Egg allergic antigen

Abstract

The present invention relates to an antigen for egg allergy. The present invention provides a novel antigen for egg allergy, a diagnostic method and a diagnostic kit for egg allergy, a pharmaceutical composition containing the antigen, an egg or egg processed product with the antigen removed or reduced, or a bird producing the egg or hatched from the egg, or a method for producing an egg processed product with the antigen removed or reduced, and a detector for determining whether an object has an egg antigen.

Description

[0001] This application is a divisional application of Chinese patent application 201780034053.7. The application date of the original application 201780034053.7 is June 2, 2017, and its name is “Antigens for Egg Allergy”. Technical Field

[0002] The present invention relates to a novel antigen for egg allergy. The present invention also relates to a diagnostic kit, a diagnostic composition and a diagnostic method for egg allergy. The present invention also relates to a pharmaceutical composition containing the antigen, an egg or egg processed product with the antigen removed or reduced, or a bird produced or hatched from the egg. The present invention also relates to a method for producing an egg processed product with the antigen removed or reduced. The present invention further relates to a detector for determining whether an object has an egg antigen. Background Art

[0003] IgE antibodies specific to specific antigens (hereinafter, also referred to as allergens) are produced in the serum and tissues of allergy patients. The physiological consequences of the interaction between the IgE antibodies and the specific antigens cause allergic reactions. Antigens in a broad sense refer to foods / ingredients that cause allergic symptoms; in a narrow sense, they refer to proteins contained in foods / ingredients that are bound by specific IgE antibodies (hereinafter, also referred to as allergen components).

[0004] Most of the existing allergy detection reagents are prepared by simply grinding allergen candidate foods / ingredients to prepare antigen reagents (Patent Document 1). Therefore, among the allergen components contained in the existing antigen reagents, a positive reaction can only be detected in the allergy test when the binding with IgE antibodies exceeds the content that can determine a positive reaction threshold, and the diagnostic efficiency is not yet sufficiently high.

[0005] As egg allergens, the substances shown in the following table are currently known (Non-Patent Document 1).

[0006] [Table 1]

[0007]

[0008] Several allergen components have been suggested in food / ingredients that are candidates for allergens and have been commercialized as test kits. However, in order to improve the reliability of allergy detection, it is necessary to comprehensively limit the allergen components, but the patient detection rate by the determination of the above allergen components is still insufficient. Identification of new egg allergens is not only necessary to improve the accuracy of diagnostic reagents, but also very important as a target for hypoallergenic foods, hypoallergenic ingredients, and therapeutic drugs.

[0009] On the other hand, regarding the separation / purification of proteins, in recent years, as a method for separating and purifying a plurality of proteins from a small amount of sample, a two-dimensional electrophoresis method is used, in which isoelectric electrophoresis is performed in the first dimension and SDS-PAGE (sodium dodecyl sulfate-polyacrylamide gel electrophoresis) is performed in the second dimension. The applicant has so far developed a two-dimensional electrophoresis method with high separation capability (Patent Documents 2 to 5).

[0010] Prior art literature

[0011] Patent Literature

[0012] Patent Document 1: Japanese Patent Application Laid-Open No. 2002-286716

[0013] Patent Document 2: Japanese Patent Application Laid-Open No. 2011-33544

[0014] Patent Document 3: Japanese Patent Application Laid-Open No. 2011-33546

[0015] Patent Document 4: Japanese Patent Application Laid-Open No. 2011-33547

[0016] Patent Document 5: Japanese Patent Application Laid-Open No. 2011-33548

[0017] Non-patent literature

[0018] Non-patent document 1: Allergen Nomenclature, WHO / IUIS Allergen Nomenclature Sub-Committee, [May 31, 2008], インターネット<URL: http: / / www.allergen.org / search.php? allergenname=&allergensource=gallus+domesticus&TaxSource=&TaxOrder=&foodallerg=all&bioname=> Summary of the invention

[0019] Problem that the invention aims to solve

[0020] The present invention provides a novel antigen for egg allergy. The present invention also provides a method for diagnosing egg allergy and a diagnostic kit. The present invention also relates to a pharmaceutical composition containing the antigen, an egg or egg processed product with the antigen removed or reduced, or a bird that produces the egg or is hatched from the egg. The present invention further provides a detector for determining whether an object has an egg antigen.

[0021] Solutions for solving problems

[0022] The present inventors have conducted intensive research on the identification of antigens that are the cause of egg allergy in order to solve the above problems. As a result, they have successfully identified a novel antigen to which IgE antibodies in the serum of patients with egg allergy specifically bind. Based on this finding, the present invention has been completed.

[0023] That is, in one embodiment, the present invention is as follows.

[0024] [1] A diagnostic kit for egg allergy, comprising at least one of the following proteins (1) to (3) as an antigen:

[0025] (1) (1A) A protein comprising the C-terminal portion of vitellogenin-3 or a mutant thereof, which is any one of the following (1A-a) to (1A-e) as an antigen for egg allergy:

[0026] (1A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 2;

[0027] (1A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 2;

[0028] (1A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 1;

[0029] (1A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence shown in SEQ ID NO: 1; or

[0030] (1A-e) a protein containing an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence shown in SEQ ID NO: 1; or

[0031] (1B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 2 to 11;

[0032] (2) (2A) A protein comprising the C-terminal portion of vitellogenin-3 or a mutant thereof, which is any one of the following (2A-a) to (2A-e) that is an antigen for egg allergy:

[0033] (2A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO:13;

[0034] (2A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 13;

[0035] (2A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 12;

[0036] (2A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 12; or

[0037] (2A-e) a protein containing an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 12; or

[0038] (2B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 9 to 11, 13, 14 and 16;

[0039] (3) (3A) A protein comprising the central portion of vitellogenin-1 or the C-terminal portion of lipovitellin-1, or a mutant thereof, which is any one of the following proteins (3A-a) to (3A-e) that is an antigen for egg allergy:

[0040] (3A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO:18;

[0041] (3A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 18;

[0042] (3A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 17;

[0043] (3A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 17; or

[0044] (3A-e) a protein containing an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence set forth in SEQ ID NO: 17; or

[0045] (3B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 18 to 45.

[0046] [2] A composition for diagnosing egg allergy, comprising at least one of the proteins specified in (1) to (3) in [1] above as an antigen.

[0047] [3] A method for providing an indicator for diagnosing egg allergy in a subject, comprising the following steps:

[0048] (i) contacting a sample obtained from a subject with an antigen, wherein the sample is a solution containing IgE antibodies;

[0049] (ii) detecting the binding of IgE antibodies in a sample obtained from the subject to the antigen;

[0050] (iii) when the subject's IgE antibody is detected to be bound to the antigen, providing an indication that the subject has an egg allergy;

[0051] Here, the antigen is at least one of the proteins specified in (1) to (3) in [1] above.

[0052] [4] A pharmaceutical composition comprising at least one of the proteins defined in (1) to (3) in [1] above.

[0053] [5] The pharmaceutical composition according to [4] above, which is used for treating egg allergy.

[0054] [6] An egg, an egg product or a bird, characterized in that it is an egg, an egg product or a bird that produces or is hatched from an antigen removed or reduced, and the antigen is at least one of the proteins specified in (1) to (3) in [1] above.

[0055] [7] A detector for determining the presence or absence of an egg antigen in an object, characterized in that it contains an antibody that binds to at least one of the proteins specified as (1) to (3) in [1] above.

[0056] [8] A detector for determining the presence or absence of an antigen causing an egg allergy in an object, characterized in that it comprises a primer having a base sequence complementary to at least one of the base sequences shown in SEQ ID NOs. 1, 12 or 17.

[0057] [9] A diagnostic kit for egg allergy, comprising at least one of the following proteins (4) to (10) as an antigen:

[0058] (4) (4A) A protein comprising vitellogenin-3 or a mutant thereof, which is any one of the following proteins (4A-a) to (4A-e) that is an antigen for egg allergy:

[0059] (4A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO:47;

[0060] (4A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 47;

[0061] (4A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 46;

[0062] (4A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 46; or

[0063] (4A-e) a protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO:46; or

[0064] (4B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 47 to 57;

[0065] (5) (5A) A protein comprising vitellogenin-2 precursor or a mutant thereof, which is any one of the following proteins (5A-a) to (5A-e) that is an antigen for egg allergy:

[0066] (5A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO: 59;

[0067] (5A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 59;

[0068] (5A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 58.

[0069] (5A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 58; or

[0070] (5A-e) a protein containing an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence set forth in SEQ ID NO: 58; or

[0071] (5B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 59 to 104;

[0072] (6) (6A) Vitellogenin-2 precursor or a mutant thereof, which is any one of the following proteins (6A-a) to (6A-e) that is an antigen for egg allergy:

[0073] (6A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO:106;

[0074] (6A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 106;

[0075] (6A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 105;

[0076] (6A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 105; or

[0077] (6A-e) a protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 105; or

[0078] (6B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 106 to 150;

[0079] (7) (7A) Apolipoprotein B precursor or a mutant thereof, which is any one of the following proteins (7A-a) to (7A-e) that is an antigen for egg allergy:

[0080] (7A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO:152;

[0081] (7A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 152;

[0082] (7A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 151;

[0083] (7A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 151; or

[0084] (7A-e) a protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 151; or

[0085] (7B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 152 to 235;

[0086] (8) (8A) Apolipoprotein B precursor or a mutant thereof, which is any one of the following proteins (8A-a) to (8A-e) that is an antigen for egg allergy:

[0087] (8A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO: 237;

[0088] (8A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence of SEQ ID NO: 237;

[0089] (8A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 236;

[0090] (8A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 236; or

[0091] (8A-e) a protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence set forth in SEQ ID NO: 236; or

[0092] (8B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 237 to 249;

[0093] (9) (9A) Apolipoprotein B precursor or a mutant thereof, which is any one of the following proteins (9A-a) to (9A-e) that is an antigen for egg allergy:

[0094] (9A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO: 251;

[0095] (9A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence represented by SEQ ID NO: 251;

[0096] (9A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 250;

[0097] (9A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 250; or

[0098] (9A-e) a protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 250; or

[0099] (9B) a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 251 to 260;

[0100] (10) (10A) Vitellogenin-2 precursor or a mutant thereof, which is any one of the following proteins (10A-a) to (10A-e) that is an antigen for egg allergy:

[0101] (10A-a) a protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted, or added in SEQ ID NO: 262;

[0102] (10A-b) a protein comprising an amino acid sequence having an identity of 70% or more to the amino acid sequence set forth in SEQ ID NO: 262;

[0103] (10A-c) a protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 261;

[0104] (10A-d) a protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more to the base sequence set forth in SEQ ID NO: 261; or

[0105] (10A-e) a protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 261; or

[0106] (10B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 262 to 271.

[0107]

[10] A composition for diagnosing egg allergy, comprising at least one of the proteins defined in (4) to (10) in [9] above as an antigen.

[0108]

[11] A method for providing an indicator for diagnosing egg allergy in a subject, comprising the following steps:

[0109] (i) contacting a sample obtained from a subject with an antigen, wherein the sample is a solution containing IgE antibodies;

[0110] (ii) detecting the binding of IgE antibodies in a sample obtained from the subject to the antigen;

[0111] (iii) when the subject's IgE antibody is detected to be bound to the antigen, providing an indication that the subject has an egg allergy;

[0112] Here, the antigen is at least one of the proteins defined as (4) to (10) in [9] above.

[0113]

[12] A pharmaceutical composition comprising at least one of the proteins defined in (4) to (10) in [9] above.

[0114]

[13] The pharmaceutical composition according to the above-mentioned

[12] , which is used for treating egg allergy.

[0115]

[14] An egg, an egg product or a bird, characterized in that it is an egg, an egg product or a bird that produces or is hatched from an antigen removed or reduced, and the antigen is at least one of the proteins defined as (4) to (10) in [9] above.

[0116]

[15] A detector for determining the presence or absence of an egg antigen in an object, characterized in that it contains an antibody that binds to at least one of the proteins defined as (4) to (10) in [9] above.

[0117]

[16] A detector for determining the presence or absence of an antigen causing an egg allergy in an object, characterized in that it comprises a primer having a base sequence complementary to at least one of the base sequences shown in sequence numbers 46, 58, 105, 151, 236, 250 or 261.

[0118]

[17] A method for producing an egg processed product from which antigens have been removed or reduced, comprising the steps of: confirming that antigens have been removed or reduced during the production process of the processed product;

[0119] Here, the antigen is at least one of the proteins specified as (1) to (3) in [1] above, or at least one of the proteins specified as (4) to (10) in [9] above.

[0120]

[18] An egg-derived antigen which is at least one of the proteins specified as (1) to (3) in [1] above, or at least one of the proteins specified as (4) to (10) in [9] above, and which causes an egg allergy.

