lys Lys Leu Thr 305 310 315 320 Thr Ser Lys Ser Val Glu Ser Tyr Val Thr Asn Lys Leu Ala Asn Phe 325 330 335 Ser Thr Asp Ile Leu Leu Ser Asp Gly Arg Ser Gly Asn Ala Thr Thr 340 345 350 Ala Asn Asp Gly Val Gly Lys Arg Arg Leu Ser Asp Gly Phe Thr Ile 355 360 365 Lys Ser Glu Asn Phe Thr Leu Gly Ser Lys Gln Tyr Asn Gly Ser Asp 370 375 380 Ser Leu Gly Val Met Tyr Asp Asp Gln Asn Gly Val Phe Lys Leu Ser 385 390 395 400 Leu Asn Met Thr Ala Leu Thr Thr Ser Leu Ala Asn Thr Phe Ala Lys 405 410 415 Leu Asp Ala Ser Asn Leu Thr Asp Asp Ser Asn Lys Glu Lys Trp Arg 420 425 430 Thr Ala Leu Asn Val Tyr Ser Lys Thr Glu Val Asp Ala Glu Ile Gln 435 440 445 Lys Ser Lys Val Thr Leu Thr Pro Asp Ser Gly Leu Ile Phe Ala Thr 450 455 460 Lys Gln Ala Gly Ser Gly Asn Asn Ala Gly Ile Asp Ala Gly Asn Lys 465 470 475 480 Lys Ile Ser Asn Val Ala Asp Gly Asp Ile Ser Pro Thr Ser Gly Asp 485 490 495 Val Val Thr Gly Arg Gln Leu Tyr Ala Leu Met Gln Lys Gly Ile Arg 500 505 510 Val Tyr Gly Asp Glu Val Ser Pro Thr Lys Thr Gln Thr Thr Ala Pro 515 520 525 Thr Asn Ala Asn Pro Thr Ala Thr Thr Ala Pro Thr Ala Ser Ser Thr 530 535 540 Gln Gly Gly Ser

Gly Leu Met Lys Asp Ile Glu Gly Val Asn Ser Ile 545 550 555 560 Thr Phe Asp Lys Ser Gly Gln Asp Leu Asn Gln Val Thr Gly Arg Met 565 570 575 Ser Ser Ala Gly Leu Thr Phe Lys Lys Gly Asp Thr Thr Asn Gly Ser 580 585 590 Thr Thr Thr Phe Ala Glu Asp Gly Leu Thr Ile Asp Ser Thr Thr Asn 595 600 605 Ser Ala Gln Thr Asn Leu Val Lys Val Ser Arg Asp Gly Phe Ser Val 610 615 620 Lys Asn Gly Ser Asp Glu Ser Lys Leu Ala Ser Thr Lys Leu Ser Ile 625 630 635 640 Gly Ala Glu Asn Ala Glu His Val Glu Val Thr Lys Ser Gly Ile Ala 645 650 655 Leu Lys Ala Asp Asn Thr Ser Asp Lys Ser Ser Ile Thr Leu Ala Gln 660 665 670 Asp Ala Ile Thr Leu Ala Gly Asn Ala Thr Gly Thr Ala Ile Lys Leu 675 680 685 Thr Gly Val Ala Asp Gly Asn Ile Thr Val Asn Ser Lys Asp Ala Val 690 695 700 Asn Gly Gly Gln Leu Arg Thr Leu Leu Gly Val Asp Ser Gly Ala Lys 705 710 715 720 Ile Gly 6810PRTArtificial SequenceDescription of Artificial Sequence Synthetic peptide 68Gly Gly Gly Gly Gly Gly Gly Gly Gly Gly 1 5 10 6912PRTArtificial SequenceDescription of Artificial Sequence Synthetic peptide 69Met Arg Gly Ser His His His His His His Gly Ser 1 5 10

Claims

1-19. (canceled)

20. A recombinant avian infectious coryza vaccine comprising as an active ingredient a peptide consisting of a sequence comprising the amino acid sequence shown by SEQ ID NO: 35, said sequence being within the amino acid sequence shown by SEQ ID NO: 1 with addition of 1 to 200 amino acid residues at the N-terminal and/or C-terminal thereof.

21. The vaccine of claim 20 wherein said vaccine comprises as an active ingredient a peptide consisting of the amino acid sequence shown by SEQ ID NO: 1.

22-23. (canceled)

24. The vaccine of claim 21 or 23 wherein said peptide comprises an amino acid sequence where one or several amino acids are deleted, added or replaced.