[0121] Effects of the Invention

[0122] According to the present invention, a novel antigen of egg allergy can be provided. In the present invention, a novel antigen (allergen component) causing egg allergy is identified, and thus a highly sensitive diagnosis method and diagnosis kit for egg allergy, a pharmaceutical composition containing the antigen, an egg or egg processed product with the antigen removed or reduced, or a bird producing the egg or hatched from the egg, or an egg processed product with the antigen removed or reduced, and a detector for determining whether an egg antigen is present in an object can be provided. BRIEF DESCRIPTION OF THE DRAWINGS

[0123] Figure 1 This is a gel photo showing the electrophoresis of proteins contained in the yolk of an egg (raw egg) using two-dimensional electrophoresis. The bands on the left side of the photo are bands of molecular weight markers, and the values ​​on the left side of the photo are the molecular weights (KDa) of each molecular weight marker. The values ​​on the top of the photo indicate the isoelectric point.

[0124] Figure 2 This is a photograph of a two-dimensional electrophoresis diagram of proteins contained in the yolk of an egg (raw egg), obtained by immunoblotting using the serum of the egg allergy patient 1.

[0125] Figure 3 This is a gel photograph showing a two-dimensional electrophoresis pattern of proteins contained in egg yolk (raw egg). Spots 1, 2, and 3 to which the serum of egg allergy patient 1 specifically reacted are shown enclosed by squares.

[0126] Figure 4 This is a photograph of a two-dimensional electrophoresis diagram of proteins contained in egg yolk (raw egg), obtained by immunoblotting using the serum of egg allergy patient 2. Spots 4 to 8, to which the serum of egg allergy patient 2 specifically reacted, are shown enclosed by boxes.

[0127] Figure 5 This is a photograph of a two-dimensional electrophoresis diagram of proteins contained in egg yolk (raw egg), obtained by immunoblotting using the serum of egg allergy patient 3. Spots 9 and 10, where the serum of egg allergy patient 3 specifically reacted, are respectively indicated by being enclosed by squares.

[0128] Figure 6This is a photograph of a two-dimensional electrophoresis diagram of proteins contained in egg yolk (raw egg), obtained by immunoblotting using the serum of egg allergy patient 4. The spot 11 to which the serum of egg allergy patient 4 specifically reacted is indicated by a box. DETAILED DESCRIPTION

[0129] The present invention will be described in detail below, but the present invention is not limited to these contents.

[0130] In this specification, unless otherwise defined, scientific terms and technical terms used in connection with the present invention have the meanings generally understood by those skilled in the art.

[0131] Allergy in this specification refers to: in an organism sensitive to a certain antigen, the state of allergic reaction that is produced when the antigen enters again and shows discomfort to the organism. Most of the allergic diseases in food produce IgE antibodies specific to antigens in blood and tissues. IgE antibodies are combined with mast cells or basophils. When the antigen specific to this IgE antibody enters the body of an allergic disease patient again, this antigen is combined with the IgE antibody combined with mast cells or basophils, and then this IgE antibody is cross-linked on the cell surface, producing the physiological effect of IgE antibody-antigen interaction. As their physiological effects, the release of histamine, 5-hydroxytryptamine, heparin, eosinophil chemotactic factor or various leukotrienes etc. can be listed. These released substances cause the allergic reaction produced by the combination of IgE antibodies and specific antigens. The allergic reaction produced by specific antigens is realized by the above-mentioned path.

[0132] In the present specification, the term "egg" refers to bird eggs, preferably chicken eggs.

[0133] In this specification, egg allergy refers to a state in which an allergic reaction occurs when a protein or the like contained in an egg is used as an antigen. Egg allergy refers to an allergic reaction that occurs when an antigen contained in an egg is contacted or ingested. Generally, an allergic reaction that occurs when a food is ingested is particularly referred to as a food allergy. Egg allergy may also be a food allergy.

[0134] In this specification, an antigen refers to a substance that causes an allergic reaction and is also called an allergen component. The antigen is preferably a protein.

[0135] In this specification, protein is a molecule having a structure in which natural amino acids are connected by peptide bonds. There is no particular limitation on the number of amino acids contained in a protein, and a protein in which about 2 to 50 amino acids are connected by peptide bonds is sometimes referred to as a peptide. In addition, with respect to amino acids, when optical isomers may exist, L-forms are indicated unless otherwise specified. The notation of the amino acid sequence of a protein or peptide used in this specification is as follows: Based on standard usage and the notation commonly used in the art, amino acids are indicated by a single character notation, with the left direction being the amino terminal direction and the right direction being the carboxyl terminal direction.

[0136] Antigen limitation

[0137] The above-mentioned method was used to define the antigens of egg allergy among the proteins contained in the egg. Specifically, the raw eggs were separated into yolk and white, and the egg proteins contained therein were subjected to two-dimensional electrophoresis under the following conditions.

[0138] The first dimension electrophoresis uses a gel with a gel length of 5 to 10 cm and a pH range of 3 to 10 as a gel for isoelectric point electrophoresis, and a pH gradient of the gel relative to the electrophoresis direction, when the total length of the gel is set as 1, the gel length to pH 5 is set as a, the gel length of pH 5 to 7 is set as b, and the gel length above pH 7 is set as c, a is in the range of 0.15 to 0.3, b is in the range of 0.4 to 0.7, and c is in the range of 0.15 to 0.3. Specifically, IPG gel Immobiline Drystrip (pH 3-10 NL) manufactured by GE Healthcare Bioscience (hereinafter referred to as GE) is used for isoelectric point electrophoresis. The electrophoresis apparatus used is IPGphor manufactured by GE. The upper limit of the electrophoresis current value was set to 75 μA per gel, and the voltage program was set as follows: (1) the constant voltage was increased from 300 V to 750 Vhr to perform a constant voltage process (the current variation amplitude during 30 minutes of electrophoresis before the end of this process was 5 μA); (2) the voltage was gradually increased from 300 Vhr to 1000 V; (3) further, the voltage was gradually increased from 4500 Vhr to 5000 V; (4) thereafter, the first-dimensional isoelectric point electrophoresis was performed at a constant voltage of 5000 V until Vhr reached 12000.

[0139] The second dimension electrophoresis uses a polyacrylamide gel in which the gel concentration at the base end of the swimming direction is set to 3-6% and the gel concentration at the front end of the swimming direction is set to be higher than the gel concentration at the base end of the swimming direction. Specifically, NuPAGE 4-12% Bris-Tris Gels IPG well mini 1mm manufactured by Life technologies is used for SDS-PAGE. The electrophoresis apparatus used is XCell SureLock Mini-Cell manufactured by Life technologies. As the swimming buffer, 50mM MOPS, 50mM Tris base, 0.1% (w / v) SDS, 1mM EDTA are used, and the swimming is carried out for about 45 minutes at a constant voltage of 200V.

[0140] The results showed that when the egg protein was subjected to two-dimensional electrophoresis under the above conditions, the antigens in spots 1 to 3 specifically bound to the IgE antibodies of patients with egg allergy who were diagnosed with food-dependent exercise-induced allergy (Food-Dependent Exercise-Induced Anaphylaxis). In addition, it was found that in patients with other egg allergies, the antigens in spots 4 to 11 specifically bound to the IgE antibodies of the patients ( Figures 4 to 6 ).

[0141] antigen

[0142] (1) Spot 1 antigen

[0143] As a result of sequence identification of spot 1 by mass spectrometry, amino acid sequences of SEQ ID NOs: 3 to 11 were detected.

[0144] In addition, for spot 1, the mass spectrum data (sequence numbers 3 to 11) obtained by the mass spectrometer were compared and analyzed with the protein data of NCBI, and identified as the C-terminal part of vitellogenin-3 (amino acid sequence: sequence number 2, base sequence encoding it: sequence number 1).

[0145] Therefore, in the present application, the antigen of spot 1 is any one of the following (1A-a) to (1A-e) and (1B).

[0146] (1A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 2.

[0147] (1A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the amino acid sequence shown in SEQ ID NO: 2.

[0148] (1A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 1.

[0149] (1A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 1.

[0150] (1A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence shown in SEQ ID NO: 1.

[0151] (1B) A protein containing at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs. 2 to 11, preferably a protein containing at least 2, 3, 4, 5, 6, 7, 8, 9 or all of the amino acid sequences. More preferably, a protein containing at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs. 2, 4 and SEQ ID NOs. 9 to 11, preferably a protein containing at least 2, 3, 4 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs. 3 to 11 may have one or more amino acids deleted, substituted, inserted or added.

[0152] The proteins of (1A-a) to (1A-e) and (1B) mentioned above may also be proteins that appear as spots with a molecular weight of 20 kDa to 40 kDa, preferably a molecular weight of 30 kDa to 35 kDa and an isoelectric point of 4.0 to 10.0, preferably 4.0 to 9.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0153] (2) Spot 2 antigen

[0154] As a result of sequence identification of spot 2 by mass spectrometry, amino acid sequences of SEQ ID NOs: 9 to 11, 14, and 16 were detected.

[0155] In addition, for spot 2, the mass spectrum data obtained by the mass spectrometer (sequence numbers 9 to 11, 14, and 16) were compared and analyzed with the protein data of NCBI, and identified as the C-terminal part of vitellogenin-3 (amino acid sequence: sequence number 13, base sequence encoding it: sequence number 12).

[0156] Therefore, in the present application, the antigen of spot 2 is any one of the following (2A-a) to (2A-e) and (2B).

[0157] (2A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO:13.

[0158] (2A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more with the amino acid sequence shown in SEQ ID NO: 13.

[0159] (2A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 12.

[0160] (2A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 12.

[0161] (2A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence shown in SEQ ID NO: 12.

[0162] (2B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 9 to 11, 13, 14, and 16, preferably a protein comprising at least 2, 3, 4, 5, or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 9 to 11, 13, and 16, preferably a protein comprising at least 2, 3, 4, or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 9 to 11, 13, 14, and 16 may have one or more amino acids deleted, substituted, inserted, or added.

[0163] The proteins of (2A-a) to (2A-e) and (2B) mentioned above may also be proteins that appear as spots with a molecular weight of 30 kDa to 60 kDa, preferably around 35 kDa to 40 kDa, and an isoelectric point of 5.0 to 10.0, preferably 6.0 to 9.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0164] (3) Spot 3 antigen

[0165] As a result of sequence identification of spot 3 by mass spectrometry, amino acid sequences of SEQ ID NOs: 19 to 45 were detected.

[0166] In addition, for spot 3, the mass spectrum data (sequence numbers 19 to 45) obtained by the mass spectrometer were compared and analyzed with the protein data of UniProt, and it was identified as the central part of vitellogenin-1 or the C-terminal part of yolk lipophosphoprotein-1 (Lipovitellin-1) that can be obtained by cutting on the N-terminal side of its protein (amino acid sequence: sequence number 18, base sequence encoding it: sequence number 17).

[0167] Therefore, in the present application, the antigen of spot 3 is any one of the following (3A-a) to (3A-e) and (3B).

[0168] (3A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO:18.

[0169] (3A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more with the amino acid sequence shown in SEQ ID NO: 18.

[0170] (3A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 17.

[0171] (3A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 17.

[0172] (3A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence shown in SEQ ID NO: 17.

[0173] (3B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 18 to 45, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 18, 19, 22 to 31, 33 to 35, 37, 39, 40, 42, 43 and 45, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 18 to 45 may contain one or more amino acids deleted, substituted, inserted or added.

[0174] The proteins of (3A-a) to (3A-e) and (3B) mentioned above may also be proteins that appear as spots with a molecular weight of 35 kDa to 60 kDa, preferably around 40 kDa to 50 kDa, and an isoelectric point of 5.0 to 10.0, preferably 6.0 to 9.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0175] (4) Spot 4 antigen

[0176] As a result of sequence identification of spot 4 by mass spectrometry, amino acid sequences of SEQ ID NOs: 48 to 57 were detected.

[0177] In addition, for spot 4, the mass spectrum data (SEQ ID NOs. 48 to 57) obtained by the mass spectrometer were compared and analyzed with the protein data of NCBI, and it was identified as vitellogenin-3 (amino acid sequence: SEQ ID NO. 47, base sequence encoding it: SEQ ID NO. 46).

[0178] Therefore, in the present application, the antigen of spot 4 is any one of the following (4A-a) to (4A-e) and (4B).

[0179] (4A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 47.

[0180] (4A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more with the amino acid sequence shown in SEQ ID NO: 47.

[0181] (4A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 46.

[0182] (4A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 46.

[0183] (4A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 46.

[0184] (4B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 47 to 57, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 47, 50, 51, 53 and 54, preferably a protein comprising at least 2, 3, 4 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 47 to 57 may have one or more amino acids deleted, substituted, inserted or added.

[0185] The proteins of (4A-a) to (4A-e) and (4B) mentioned above may also be proteins that appear as spots with a molecular weight of 20 kDa to 50 kDa, preferably a molecular weight of 25 kDa to 40 kDa, more preferably around a molecular weight of 30 kDa to 35 kDa, and an isoelectric point of 3.0 to 8.0, preferably 3.5 to 7.0, and further preferably 4.0 to 6.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0186] (5) Antigens of spots 5 and 6

[0187] As a result of sequence identification of spots 5 and 6 by mass spectrometry, amino acid sequences of SEQ ID NOs: 60 to 104 were detected.

[0188] In addition, for spots 5 and 6, the mass spectrum data (SEQ ID NOs. 60 to 104) obtained by the mass spectrometer were compared and analyzed with the protein data of NCBI, and they were identified as vitellogenin-2 precursor (amino acid sequence: SEQ ID NO. 59, base sequence encoding it: SEQ ID NO. 58).

[0189] Therefore, in the present application, the antigens of spots 5 and 6 are any of the following (5A-a) to (5A-e) and (5B).

[0190] (5A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 59.

[0191] (5A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more with the amino acid sequence shown in SEQ ID NO: 59.

[0192] (5A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 58.

[0193] (5A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 58.

[0194] (5A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 58.

[0195] (5B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 59 to 104, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 59, 60, 63, 65, 68, 69, 71, 73, 75 to 79, 81, 83 to 88, 91 to 94, 96 to 99 and 101 to 103, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 59 to 104 may have one or more amino acids deleted, substituted, inserted or added.

[0196] The proteins of (5A-a) to (5A-e) and (5B) mentioned above may also be proteins that appear as spots with a molecular weight of 80 kDa to 260 kDa, preferably a molecular weight of 90 kDa to 200 kDa, and more preferably a molecular weight of about 110 kDa to 160 kDa, and an isoelectric point of 1.0 to 8.0, preferably 2.0 to 7.0, and even more preferably 3.0 to 6.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0197] (6) Spot 7 antigen

[0198] As a result of sequence identification of spot 7 by mass spectrometry, an amino acid sequence of SEQ ID NOs: 107 to 150 was detected.

[0199] In addition, for spot 7, mass spectrum data (SEQ ID NOs. 107 to 150) obtained by a mass spectrometer were compared and analyzed with protein data from NCBI, and it was identified as vitellogenin-2 precursor (amino acid sequence: SEQ ID NO. 106, base sequence encoding it: SEQ ID NO. 105).

[0200] Therefore, in the present application, the antigen of spot 7 is any one of the following (6A-a) to (6A-e) and (6B).

[0201] (6A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 106.

[0202] (6A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more with the amino acid sequence shown in SEQ ID NO: 106.

[0203] (6A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 105.

[0204] (6A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 105.

[0205] (6A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 105.

[0206] (6B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 106 to 150, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 44 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 106, 108, 110, 111, 113, 114, 116, 117, 120 to 124, 126 to 131, 133, 134, 136 to 138, 140 to 143, 145 to 147 and 149, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 31 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 106 to 150 may have one or more amino acids deleted, substituted, inserted or added.

[0207] The proteins of (6A-a) to (6A-e) and (6B) mentioned above may also be proteins that appear as spots with a molecular weight of 110 kDa to 300 kDa, preferably a molecular weight of 130 kDa to 280 kDa, and more preferably a molecular weight of about 160 kDa to 260 kDa, and an isoelectric point of 3.0 to 8.0, preferably 3.5 to 7.0, and even more preferably 4.0 to 6.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0208] (7) Spot 8 antigen

[0209] As a result of sequence identification of spot 8 by mass spectrometry, an amino acid sequence of SEQ ID NOs: 153 to 235 was detected.

[0210] In addition, for spot 8, mass spectrum data (SEQ ID NOs. 153 to 235) obtained by a mass spectrometer were compared and analyzed with protein data from NCBI, and it was identified as apolipoprotein B precursor (amino acid sequence: SEQ ID NO. 152, base sequence encoding it: SEQ ID NO. 151).

[0211] Therefore, in the present application, the antigen of spot 8 is any one of the following (7A-a) to (7A-e) and (7B).

[0212] (7A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO:152.

[0213] (7A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the amino acid sequence shown in SEQ ID NO: 152.

[0214] (7A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 151.

[0215] (7A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 151.

[0216] (7A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 151.

[0217] (7B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 152 to 235, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55, 60, 65, 70, 75, 80, 83 sequences or all of the sequences. More preferably, the protein comprises at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 152, 154, 157 to 160, 163, 164, 167 to 172, 174, 175, 177, 178, 180, 182 to 185, 187, 189, 190, 192, 194 to 196, 198 to 200, 203 to 207, 209, 211, 212, 214 to 216, 220 to 229, 231 and 232, and preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 15, 20, 25, 30, 35, 40, 45, 50, 55 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 152 to 235 may have one or more amino acids deleted, substituted, inserted or added.

[0218] The proteins of (7A-a) to (7A-e) and (7B) mentioned above may also be proteins that appear as spots with a molecular weight of 160 kDa to 550 kDa, preferably a molecular weight of 180 kDa to 400 kDa, and more preferably a molecular weight of around 200 kDa to 300 kDa, and an isoelectric point of 3.0 to 8.0, preferably 3.5 to 7.0, and even more preferably 4.0 to 6.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0219] (8) Spot 9 antigen

[0220] As a result of sequence identification of spot 9 by mass spectrometry, amino acid sequences of SEQ ID NOs: 238 to 249 were detected.

[0221] In addition, for spot 9, mass spectrum data (SEQ ID NOs. 238 to 249) obtained by a mass spectrometer were compared and analyzed with protein data from NCBI, and it was identified as apolipoprotein B precursor (amino acid sequence: SEQ ID NO. 237, base sequence encoding it: SEQ ID NO. 236).

[0222] Therefore, in the present application, the antigen of spot 9 is any one of the following (8A-a) to (8A-e) and (8B).

[0223] (8A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 237.

[0224] (8A-b) A protein comprising an amino acid sequence that is 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more identical to the amino acid sequence shown in SEQ ID NO: 237.

[0225] (8A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 236.

[0226] (8A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 236.

[0227] (8A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 236.

[0228] (8B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 237 to 249, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 237 to 239, 241, 242, 244 and 246 to 249, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 237 to 249 may have one or more amino acids deleted, substituted, inserted or added.

[0229] The proteins of (8A-a) to (8A-e) and (8B) mentioned above may also be proteins that appear as spots with a molecular weight of 20 kDa to 50 kDa, preferably a molecular weight of 25 kDa to 45 kDa, more preferably around a molecular weight of 30 kDa to 40 kDa, and an isoelectric point of 7.0 to 11.0, preferably 8.0 to 10.0, and even more preferably 9.0 to 10.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0230] (9) Spot 10 antigen

[0231] As a result of sequence identification of spot 10 by mass spectrometry, an amino acid sequence of SEQ ID NOs: 252 to 260 was detected.

[0232] In addition, the mass spectrum data (SEQ ID NOs. 252 to 260) obtained by the mass spectrometer were compared and analyzed with the protein data of NCBI, and spot 10 was identified as apolipoprotein B precursor (amino acid sequence: SEQ ID NO. 251, base sequence encoding it: SEQ ID NO. 250).

[0233] Therefore, in the present application, the antigen of spot 10 is any one of the following (9A-a) to (9A-e) and (9B).

[0234] (9A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 251.

[0235] (9A-b) A protein comprising an amino acid sequence that is 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more identical to the amino acid sequence shown in SEQ ID NO: 251.

[0236] (9A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted, or added in SEQ ID NO: 250.

[0237] (9A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 250.

[0238] (9A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 250.

[0239] (9B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 251 to 260, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 251 to 254, 256, 257 and 260, preferably a protein comprising at least 2, 3, 4, 5, 6 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 251 to 260 may have one or more amino acids deleted, substituted, inserted or added.

[0240] The proteins of (9A-a) to (9A-e) and (9B) mentioned above may also be proteins that appear as spots with a molecular weight of 20 kDa to 50 kDa, preferably a molecular weight of 25 kDa to 45 kDa, more preferably around a molecular weight of 30 kDa to 40 kDa, and an isoelectric point of 7.0 to 11.0, preferably 8.0 to 10.0, and even more preferably 9.0 to 10.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0241] (10) Antigen of spot 11

[0242] As a result of sequence identification of spot 11 by mass spectrometry, the amino acid sequence of SEQ ID NOs: 263 to 271 was detected.

[0243] In addition, for spot 11, the mass spectrum data (sequence numbers 263 to 271) obtained by the mass spectrometer were compared and analyzed with the protein data of NCBI, and it was identified as vitellogenin-2 precursor (amino acid sequence: sequence number 262, base sequence encoding it: sequence number 261).

[0244] Therefore, in the present application, the antigen of spot 11 is any one of the following (10A-a) to (10A-e) and (10B).

[0245] (10A-a) A protein comprising an amino acid sequence in which one or more amino acids are deleted, substituted, inserted or added in SEQ ID NO: 262.

[0246] (10A-b) A protein comprising an amino acid sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the amino acid sequence shown in SEQ ID NO: 262.

[0247] (10A-c) A protein comprising an amino acid sequence encoded by a base sequence in which one or more nucleotides are deleted, substituted, inserted or added in SEQ ID NO: 261.

[0248] (10A-d) A protein comprising an amino acid sequence encoded by a base sequence having an identity of 70% or more, preferably 75% or more, 80% or more, 85% or more, 90% or more, 95% or more, 97% or more, 98% or more, or 99% or more to the base sequence shown in SEQ ID NO: 261.

[0249] (10A-e) A protein comprising an amino acid sequence encoded by a nucleic acid that hybridizes under stringent conditions with a nucleic acid consisting of a base sequence complementary to the base sequence represented by SEQ ID NO: 261.

[0250] (10B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 262 to 271, preferably a protein comprising at least 2, 3, 4, 5, 6, 7, 8, 9 or all of the amino acid sequences. More preferably, a protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 262 to 265, 268 and 269, preferably a protein comprising at least 2, 3, 4, 5 or all of the amino acid sequences. The amino acid sequence represented by any one of SEQ ID NOs: 262 to 271 may have one or more amino acids deleted, substituted, inserted or added.

[0251] The proteins (10A-a) to (10A-e) and (10B) mentioned above may also be proteins that appear as spots with a molecular weight of 15 kDa to 40 kDa, preferably a molecular weight of 17 kDa to 35 kDa, more preferably around a molecular weight of 20 kDa to 30 kDa, and an isoelectric point of 6.0 to 11.0, preferably 7.0 to 10.0, and even more preferably 8.0 to 10.0, in the gel when two-dimensional electrophoresis is performed under the conditions described in the above-mentioned "Limitation of Antigens" item.

[0252] The proteins as antigens described in (1) to (3) and (4) to (10) above also include proteins whose amino acid residues are modified by phosphorylation, sugar chain modification, aminoacylation, ring opening, deamination, etc.

[0253] Preferably, the protein as an antigen in (1) to (3) and (4) to (10) above is an antigen for egg allergy.

[0254] In the present specification, the situation of "one or more amino acids are deleted, substituted, inserted or added" in an amino acid sequence means that in the amino acid sequence of interest, one or more amino acids are deleted (for example, 30%, preferably 25%, 20%, 15%, 10%, 5%, 3%, 2% or 1% of the amino acids relative to the total length of the amino acid sequence), or are substituted with other amino acids, or other amino acids are inserted, and / or other amino acids are added to form an amino acid sequence.

[0255] In the above, the substitution is preferably a conservative substitution. Conservative substitution refers to replacing a specific amino acid residue with a residue having similar physical and chemical characteristics; any substitution can be made as long as the characteristics related to the original sequence structure are not substantially changed. For example, the substitution of amino acids can be made as long as the helix present in the original sequence is not destroyed, or other types of secondary structures that are characteristics of the original sequence are not destroyed. In the following, conservative substitutions of amino acid residues are exemplified according to the classification of residues that can be substituted, but the amino acid residues that can be substituted are not limited to the substances described below.

[0256] Group A: leucine, isoleucine, valine, alanine, methionine

[0257] Group B: Aspartic acid, Glutamic acid

[0258] Group C: Asparagine, Glutamine

[0259] Group D: lysine, arginine

[0260] Group E: Serine, Threonine

[0261] Group F: Phenylalanine, Tyrosine

[0262] In the case of non-conservative substitutions, one of the above-mentioned types can also be replaced with a member of another type. For example, in order to exclude unexpected sugar chain modifications, the amino acids in the above-mentioned B, D, and E groups can also be replaced with amino acids in other groups. Alternatively, in order to prevent folding in the three-dimensional protein, cysteine ​​can be deleted or replaced with other amino acids. Alternatively, in order to maintain the hydrophilicity / hydrophobicity balance, or to facilitate synthesis, the hydrophilicity index (hydropathy index) of amino acids related to amino acids as a hydrophobicity / hydrophilicity index (J. Kyte and R. Doolittle, J. Mol. Biol., Vol. 157, p. 105-132, 1982) can also be replaced with amino acids in order to increase the hydrophilicity.

[0263] In this specification, the % identity of two amino acid sequences can be determined by visual inspection and mathematical calculation. In addition, computer programs can also be used to determine the % identity. As such computer programs, for example, BLAST and ClustalW can be listed. In particular, the various conditions (parameters) of the identity search using the BLAST program can be recorded according to Altschul et al. (Nucl. Acids. Res., 25, p. 3389-3402, 1997), from the National Center for Biotechnology Information (NCBI), DNA Data Bank of Japan (DDBJ) website, etc., publicly obtained (BLAST manual, Altschul et al. NCB / NLM / NIH Bethesda, MD 20894; Altschul et al.). In addition, programs such as genetic information processing software GENETYX Ver. 7 (GENETYX), DINASIS Pro (Hitachi Soft, Ltd.), Vector NTI (Infomax) can also be used to determine.

[0264] In this specification, the situation of "deletion, substitution, insertion or addition of one or more nucleotides" in the base sequence means that in the base sequence to be targeted, one or more nucleotides are deleted (for example, 30%, preferably 25%, 20%, 15%, 10%, 5%, 3%, 2% or 1% of the amino acids relative to the total length of the base sequence), or replaced with other nucleotides, or inserted with other nucleotides, and / or the base sequence formed by the addition of other nucleotides. It is preferred that no frame shift is generated in the sequence encoding the amino acid by the deletion, substitution, insertion or addition of the above nucleotides.

[0265] In this specification, the % identity of two base sequences can be determined by visual inspection and mathematical calculation. In addition, the % identity can also be determined using a computer program. As such a sequence comparison computer program, for example, the BLASTN program (Altschul et al. (1990) J. Mol. Biol. 215: 403-10) available from the website of the National Library of Medicine of the United States can be used, and the default parameters (Default Parameter) are used to determine.

[0266] In this specification, "stringent conditions" refers to hybridization under moderate or highly stringent conditions. Specifically, as moderately stringent conditions, for example, a person skilled in the art with general skills can easily determine based on the length of the DNA. Basic conditions are shown in Sambrook et al., Molecular Cloning: A Laboratory Manual, 3rd edition, Chapter 6-7, Cold Spring Harbor Laboratory Press, 2001. Preferably, moderately stringent conditions as hybridization conditions include: 1×SSC to 6×SSC, 42°C to 55°C; more preferably 1×SSC to 3×SSC, 45°C to 50°C; most preferably 2×SSC, 50°C. When the hybridization solution contains, for example, about 50% formamide, a temperature 5 to 15°C lower than the above temperature can be used. Washing conditions include: 0.5×SSC to 6×SSC, 40°C to 60°C. During hybridization and washing, 0.05% to 0.2%, preferably about 0.1% SDS is usually added. As highly stringent conditions, it can also be easily determined by a person skilled in the art based on the length of the DNA, for example. Generally, highly stringent conditions include hybridization and / or washing with a higher temperature and / or a lower salt concentration than moderately stringent conditions. For example, as hybridization conditions, there can be listed: 0.1×SSC to 2×SSC, 55°C to 65°C; more preferably 0.1×SSC to 1×SSC, 60°C to 65°C; most preferably 0.2×SSC, 63°C. As washing conditions, there can be listed: 0.2×SSC to 2×SSC, 50°C to 68°C, more preferably 0.2×SSC, 60 to 65°C.

[0267] Antigens can also be obtained by separation / purification from eggs (preferably chicken eggs) by combining protein purification methods known to those skilled in the art. Alternatively, antigens can also be obtained by expressing antigens as recombinant proteins using gene recombination techniques known to those skilled in the art, and then by separation / purification using protein purification methods known to those skilled in the art.

[0268] Examples of protein purification methods include methods utilizing solubility such as salting out and solvent precipitation; methods utilizing differences in molecular weight such as dialysis, ultrafiltration, gel filtration, and SDS-PAGE; methods utilizing charge such as ion exchange chromatography and hydroxyapatite chromatography; methods utilizing specific affinity such as affinity chromatography; methods utilizing differences in hydrophobicity such as reversed-phase high performance liquid chromatography; and methods utilizing differences in isoelectric points such as isoelectric point electrophoresis.

[0269] The preparation of proteins using genetic recombination technology can be carried out as follows: prepare an expression vector containing a nucleic acid encoding an antigen, introduce the expression vector into a suitable host cell by gene introduction or transformation, culture the host cell under conditions suitable for the expression of the recombinant protein, and then recover the recombinant protein expressed in the host cell.

[0270] A "vector" is a nucleic acid that can be used to introduce a nucleic acid connected to it into a host cell; an "expression vector" is a vector that can guide the expression of a protein encoded by a nucleic acid introduced by the vector. Vectors include plasmid vectors, viral vectors, etc. Those skilled in the art can select an expression vector suitable for recombinant protein expression according to the type of host cell used.

[0271] "Host cell" is a cell into which a gene has been introduced or transformed by a vector. The host cell can be appropriately selected by a person skilled in the art according to the vector used. The host cell can be derived from a prokaryotic organism such as Escherichia coli (E. coli). When a prokaryotic cell such as Escherichia coli is used as a host, in order to facilitate the expression of the recombinant protein in the prokaryotic cell, the antigen of the present invention preferably contains an N-terminal methionine residue. The N-terminal methionine can also be cut off from the recombinant protein after expression. Alternatively, it can be a unicellular eukaryotic organism such as yeast; a cell from a eukaryotic organism such as a plant cell, an animal cell (for example, a human cell, a monkey cell, a hamster cell, a rat cell, a mouse cell or an insect cell), or a silkworm.

[0272] The gene introduction or transformation of the expression vector to the host cell can be suitably carried out by methods well known to those skilled in the art. In addition, those skilled in the art will suitably select conditions suitable for expressing the recombinant protein to cultivate the host cell according to the type of the host cell, so that the recombinant protein can be expressed. Then, the host cell expressing the recombinant protein is homogenized, and the method of purifying the above-mentioned protein by the homogenous mixture obtained is suitably combined, so that the antigen expressed as the recombinant protein can be separated / purified.

[0273] Diagnostic kits / diagnostic methods

[0274] The present invention provides a method for diagnosing an indicator of egg allergy in a subject, comprising the following steps:

[0275] (i) contacting a sample obtained from a subject with an antigen, wherein the sample is a solution containing IgE antibodies;

[0276] (ii) detecting the binding of IgE antibodies in a sample obtained from the subject to the antigen;

[0277] (iii) when binding of the subject's IgE antibodies to the antigen is detected, providing an indication that the subject has an egg allergy;

[0278] Here, the antigen is at least one of the proteins specified as the antigens in (1) to (3) and (4) to (10) above.

[0279] The sample obtained from the object refers to a solution containing IgE antibodies collected from the object. Such a solution contains, for example, blood, saliva, sputum, nasal mucus, urine, sweat, and tears. Before contacting with the antigen, the sample obtained from the object may also be subjected to a pretreatment for increasing the concentration of IgE antibodies in the sample. As a pretreatment of the sample, it may also include, for example, obtaining serum or plasma from blood. In addition, the Fab portion as the antigen-binding portion may also be further purified. In a particularly preferred embodiment, the above-mentioned step (i) is performed by contacting the IgE antibodies in the serum obtained from the object with the antigen.

[0280] The IgE antibody may be the IgE antibody itself, or may be a mast cell or the like to which the IgE antibody binds.

[0281] The contact of the sample obtained from the object with the antigen and the detection of their combination can be carried out by known methods. As such a method, for example, ELISA (enzyme-linked immunosorbent assay), sandwich immunoassay, protein immunoblotting, immunoprecipitation, and immunochromatography can be used. These are all methods of contacting and combining the antigen with the object IgE antibody, causing it to act on the secondary antibody formed by enzyme labeling of the IgE antibody specifically bound to the antigen, adding the substrate of the enzyme (usually a color developing or luminescent reagent) to detect the product of the enzyme reaction, thereby being able to detect the method of binding the antigen to the object IgE antibody. Or a method for detecting a fluorescently labeled secondary antibody. Alternatively, it is also possible to use surface plasmon resonance (SPR) and other assays that can evaluate the binding of antigens to IgE antibodies for detection. It is also possible to mix a variety of antigen-specific IgE antibodies.

[0282] The antigen may also be in a state where the separated antigen is fixed to a carrier. In this case, ELISA, sandwich immunoassay, immunochromatography, surface plasmon resonance may be used in the above steps (i) and (ii); in addition, in the above step (i), the sample obtained from the object is contacted with the surface on which the antigen is fixed. The separated antigen can be obtained by separation / purification from eggs (preferably chicken eggs) in combination with a protein purification method known to those skilled in the art, or it can also be prepared by genetic recombination technology. In addition, the antibody may be fixed.

[0283] The antigen may also be in a state of being fixed to a carrier. In this case, in the above steps (i) and (ii), a flow cytometer or the like may be used, and the presence of the antigen bound to the antibody may be confirmed by laser. Examples thereof include a basophil activation test (BAT) and the like. In addition, a histamine free test (HRT) may also be used to confirm whether histamine is freed by further contacting the antigen with the blood cells in the sample.

[0284] In addition, the antigen can also be transferred from a state separated by two-dimensional electrophoresis and detected by protein immunoblotting. Two-dimensional electrophoresis is a method of separating protein samples by performing isoelectric point electrophoresis in the first dimension and SDS-PAGE (SDS-polyacrylamide gel electrophoresis) in the second dimension. In this case, the conditions of two-dimensional electrophoresis are not particularly limited as long as they are conditions that can separate the antigens of the present invention. For example, the conditions of two-dimensional electrophoresis described in the above-mentioned "Limitation of Antigens" item can be used. Alternatively, the electrophoresis conditions can be set with reference to the records of the above-mentioned patent documents 1 to 4, for example, two-dimensional electrophoresis is performed under at least one condition selected from the group consisting of the following:

[0285] (A) As a first-dimensional isoelectric point electrophoresis gel, when the gel length is in the range of 5 to 10 cm and the pH range of the gel is 3 to 10, the gel length of the pH gradient of the gel relative to the migration direction up to pH 5 is set as a, the gel length of pH 5 to 7 is set as b, and the gel length of pH 7 or above is set as c, the relationship of "a < b" and "b > c" is satisfied;

[0286] (B) In the case of (A), when the total length of the gel is 1, a is in the range of 0.15 to 0.3, b is in the range of 0.4 to 0.7, and c is in the range of 0.15 to 0.3;

[0287] (C) in the first-dimensional isoelectric point electrophoresis, a constant voltage of 100 V to 600 V is applied to each gel containing the sample to perform a constant voltage step, and after the electrophoresis amplitude is within the range of 5 μA for every 30 minutes of electrophoresis, a voltage increase step is started to increase the voltage from the constant voltage;

[0288] (D) In ​​the case of (C), the final voltage of the voltage increasing step is set within the range of 3000V to 6000V;

[0289] (E) the length of the first-dimension isoelectric point electrophoresis gel in the long-side direction is set to 5 to 10 cm, and the gel concentration at the base end of the second-dimension electrophoresis gel in the migration direction is set to 3 to 6%; and

[0290] (F) In the case of (E), the gel concentration at the front end side portion in the migration direction of the second-dimensional electrophoresis gel is set higher than the gel concentration at the base end portion in the migration direction.

[0291] The antigens of (1) to (3) and (4) to (10) above are antigens that specifically bind to IgE antibodies of patients with egg allergy. Therefore, if the binding of the subject's IgE antibodies to the antigen is detected, it provides an indicator that the subject is egg allergic.

[0292] The present invention also provides a diagnostic kit for egg allergy comprising at least one of the above-mentioned antigens (1) to (3) and (4) to (10). The diagnostic kit of the present invention can be used in the above-mentioned method for providing indicators for diagnosing egg allergy or the following diagnostic method. In addition to containing at least one of the above-mentioned antigens (1) to (3) and (4) to (10), the diagnostic kit of the present invention may also contain an enzyme-labeled anti-IgE antibody and a colorimetric substrate or a luminescent substrate that serves as a substrate for the enzyme. In addition, a fluorescently labeled anti-IgE antibody may also be used. In the diagnostic kit of the present invention, the antigen may also be provided in a state where the antigen is immobilized on a carrier. The diagnostic kit of the present invention may also be provided together with instructions regarding the steps used for diagnosis and a method package containing the instructions.

[0293] In another embodiment, the diagnostic kit includes a companion diagnostic drug for egg allergy. A companion diagnostic drug refers to a substance used for the following purposes: identifying patients who expect the effect of a drug or patients who are at risk of severe side effects of a drug, or studying the reactivity of the drug in order to optimize the treatment using the drug. Here, the optimization of treatment includes, for example, determining the dosage volume, determining the suspension of drug administration, and confirming whether immune tolerance is obtained by using which allergen component.

[0294] The present invention also provides a composition for diagnosing egg allergy, comprising at least one of the above-mentioned antigens (1) to (3) and (4) to (10). The composition for diagnosing the present invention can be used in the following diagnostic method. The composition for diagnosing the present invention can also contain pharmaceutically acceptable carriers and additives that are usually used together with the antigen of the present invention, as required.

[0295] In one embodiment, the present invention is a method for diagnosing egg allergy in a subject, comprising the following steps:

[0296] (i) contacting a sample obtained from a subject with an antigen;

[0297] (ii) detecting the binding of IgE antibodies in a sample obtained from the subject to the antigen;

[0298] (iii) when the subject's IgE antibody is detected to be bound to the antigen, the subject is judged to have an egg allergy;

[0299] Here, the antigen is at least one of the proteins defined as the antigens in (1) to (3) and (4) to (10) above. The steps (i) and (ii) are performed according to the description of the steps of the method for providing an indicator for diagnosing egg allergy.

[0300] In another embodiment, the present invention provides a method for diagnosing an egg allergy in a subject, comprising administering to the subject at least one of the antigens of (1) to (3) and (4) to (10) above. The method may also be performed in the form of a skin test characterized in that the antigen is administered to the skin. The skin test includes the following forms: a prick test in which a diagnostic composition is applied to the skin, the skin is lightly scratched to a level that does not bleed, the skin is penetrated with the antigen, and then the skin reaction is observed; a scratch test in which the skin is lightly scratched after the diagnostic composition is applied and then the reaction is observed; a patch test in which a diagnostic composition in the form of a cream, ointment, etc. is applied to the skin and then the reaction is observed; an intradermal test in which the antigen is administered intradermally and then the reaction is observed; etc. In the case where a skin reaction such as swelling occurs on the part of the skin to which the antigen is applied, the subject is diagnosed as having an egg allergy. Here, the amount of antigen administered to the skin may be, for example, an amount of 100 μg or less per time.

[0301] In the diagnosis of allergy, a load test for the purpose of limiting antigens is often performed. At least one of the antigens (1) to (3) and (4) to (10) above can be used as an effective component of a load test for diagnosing egg allergy. Here, the antigen protein used in the load test may be a purified protein or a protein expressed in food / ingredients, such as pollen rice in which a gene for a Chinese fir pollen antigen is transformed into rice and the antigen protein is expressed in rice.

[0302] In another embodiment, the present invention provides at least one of the antigens (1) to (3) and (4) to (10) for use in diagnosing egg allergy. This also includes providing at least one of the antigens (1) to (3) and (4) to (10) mixed with a known antigen.

[0303] In yet another embodiment, the present invention provides use of at least one of the antigens of (1) to (3) and (4) to (10) above in the preparation of a diagnostic drug for egg allergy.

[0304] Pharmaceutical compositions / therapeutic methods

[0305] The present invention provides a pharmaceutical composition comprising at least one of the antigens described in (1) to (3) and (4) to (10).

[0306] In one embodiment, the above-mentioned pharmaceutical composition is used to treat egg allergy.

[0307] The present invention also provides a method for treating egg allergy, comprising administering at least one of the antigens (1) to (3) and (4) to (10) above to a patient in need of treatment for egg allergy.

[0308] In another embodiment, the present invention provides at least one of the antigens (1) to (3) and (4) to (10) for use in the treatment of egg allergy. In yet another embodiment, the present invention provides use of at least one of the antigens (1) to (3) and (4) to (10) for the preparation of a therapeutic drug for egg allergy.

[0309] In the treatment of allergies, desensitization therapy is often performed in which the purpose is to induce immune tolerance by administering antigens to patients. At least one of the antigens (1) to (3) and (4) to (10) can be used as an active ingredient in the desensitization therapy for treating egg allergies. Here, the antigen protein used in the desensitization therapy may be a purified protein or a protein expressed in food / ingredients, such as pollen rice in which a gene for a cedar pollen antigen is transformed into rice and the antigen protein is expressed in rice.

[0310] The pharmaceutical composition of the present invention can be administered via common administration routes, including, for example, oral, sublingual, transdermal, intradermal, subcutaneous, intravascular, intranasal, intramuscular, intraperitoneal, and intrarectal administration.

[0311] The pharmaceutical composition of the present invention can be used as needed together with the antigen of the present invention by conventional methods to add commonly used pharmaceutically permitted adjuvants, excipients, or various additives (such as stabilizers, cosolvents, emulsifiers, buffers, storage agents, colorants, etc.) to the pharmaceutical composition. The dosage form of the pharmaceutical composition can be appropriately selected by a person skilled in the art according to the route of administration. It can also be in the form of, for example, tablets, capsules, syrups, sublingual tablets, injections, nasal sprays, ointments, solutions, creams, lotions, etc. The dosage, number of administrations and / or administration period of the pharmaceutical composition of the present invention can be appropriately selected by a physician according to the characteristics of the patient such as the route of administration, symptoms, age, and weight. For example, in the case of adults, it can also be administered in an amount of less than 100 μg per time. The dosing interval can be, for example, once a day, once a week, twice a month, or once every three months. The administration period can be, for example, several weeks to several years. During the administration period, it can also be an administration method that increases the dosage in a gradient.

[0312] Detector

[0313] The present invention provides a detector comprising an antibody against at least one of the antigens of (1) to (3) and (4) to (10) above.

[0314] The antibody can be prepared by conventional methods. For example, it can be prepared by immunizing mammals such as rabbits with the antigens of (1) to (3) and (4) to (10) above. The antibody can be an IgE antibody, a polyclonal antibody, a monoclonal antibody, or an antigen-binding fragment thereof (e.g., Fab, F(ab')2, Fab').

[0315] In addition, in the above-mentioned detector, the antibody can be provided in the form of being bound to a carrier. The carrier is not particularly limited as long as it can be used in the detection of antibody-antigen binding. Any carrier known to those skilled in the art can be used.

[0316] Examples of methods for examining whether an antigen is contained include the following methods.

[0317] A method in which a detector containing the prepared IgE antibody is brought into contact with a sample obtained from a food / ingredient, etc., and the binding of the IgE antibody to an antigen in the sample is detected using, for example, an ELISA method, and when the binding of the IgE antibody to the antigen is detected, it is determined that the antigen remains in the target food / ingredient, etc.

[0318] A method in which food / ingredients are wrapped with filter paper or the like and reacted with an antibody solution to detect antigens contained therein.

[0319] Another embodiment of the present invention includes a detector for determining the presence or absence of an antigen causing an egg allergy in an object, characterized in that it includes a primer having a base sequence complementary to at least a portion of the base sequence shown in SEQ ID NO: 1, 12, 17, 46, 58, 105, 151, 236, 250, or 261. In a non-limiting manner, the primer has, for example, a base sequence complementary to a portion of the 3' end or the central portion of at least one of the base sequences shown in SEQ ID NO: 1, 12, 17, 46, 58, 105, 151, 236, 250, or 261, preferably 12 bases, 15 bases, 20 bases, or 25 bases. In particular, when mRNA is used as the object, the primer has a complementary primer of a poly(A) tail. In a preferred embodiment, the detector comprising the above-mentioned primers further comprises a primer comprising a base sequence at the 5' end portion of at least one of the base sequences shown in sequence numbers 1, 12, 17, 46, 58, 105, 151, 236, 250 or 261, preferably a base sequence consisting of 12 bases, 15 bases, 20 bases or 25 bases.

[0320] For example, cDNA is amplified by PCR (polymerase chain reaction) including RT-PCR using DNA or mRNA obtained from eggs or birds as a template and the complementary primers, and the presence or absence of the antigen is determined by comparing the sequence of the amplified cDNA with SEQ ID NOs: 1, 12, 17, 46, 58, 105, 151, 236, 250 or 261. Examples of methods for amplification by PCR include RACE method and the like. At this time, when a point mutation encoding the same amino acid is present in the comparison between the amplified cDNA and sequence number 1, 12, 17, 46, 58, 105, 151, 236, 250 or 261; or, even if there is a base insertion, deletion, substitution or addition in the base sequence of the amplified cDNA to the base sequence of sequence number 1, 12, 17, 46, 58, 105, 151, 236, 250 or 261, the antigen is judged to be present when the amino acid sequence encoding the cDNA has an identity of 70% or more, preferably 80, 90, 95, 98, 99% or more, to the amino acid sequence of sequence number 2, 13, 18, 47, 59, 106, 152, 237, 251 or 262.

[0321] In one embodiment, the detector can be used to detect whether antigens are contained in food (eggs or birds) or in objects in food production lines. The detector can be used by manufacturers to check the quality of products on production lines and before shipment; it can also be used by tasters to check whether the target food / ingredients contain antigens.

[0322] Antigen-removed foods, etc.

[0323] The present invention provides an egg, an egg processed product, or a bird producing the egg or hatched from the egg, characterized in that at least one of the antigens (1) to (3) and (4) to (10) is removed or reduced.

[0324] The method for removing or reducing antigens of the present invention is not limited to eggs, processed egg products, or birds that produce or hatch eggs. The removal or reduction of antigens is not limited to the removal or reduction of antigens of the present invention, and any method may be used.

[0325] For example, eggs in which the expression of the antigen of the present invention is deleted or reduced can be prepared using gene knockout technology to produce eggs in which the expression of the antigen of the present invention is knocked out.

[0326] The gene knockout technology can use any of the methods known to those skilled in the art. For example, Oishi, et al. (Scientific Reports, Vol. 6, Article number: 23980, 2016, doi: 10.1038 / srep23980) describes the application of CRISPER / Cas9 to primordial germ cells of chickens as a genome editing technology to obtain individuals with ovomucoid gene deletions. The same method can also be used to obtain eggs from which antigens have been removed in the present invention. In addition, birds or eggs that do not contain antigens or have low antigen content can also be mated through artificial insemination to obtain birds or eggs from which antigens have been removed / reduced in the present invention. Artificial mating of birds or eggs can be performed by conventional methods.

[0327] The processed egg product with antigens removed or reduced in the present invention may also be a processed product using as a raw material an egg from which the antigens of the present invention have been removed or reduced. When ordinary eggs are used as raw materials, the treatment for removing or reducing antigens of the present invention is performed before or after the preparation of the processed egg product. In the processed egg product using ordinary eggs as raw materials, methods for removing or reducing antigens of the present invention include: methods for removing protein components in food / ingredients by high pressure treatment and elution with neutral salt solutions, high temperature steam, etc.; methods for hydrolysis, denaturation, and amino acid denaturation (chemical modification / detachment of side chains, etc.) by heat treatment and acid treatment.

[0328] The bird from which the antigen is removed or reduced in the present invention can also be a bird hatched and grown from an egg from which the antigen is removed or reduced in the present invention. Birds include birds at various growth stages, including chicks, young birds, young birds, adult birds, and old birds. In this specification, a bird refers to an animal belonging to the avian species, preferably a chicken.

[0329] Method for producing antigen-removed egg processed product

[0330] The present invention is a method for producing an egg processed product with antigens removed or reduced, comprising the steps of: confirming that the antigens have been removed or reduced during the production process of the processed product;

[0331] Here, the antigen is at least one of the antigens described in (1) to (3) and (4) to (10).

[0332] In the production process of the antigen-removed or reduced egg processed product, the step of confirming the removal or reduction of antigens can be performed by confirming whether antigens are contained by the method described in the above item "Detector".

[0333] In addition, the production of egg processed products from which antigens have been removed or reduced can be carried out by the method described in the above-mentioned section "Antigen-removed foods, etc."

[0334] Example

[0335] Hereinafter, examples of the present invention will be described, but the technical scope of the present invention is not limited to these examples.

[0336] Example 1: Confirmation of protein profile

[0337] The proteins contained in the eggs were detected using the two-dimensional electrophoresis method described below.

[0338] Protein extraction

[0339] Separate raw eggs into egg whites and yolks.

[0340] The extraction and purification of proteins contained in egg white and egg yolk are performed as follows. After adding a solubilizing agent to the egg white to extract the protein, water or urea buffer is added to obtain a protein extract. The composition of the urea buffer is as follows.

[0341] 30mM Tris

[0342] 2M Thiourea

[0343] 7M Urea

[0344] 4% (w / v) CHAPS:

[0345] 3-[3-(Cholamidopropyl)dimethylamino]propanesulfonic acid inner salt

[0346] Appropriate amount of dilute hydrochloric acid

[0347] Distilled water was added to adjust the total volume to 100 mL and the pH to 8.5.

[0348] Then, 25 μg of each was mixed based on the weight of protein to obtain an extract. A surfactant buffer (Mammalian Lysis Buffer (MCLI), SIGMA) was added to the egg yolk as a solubilizing agent to extract the protein.

[0349] After that, two precipitation operations were performed using the 2D-CleanUP kit (manufactured by GE). In the first precipitation operation, TCA (trichloroacetic acid) was added to the recovered protein extract to precipitate, and the precipitate (TCA precipitate) produced by the operation was recovered. In the second precipitation operation, acetone was added to the recovered TCA precipitate to precipitate, and the precipitate (test sample) obtained by the operation was recovered.

[0350] Preparation of sample solution

[0351] A portion of the obtained sample (50 μg in terms of protein weight) was dissolved in 150 μl of DeStreak Rehydration Solution (GE), a swelling buffer for gel for first-dimensional isoelectric electrophoresis, to prepare a sample solution for first-dimensional isoelectric electrophoresis (swelling sample solution). The composition of DeStreak Rehydration Solution is as follows.

[0352] 7M Thiourea

[0353] 2M Urea

[0354] 4%(w / v)CHAPS

[0355] 0.5% (v / v) IPG buffer; manufactured by GE

[0356] Appropriate amount of BPB (bromophenol blue)

[0357] Penetration of the specimen into the first-dimension isoelectric electrophoresis gel

[0358] A gel for first-dimensional isoelectric electrophoresis (IPG gel Immobiline Drystrip (pH 3-10 NL, manufactured by GE) was immersed in 140 μl of the above-mentioned sample solution for first-dimensional isoelectric electrophoresis (sample solution for expansion) and allowed to permeate overnight at room temperature.

[0359] In this example, IPGphor manufactured by GE was used as the electrophoresis apparatus.

[0360] The swimming lane was filled with silicone oil. Filter papers moistened with water were placed at both ends of the gel soaked with the specimen, and the gel was placed in the swimming lane so that the gel was covered with silicone oil. Electrodes were placed between the gel and the filter paper.

[0361] The upper limit of the current value of the isoelectric point electrophoresis instrument is set to 75 μA per gel, and the voltage program is set as follows: (1) the constant voltage is increased from 300 V to 750 Vhr to perform a constant voltage process (the current change amplitude during the 30 minutes of electrophoresis before the end of this process is 5 μA); (2) the voltage is gradually increased from 300 Vhr to 1000 V; (3) further, the voltage is gradually increased from 4500 Vhr to 5000 V; (4) thereafter, the first dimension isoelectric point electrophoresis is performed at a constant voltage of 5000 V until Vhr reaches 12000.

[0362] SDS equilibration of isoelectric point electrophoresis gel

[0363] After the first-dimensional isoelectric electrophoresis, the gel was removed from the isoelectric electrophoresis apparatus and immersed in an equilibration buffer containing a reducing agent and shaken at room temperature for 15 minutes. The composition of the equilibration buffer containing a reducing agent is as follows.

[0364] 100 mM Tris-HCl (pH 8.0)

[0365] 6M urea

[0366] 30% (v / v) glycerol

[0367] 2%(w / v)SDS

[0368] 1%(w / v)DTT

[0369] Next, the equilibration buffer containing the reducing agent was removed, and the gel was immersed in an equilibration buffer containing an alkylating agent and shaken at room temperature for 15 minutes to obtain an SDS-equilibrated gel. The composition of the equilibration buffer containing an alkylating agent is as follows.

[0370] 100 mM Tris-HCl (pH 8.0)

[0371] 6M urea

[0372] 30% (v / v) glycerol

[0373] 2%(w / v)SDS

[0374] 2.5% (w / v) iodoacetamide

[0375] SDS-PAGE in the second dimension

[0376] In this example, the electrophoresis apparatus used was XCell SureLock Mini-Cell manufactured by Life Technologies, Inc. The second-dimensional electrophoresis gel used was NuPAGE 4-12% Bis-Tris Gels manufactured by Life Technologies, Inc. In addition, a running buffer having the following composition was prepared and used.

[0377] 50mM MOPS

[0378] 50mM Tris base

[0379] 0.1%(w / v)SDS

[0380] 1mM EDTA

[0381] In this example, an agarose solution for bonding was used in which 0.5% (w / v) agarose S (manufactured by Nippongene Co., Ltd.) and an appropriate amount of BPB (bromophenol blue) were dissolved in a running buffer.

[0382] After the wells of SDS-PAGE were fully cleaned with the above-mentioned electrophoresis buffer, the buffer used in the washing was removed. Then, a fully dissolved agarose solution was added to the wells for bonding. Then, the gel that had been subjected to SDS equilibration was immersed in agarose, and the gel that had been subjected to SDS equilibration was closely fitted with the second dimension electrophoresis gel using tweezers. Under the closely fitted state of the two gels, it was confirmed that agarose was fully solidified, and electrophoresis was performed for about 45 minutes with a constant voltage of 200V.

[0383] Fluorescent staining of gels

[0384] The gel was fluorescently stained using SYPRO Ruby (manufactured by Life Technologies).

[0385] First, the sealed container used was thoroughly cleaned with 98% (v / v) ethanol in advance. The following treatment was performed twice: the second-dimensional electrophoresis gel was removed from the SDS-PAGE instrument after electrophoresis, placed in a clean sealed container, and immersed in an aqueous solution containing 50% (v / v) methanol and 7% (v / v) acetic acid for 30 minutes. After that, the aqueous solution was replaced with water and immersed for 10 minutes. Next, the second-dimensional electrophoresis gel was immersed in 40 ml of SYPRO Ruby and shaken at room temperature overnight. Next, SYPRO Ruby was removed, the second-dimensional electrophoresis gel was washed with water, and then shaken with an aqueous solution containing 10% (v / v) methanol and 7% (v / v) acetic acid for 30 minutes. Furthermore, the aqueous solution was replaced with water and shaken for more than 30 minutes.

[0386] Analysis

[0387] The gel for the second-dimensional electrophoresis subjected to the above series of treatments was subjected to scanning of a fluorescent image using Typhoon 9400 (manufactured by GE). The results of the two-dimensional electrophoresis of the proteins contained in the egg yolk are shown in FIG. Figure 1 The results for proteins are not shown. Molecular weight marker bands are visible on the left side of the gel photograph, and the positions of the bands indicate specific molecular weights (KDa).

[0388] Example 2: Confirmation of antigen by immunoblotting (1)

[0389] Antigen confirmation by immunoblotting was performed by performing the steps described in Example 1 up to "second-dimensional SDS-PAGE" and then performing the following operations of "transfer to membrane", "immunoblotting" and "analysis".

[0390] Transfer to membrane

[0391] Transfer to the membrane was performed using the following transfer apparatus and transfer buffer.

[0392] Blotting device: XCell SureLock Mini-Cell and XCell II blot module (Lifetechnologies)

[0393] Transfer buffer: NuPAGE transfer buffer (×20) (manufactured by Life Technologies) was diluted 20-fold with milliQ water and used.

[0394] Specifically, the proteins in the two-dimensional electrophoresis gel were transferred to a membrane (PVDF membrane) according to the following procedure.

[0395] (1) The PVDF membrane was immersed in 100% methanol, then immersed in milliQ water, and then transferred to a transfer buffer to perform a hydrophilization treatment on the PVDF membrane.

[0396] (2) The sponge, filter paper, second-dimensional SDS-PAGE gel, hydrophilized PVDF membrane, filter paper, and sponge were placed in the order described above and energized at a constant voltage of 30 V for 1 hour in a transfer device.

[0397] Immunoblotting

[0398] The serum of a patient with egg allergy (patient 1) or the serum of a non-egg allergy subject was used as the first antibody for immunoblotting of the membrane. The patient with egg allergy was diagnosed with food-dependent exercise-induced allergy (FDEIA) caused by eggs. It should be noted that for this patient, in the puncture test, raw eggs, boiled eggs, and hot spring eggs were all negative; in the specific IgE antibody test, the egg white, egg yolk, and ovomucoid were negative.

[0399] Immunoblotting of membranes was performed as follows.

[0400] (1) The transferred membrane was shaken in a 5% skim milk / PBST solution (PBS buffer containing 0.1% nonionic surfactant Tween 20) at room temperature for 1 hour.

[0401] (2) As the primary antibody, the cells were incubated in a 5% serum / 5% skim milk / PBST solution at room temperature for 1 hour.

[0402] (3) Wash with PBST solution (5 minutes x 3 times).

[0403] (4) As a secondary antibody, anti-human IgE-HRP (horseweed peroxidase) was diluted 5000 times with a 5% skim milk / PBST solution and allowed to stand at room temperature for 1 hour.

[0404] (5) Wash with PBST solution (5 minutes x 3 times).

[0405] (6) The sample was allowed to stand in Pierce Western Blotting Substrate Plus (manufactured by Thermo Fisher Scientific) for 5 minutes.

[0406] Analysis

[0407] The membrane subjected to the above series of treatments was subjected to scanning of a fluorescent image using Typhoon 9500 (manufactured by GE).

[0408] The immunoblot using the serum of the patient with egg allergy was compared with the immunoblot using the serum of the non-egg allergy subject as a control. The protein contained in the raw egg yolk was immunoblotted using the serum of the patient with egg allergy ( Figure 2 ), unlike the case where the serum of a non-egg allergic subject was used, three spots different from the known egg allergen proteins were detected.

[0409] The molecular weights and isoelectric points of the above three spots are as follows: Figure 3 ).

[0410] Spot 1: molecular weight 20-40 kDa, pI 4.0-10.0

[0411] Spot 2: molecular weight 30-60 kDa, pI 5.0-10.0

[0412] Spot 3: molecular weight 35-60 kDa, pI 5.0-10.0

[0413] Example 3: Mass spectrometry analysis and identification of antigens (1)

[0414] The amino acid sequence of the antigen producing three spots in Example 2 was identified by mass spectrometry.

[0415] Specifically, protein extraction and mass spectrometry analysis were performed according to the following steps.

[0416] (1) Protein extraction, two-dimensional electrophoresis and membrane transfer were performed on raw egg yolks according to the procedures of Examples 1 and 2, and the yolks were stained with 0.008% direct blue / 40% ethanol / 10% acetic acid by shaking.

[0417] (2) Thereafter, the sample was treated with 40% ethanol / 10% acetic acid for 5 minutes three times for decolorization, washed with water for 5 minutes, and then air-dried.

[0418] (3) Cut the target spot with a clean cutter and add it to a centrifuge tube. After hydrophilizing the membrane with 50 μL of methanol, wash it twice with 100 μL of water and remove it by centrifugation. Then add 20 μL of 20 mM NH4HCO3·50% acetonitrile.

[0419] (4) Add 1 μL of 1 pmol / μL lysine-endo-peptidase (WAKO), let stand at 37°C for 60 minutes, and then recover the solution in a new centrifuge tube. Add 20 μL of 20 mM NH4HCO3·70% acetonitrile to the membrane, immerse it at room temperature for 10 minutes, and then recover it. Dissolve it with 10 μL of 0.1% formic acid and 4% acetonitrile, and transfer it to a test tube.

[0420] (5) The recovered solution was dried under reduced pressure, dissolved in 15 μl of solution A (0.1% formic acid, 4% acetonitrile solution), and subjected to mass spectrometry analysis (ESI-TOF6600, manufactured by AB Sciex).

[0421] (6) Protein identification based on mass spectrometry data obtained by a mass spectrometer was performed by searching NCBI or UniProt.

[0422] result

[0423] As a result of mass spectrometry analysis of each spot, the following amino acid sequences were detected.

[0424] Spot 1: Amino acid sequence shown in SEQ ID NOs: 3 to 11

[0425] Spot 2: amino acid sequence shown in SEQ ID NOs: 9 to 11, 14, and 16

[0426] Spot 3: Amino acid sequence shown in SEQ ID NOs: 19 to 45

[0427] Furthermore, for each spot, the mass spectrum data obtained by the mass spectrometer were analyzed using NCBI for spot 1 and spot 2, and the mass spectrum data obtained by the mass spectrometer were analyzed using UniProt for spot 3. As a result, each spot was identified as the following protein.

[0428] Spot 1: C-terminal portion of vitellogenin-3 (amino acid sequence: NCBI accession number XP_015146355, base sequence encoding it: GenBank accession number XM_015290869.1) (amino acid sequence: sequence number 2, base sequence encoding it: sequence number 1)

[0429] Spot 2: C-terminal portion of vitellogenin-3 (amino acid sequence: NCBI accession number XP_015146355, base sequence encoding it: GenBank accession number XM_015290869.1) (amino acid sequence: sequence number 13, base sequence encoding it: sequence number 12)

[0430] Spot 3: The central part of vitellogenin-1 (amino acid sequence: UniProt accession number P87498, base sequence encoding it: ENA (EMBL) accession number D89547.1), or the C-terminal part of lipovitellin-1 (amino acid sequence: sequence number 18, base sequence encoding it: sequence number 17)

[0431] Example 4: Confirmation of antigen by immunoblotting (2)

[0432] Similar to Example 2, antigen confirmation was performed by immunoblotting using sera from three other egg allergy patients (patient 2, patient 3, and patient 4). For proteins contained in raw egg yolk, immunoblotting using sera from egg allergy patients (patient 2 was Figure 4 For patient 3, Figure 5 For patient 4, Figure 6 ), unlike the case where the serum of a non-egg allergic subject was used, spots different from the known egg allergen protein were detected. Specifically, spots 4 to 8 were detected for patient 2, spots 9 and 10 were detected for patient 3, and spot 11 was detected for patient 4.

[0433] The molecular weights and isoelectric points of the above spots 4 to 11 are as follows: Figures 4 to 6 ).

[0434] Spot 4: molecular weight 20-50 kDa, pI 3.0-8.0

[0435] Spots 5 and 6: molecular weight 80-260 kDa, pI 1.0-8.0

[0436] Spot 7: molecular weight 110-300 kDa, pI 3.0-8.0

[0437] Spot 8: molecular weight 160-550 kDa, pI 3.0-8.0

[0438] Spot 9: molecular weight 20-50 kDa, pI 7.0-11.0

[0439] Spot 10: molecular weight 20-50 kDa, pI 7.0-11.0

[0440] Spot 11: molecular weight 15-40 kDa, pI 6.0-11.0

[0441] Example 5: Mass spectrometry analysis and identification of antigens (2)

[0442] In the same manner as in Example 3, the amino acid sequences of the antigens producing spots 4 to 11 in Example 4 were identified by mass spectrometry.

[0443] As a result of mass spectrometry analysis of each spot, the following amino acid sequences were detected.

[0444] Spot 4: amino acid sequence shown in SEQ ID NOs: 48 to 57

[0445] Spots 5 and 6: Amino acid sequences shown in SEQ ID NOs: 60 to 104

[0446] Spot 7: amino acid sequence shown in SEQ ID NOs: 107 to 150

[0447] Spot 8: Amino acid sequence shown in SEQ ID NOs: 153 to 235

[0448] Spot 9: amino acid sequence shown in SEQ ID NOs: 238 to 249

[0449] Spot 10: amino acid sequence shown in SEQ ID NOs: 252 to 260

[0450] Spot 11: Amino acid sequence shown in SEQ ID NOs: 263 to 271

[0451] Furthermore, as a result of analyzing the mass spectrum data obtained by the mass spectrometer for each spot using NCBI, each spot was identified as the following protein.

[0452] Spot 4: Vitellogenin-3 (amino acid sequence: NCBI accession number XP_015146355, base sequence encoding it: GenBank accession number XM_015290869.1) (amino acid sequence: sequence number 47, base sequence encoding it: sequence number 46)

[0453] Spots 5 and 6: Vitellogenin-2 precursor (amino acid sequence: NCBI accession number NP_001026447.1, base sequence encoding it: GenBank accession number NM_001031276.1) (amino acid sequence: sequence number 59, base sequence encoding it: sequence number 58)

[0454] Spot 7: Vitellogenin-2 precursor (amino acid sequence: NCBI accession number NP_001026447.1, base sequence encoding it: GenBank accession number NM_001031276.1) (amino acid sequence: sequence number 106, base sequence encoding it: sequence number 105)

[0455] Spot 8: Apolipoprotein B precursor (amino acid sequence: NCBI accession number NP_001038098.1, base sequence encoding it: GenBank accession number NM_001044633.1) (amino acid sequence: sequence number 152, base sequence encoding it: sequence number 151)

[0456] Spot 9: Apolipoprotein B precursor (amino acid sequence: NCBI accession number NP_001038098.1, base sequence encoding it: GenBank accession number NM_001044633.1) (amino acid sequence: sequence number 237, base sequence encoding it: sequence number 236)

[0457] Spot 10: Apolipoprotein B precursor (amino acid sequence: NCBI accession number NP_001038098.1, base sequence encoding it: GenBank accession number NM_001044633.1) (amino acid sequence: sequence number 251, base sequence encoding it: sequence number 250)

[0458] Spot 11: Vitellogenin-2 precursor (amino acid sequence: NCBI accession number NP_001026447.1, base sequence encoding it: GenBank accession number NM_001031276.1) (amino acid sequence: sequence number 262, base sequence encoding it: sequence number 261)

[0459] Industrial Applicability

[0460] The present invention provides a novel antigen for egg allergy, a method for diagnosing egg allergy and a diagnostic kit, a pharmaceutical composition containing the antigen, an egg or egg processed product with the antigen removed or reduced, or a bird producing the egg or hatched from the egg, and a method for producing an egg processed product with the antigen removed or reduced. The present invention can also provide a detector for determining whether an object has an egg antigen. Sequence Listing <110> Hoyu Co., Ltd. <120> Egg allergic antigen <130> 2073-1857212D1 <150> JP2016-111308 <151> 2016-06-02 <160> 271 <170> PatentIn version 3.5 <210> 1 <211> 831 <212> DNA <213> Chicken (Gallus gallus) <400> 1 tcaatcattg aaaaccttaa agctcgttgt tcagtttcac aaaatatgat aacaaccttc 60 aatggagttg agtttaacta ttcaatgcct gcaaattgct accacatctt ggcacaggat 120 tgtagtccag aactgaagtt cctggtaatg atgaaaagac ttggagaatc tgctgatctc 180 acagcaataa gtgtcagact tgccagccat gaggttgaca tgtatgtttc caatggacta 240 atccagctga agattaatgg tgttcaaacc ccaacagacg ttccataacac atctaagtct 300 ggtctgctga taagcagtga gaaggaaggt ttgtcattaa aagcccctga atatggtgta 360 gaaaaactat attacgatag acgtaaactt gagattcggg ttgctttctg gatggttgga 420 aaaacatgtg gtatttgtgg aaaatatgat gctgagaaga aaagggagta tcaaatgccc 480 agtggatatt tagctaaaga tgcagtgagt tttgctcagt cctgggtcat ctcagaagac 540 acgtgtactg gagcttgcaa gctgcagagg aaatttgtca aaattgagaa gccggttgca 600 tttaacaaaa aggcctcaaa atgcttttcc attgagccag ttttacgctg tgcagaaggc 660 tgttcagcaa ccaggactgt tcctgtctct gtgggtttcc actgtgtccc atctgactcc 720 acactcgagc tggaggaaga gcaggtgagg ttagaccaga agtctgagga cttggtgagc 780 agggtcgatg cccatacggc gtgttcctgc gcccagcagc tgtgctcagc g 831 <210> 2 <211> 277 <212> PRT <213> Chicken (Gallus gallus) <400> 2 Ser Ile Ile Glu Asn Leu Lys Ala Arg Cys Ser Val Ser Gln Asn Met 1 5 10 15 Ile Thr Thr Phe Asn Gly Val Glu Phe Asn Tyr Ser Met Pro Ala Asn 20 25 30 Cys Tyr His Ile Leu Ala Gln Asp Cys Ser Pro Glu Leu Lys Phe Leu 35 40 45 Val Met Met Lys Arg Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile Ser 50 55 60 Val Arg Leu Ala Ser His Glu Val Asp Met Tyr Val Ser Asn Gly Leu 65 70 75 80 Ile Gln Leu Lys Ile Asn Gly Val Gln Thr Pro Thr Asp Val Pro Tyr 85 90 95 Thr Ser Lys Ser Gly Leu Leu Ile Ser Ser Glu Lys Glu Gly Leu Ser 100 105 110 Leu Lys Ala Pro Glu Tyr Gly Val Glu Lys Leu Tyr Tyr Asp Arg Arg 115 120 125 Lys Leu Glu Ile Arg Val Ala Phe Trp Met Val Gly Lys Thr Cys Gly 130 135 140 Ile Cys Gly Lys Tyr Asp Ala Glu Lys Lys Arg Glu Tyr Gln Met Pro 145 150 155 160 Ser Gly Tyr Leu Ala Lys Asp Ala Val Ser Phe Ala Gln Ser Trp Val 165 170 175 Ile Ser Glu Asp Thr Cys Thr Gly Ala Cys Lys Leu Gln Arg Lys Phe 180 185 190 Val Lys Ile Glu Lys Pro Val Ala Phe Asn Lys Lys Ala Ser Lys Cys 195 200 205 Phe Ser Ile Glu Pro Val Leu Arg Cys Ala Glu Gly Cys Ser Ala Thr 210 215 220 Arg Thr Val Pro Val Ser Val Gly Phe His Cys Val Pro Ser Asp Ser 225 230 235 240 Thr Leu Glu Leu Glu Glu Glu Gln Val Arg Leu Asp Gln Lys Ser Glu 245 250 255 Asp Leu Val Ser Arg Val Asp Ala His Thr Ala Cys Ser Cys Ala Gln 260 265 270 Gln Leu Cys Ser Ala 275 <210> 3 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 3 Ala Pro Glu Tyr Gly Val Glu Lys 1 5 <210> 4 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 4 Gly Val Gln Thr Pro Thr Asp Val Pro Tyr Thr Ser Lys 1 5 10 <210> 5 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 5 Ile Glu Lys Pro Val Ala Phe Asn 1 5 <210> 6 <211> 5 <212> PRT <213> Chicken (Gallus gallus) <400> 6 Pro Val Ala Phe Asn 1 5 <210> 7 <211> 6 <212> PRT <213> Chicken (Gallus gallus) <400> 7 Ser Ile Ile Glu Asn Leu 1 5 <210> 8 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 8 Ile Glu Lys Pro Val Ala Phe Asn Lys 1 5 <210> 9 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 9 Ile Asn Gly Val Gln Thr Pro Thr Asp Val Pro Tyr Thr Ser Lys 1 5 10 15 <210> 10 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 10 Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile Ser Val Arg 1 5 10 <210> 11 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 11 Arg Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile Ser Val Arg 1 5 10 <210> 12 <211> 1314 <212> DNA <213> Chicken (Gallus gallus) <400> 12 gtgcaggtgt ttgtttcaag catcacagaa tcagataggt ggaaactctg tgctgatgct 60 tcagtagtaa attcccataa agcatcgggt acccttaaat ggggtaaaga ttgccaggac 120 tatcaggttg ctactcagat tgcaacaggg caatttgctg cacacccggc tatacaggtg 180 aagctggagt ggtcagaagt gccttcaagt gtccgaaaaa ctgccagatg gttctacaca 240 tatcttccag gagctgcgta tatgcttggc tactcccaga agcagcagcg tggtccttct 300 caccaggcag ccatggtgat ggctctgacg tctccaagaa cctgcgatgt ggtcctgaag 360 ctacctgagc tcacagttta caacagagcc atcaggcttc ccctgccact cccttcaagt 420 tcagatacac caacctcaac actaccatcc tccaaatgga acgtctttta ccaagcagcc 480 ttttcaatca ttgaaaacct taaagctcgt tgttcagttt cacaaaatat gataacaacc 540 ttcaatggag ttgagtttaa ctattcaatg cctgcaaatt gctaccacat cttggcacag 600 gattgtagtc cagaactgaa gttcctggta atgatgaaaa gacttggaga atctgctgat 660 ctcacagcaa taagtgtcag acttgccagc catgaggttg acatgtatgt ttccaatgga 720 ctaatccagc tgaagattaa tggtgttcaa accccaacag acgttccata cacatctaag 780 tctggtctgc tgataagcag tgagaaggaa ggtttgtcat taaaagcccc tgaatatggt 840 gtagaaaaac tatattacga tagacgtaaa cttgagattc gggttgcttt ctggatggtt 900 ggaaaaacat gtggtatttg tggaaaatat gatgctgaga agaaaaggga gtatcaaatg 960 cccagtggat atttagctaa agatgcagtg agttttgctc agtcctgggt catctcagaa 1020 gacacgtgta ctggagcttg caagctgcag aggaaatttg tcaaaattga gaagccggtt 1080 gcatttaaca aaaaggcctc aaaatgcttt tccattgagc cagttttacg ctgtgcagaa 1140 ggctgttcag caaccaggac tgttcctgtc tctgtgggtt tccactgtgt cccatctgac 1200 tccacactcg agctggagga agagcaggtg aggttagacc agaagtctga ggacttggtg 1260 agcagggtcg atgcccatac ggcgtgttcc tgcgcccagc agctgtgctc agcg 1314 <210> 13 <211> 438 <212> PRT <213> Chicken (Gallus gallus) <400> 13 Val Gln Val Phe Val Ser Ser Ile Thr Glu Ser Asp Arg Trp Lys Leu 1 5 10 15 Cys Ala Asp Ala Ser Val Val Asn Ser His Lys Ala Ser Gly Thr Leu 20 25 30 Lys Trp Gly Lys Asp Cys Gln Asp Tyr Gln Val Ala Thr Gln Ile Ala 35 40 45 Thr Gly Gln Phe Ala Ala His Pro Ala Ile Gln Val Lys Leu Glu Trp 50 55 60 Ser Glu Val Pro Ser Ser Val Arg Lys Thr Ala Arg Trp Phe Tyr Thr 65 70 75 80 Tyr Leu Pro Gly Ala Ala Tyr Met Leu Gly Tyr Ser Gln Lys Gln Gln 85 90 95 Arg Gly Pro Ser His Gln Ala Ala Met Val Met Ala Leu Thr Ser Pro 100 105 110 Arg Thr Cys Asp Val Val Leu Lys Leu Pro Glu Leu Thr Val Tyr Asn 115 120 125 Arg Ala Ile Arg Leu Pro Leu Pro Leu Pro Ser Ser Ser Asp Thr Pro 130 135 140 Thr Ser Thr Leu Pro Ser Ser Lys Trp Asn Val Phe Tyr Gln Ala Ala 145 150 155 160 Phe Ser Ile Ile Glu Asn Leu Lys Ala Arg Cys Ser Val Ser Gln Asn 165 170 175 Met Ile Thr Thr Phe Asn Gly Val Glu Phe Asn Tyr Ser Met Pro Ala 180 185 190 Asn Cys Tyr His Ile Leu Ala Gln Asp Cys Ser Pro Glu Leu Lys Phe 195 200 205 Leu Val Met Met Lys Arg Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile 210 215 220 Ser Val Arg Leu Ala Ser His Glu Val Asp Met Tyr Val Ser Asn Gly 225 230 235 240 Leu Ile Gln Leu Lys Ile Asn Gly Val Gln Thr Pro Thr Asp Val Pro 245 250 255 Tyr Thr Ser Lys Ser Gly Leu Leu Ile Ser Ser Glu Lys Glu Gly Leu 260 265 270 Ser Leu Lys Ala Pro Glu Tyr Gly Val Glu Lys Leu Tyr Tyr Asp Arg 275 280 285 Arg Lys Leu Glu Ile Arg Val Ala Phe Trp Met Val Gly Lys Thr Cys 290 295 300 Gly Ile Cys Gly Lys Tyr Asp Ala Glu Lys Lys Arg Glu Tyr Gln Met 305 310 315 320 Pro Ser Gly Tyr Leu Ala Lys Asp Ala Val Ser Phe Ala Gln Ser Trp 325 330 335 Val Ile Ser Glu Asp Thr Cys Thr Gly Ala Cys Lys Leu Gln Arg Lys 340 345 350 Phe Val Lys Ile Glu Lys Pro Val Ala Phe Asn Lys Lys Ala Ser Lys 355 360 365 Cys Phe Ser Ile Glu Pro Val Leu Arg Cys Ala Glu Gly Cys Ser Ala 370 375 380 Thr Arg Thr Val Pro Val Ser Val Gly Phe His Cys Val Pro Ser Asp 385 390 395 400 Ser Thr Leu Glu Leu Glu Glu Glu Gln Val Arg Leu Asp Gln Lys Ser 405 410 415 Glu Asp Leu Val Ser Arg Val Asp Ala His Thr Ala Cys Ser Cys Ala 420 425 430 Gln Gln Leu Cys Ser Ala 435 <210> 14 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 14 Leu Pro Glu Leu Thr Val Tyr Asn Arg 1 5 <210> 15 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 15 Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile Ser Val Arg 1 5 10 <210> 16 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 16 Val Gln Val Phe Val Ser Ser Ile Thr Glu Ser Asp Arg 1 5 10 <210> 17 <211> 996 <212> DNA <213> Chicken (Gallus gallus) <400> 17 gacaaacctt ttgcatcagg ttacttgaag atgtttggcc aggagttgct ctttggtaga 60 ctcgataaag acaccctcca aaatgtattg caggtatggt atggacctga tgaaaaaatc 120 ccttcaataa ggagattaat cagtagcctt caaactggca taggaagaca atggactaag 180 gctttactat tgtctgagat tcgttgtatt gtgcctacct gtgttgggtt cccgatggag 240 accagcttct attactcttc tgtcacaaaa gtggcaggaa acgttcaagc gcaaattaca 300 ccttcaccga ggtctgattt cagattgact gagttactaa attccaacgt taggctgcga 360 tccaaaatga gtctaagcat ggctaaacat atgacctttg taattgggat caacacaaac 420 atgatccagg cagggctgga agcacacacc aaagtaaatg ctcatgtacc tgtgaatgtt 480 gttgccacta ttcaaatgaa ggaaaaaagt atcaaagctg aaattccacc atgcaaagaa 540 gagactaact taattattgt aagctctaag acatttgctg ttacacgaaa tattgaagat 600 ttggctgcta gtaagatgac tccagttctt ctacctgaag cagtgcctga cataatgaag 660 atgtccttcg actcagattc tgcatcaggc gagactgata acatcaggga cagacagtct 720 gtagaagatg ttcgtctgg aaattccttc tcctttggac atccttcttc cgggaaggag 780 ccatttattc agtccatgtg ctccaacgca agtacatttg gggttcaagt gtgcattgag 840 aagaaaagtg tacatgcagc attcatcaga aatgtgcctc tttataacgc tattggagaa 900 catgccctta gaatgagctt caagccagtc tactcagatg tacctattga aaaaatacaa 960 gtcacaattc aagcaggaga tcaagctcct acaaaa 996 <210> 18 <211> 332 <212> PRT <213> Chicken (Gallus gallus) <400> 18 Asp Lys Pro Phe Ala Ser Gly Tyr Leu Lys Met Phe Gly Gln Glu Leu 1 5 10 15 Leu Phe Gly Arg Leu Asp Lys Asp Thr Leu Gln Asn Val Leu Gln Val 20 25 30 Trp Tyr Gly Pro Asp Glu Lys Ile Pro Ser Ile Arg Arg Leu Ile Ser 35 40 45 Ser Leu Gln Thr Gly Ile Gly Arg Gln Trp Thr Lys Ala Leu Leu Leu 50 55 60 Ser Glu Ile Arg Cys Ile Val Pro Thr Cys Val Gly Phe Pro Met Glu 65 70 75 80 Thr Ser Phe Tyr Tyr Ser Ser Val Thr Lys Val Ala Gly Asn Val Gln 85 90 95 Ala Gln Ile Thr Pro Ser Pro Arg Ser Asp Phe Arg Leu Thr Glu Leu 100 105 110 Leu Asn Ser Asn Val Arg Leu Arg Ser Lys Met Ser Leu Ser Met Ala 115 120 125 Lys His Met Thr Phe Val Ile Gly Ile Asn Thr Asn Met Ile Gln Ala 130 135 140 Gly Leu Glu Ala His Thr Lys Val Asn Ala His Val Pro Val Asn Val 145 150 155 160 Val Ala Thr Ile Gln Met Lys Glu Lys Ser Ile Lys Ala Glu Ile Pro 165 170 175 Pro Cys Lys Glu Glu Thr Asn Leu Ile Ile Val Ser Ser Lys Thr Phe 180 185 190 Ala Val Thr Arg Asn Ile Glu Asp Leu Ala Ala Ser Lys Met Thr Pro 195 200 205 Val Leu Leu Pro Glu Ala Val Pro Asp Ile Met Lys Met Ser Phe Asp 210 215 220 Ser Asp Ser Ala Ser Gly Glu Thr Asp Asn Ile Arg Asp Arg Gln Ser 225 230 235 240 Val Glu Asp Val Ser Ser Gly Asn Ser Phe Ser Phe Gly His Pro Ser 245 250 255 Ser Gly Lys Glu Pro Phe Ile Gln Ser Met Cys Ser Asn Ala Ser Thr 260 265 270 Phe Gly Val Gln Val Cys Ile Glu Lys Lys Ser Val His Ala Ala Phe 275 280 285 Ile Arg Asn Val Pro Leu Tyr Asn Ala Ile Gly Glu His Ala Leu Arg 290 295 300 Met Ser Phe Lys Pro Val Tyr Ser Asp Val Pro Ile Glu Lys Ile Gln 305 310 315 320 Val Thr Ile Gln Ala Gly Asp Gln Ala Pro Thr Lys 325 330 <210> 19 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 19 Ala Gly Asn Val Gln Ala Gln Ile Thr Pro Ser Pro Arg 1 5 10 <210> 20 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 20 Ala Leu Leu Leu Ser Glu Ile Arg 1 5 <210> 21 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 21 Asp Lys Pro Phe Ala Ser Gly Tyr 1 5 <210> 22 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 22 Asp Lys Pro Phe Ala Ser Gly Tyr Leu Lys 1 5 10 <210> 23 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 23 Asp Thr Leu Gln Asn Val Leu Gln Val Trp Tyr Gly Pro Asp Glu Lys 1 5 10 15 <210> 24 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 24 Glu Glu Thr Asn Leu Ile Ile Val Ser Ser Lys 1 5 10 <210> 25 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 25 Gly Asn Val Gln Ala Gln Ile Thr Pro Ser Pro Arg 1 5 10 <210> 26 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 26 Ile Gln Ala Gly Asp Gln Ala Pro Thr Lys 1 5 10 <210> 27 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 27 Ile Gln Val Thr Ile Gln Ala Gly Asp Gln Ala Pro Thr 1 5 10 <210> 28 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 28 Ile Gln Val Thr Ile Gln Ala Gly Asp Gln Ala Pro Thr Lys 1 5 10 <210> 29 <211> 20 <212> PRT <213> Chicken (Gallus gallus) <400> 29 Ile Thr Pro Ser Pro Arg Ser Asp Phe Arg Leu Thr Glu Leu Leu Asn 1 5 10 15 Ser Asn Val Arg 20 <210> 30 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 30 Lys Glu Glu Thr Asn Leu Ile Ile Val Ser Ser Lys 1 5 10 <210> 31 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 31 Lys Pro Val Tyr Ser Asp Val Pro Ile Glu Lys 1 5 10 <210> 32 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 32 Leu Asp Lys Asp Thr Leu Gln Asn 1 5 <210> 33 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 33 Leu Asp Lys Asp Thr Leu Gln Asn Val Leu Gln 1 5 10 <210> 34 <211> 19 <212> PRT <213> Chicken (Gallus gallus) <400> 34 Leu Asp Lys Asp Thr Leu Gln Asn Val Leu Gln Val Trp Tyr Gly Pro 1 5 10 15 Asp Glu Lys <210> 35 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 35 Leu Ile Ser Ser Leu Gln Thr Gly Ile Gly Arg 1 5 10 <210> 36 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 36 Leu Thr Glu Leu Leu Asn Ser Asn 1 5 <210> 37 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 37 Leu Thr Glu Leu Leu Asn Ser Asn Val Arg 1 5 10 <210> 38 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 38 Asn Ile Glu Asp Leu Ala Ala Ser Lys 1 5 <210> 39 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 39 Asn Val Pro Leu Tyr Asn Ala Ile Gly Glu His Ala Leu Arg 1 5 10 <210> 40 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 40 Asn Val Gln Ala Gln Ile Thr Pro Ser Pro Arg 1 5 10 <210> 41 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 41 Pro Ser Ser Gly Lys Glu Pro Phe 1 5 <210> 42 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 42 Pro Val Tyr Ser Asp Val Pro Ile Glu Lys 1 5 10 <210> 43 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 43 Arg Leu Ile Ser Ser Leu Gln Thr Gly Ile Gly Arg 1 5 10 <210> 44 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 44 Ser Val His Ala Ala Phe Ile Arg 1 5 <210> 45 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 45 Val Gln Ala Gln Ile Thr Pro Ser Pro Arg 1 5 10 <210> 46 <211> 1023 <212> DNA <213> Chicken (Gallus gallus) <400> 46 ggtccttctc accaggcagc catggtgatg gctctgacgt ctccaagaac ctgcgatgtg 60 gtcctgaagc tacctgagct cacagtttac aacagagcca tcaggcttcc cctgccactc 120 ccttcaagtt cagatacacc aacctcaaca ctaccatcct ccaaatggaa cgtcttttac 180 caagcagcct tttcaatcat tgaaaacctt aaagctcgtt gttcagtttc acaaaatatg 240 ataacaacct tcaatggagt tgagtttaac tattcaatgc ctgcaaattg ctaccacatc 300 ttggcacagg attgtagtcc agaactgaag ttcctggtaa tgatgaaaag acttggagaa 360 tctgctgatc tcacagcaat aagtgtcaga cttgccagcc atgaggttga catgtatgtt 420 tccaatggac taatccagct gaagattaat ggtgttcaaa ccccaacaga cgttccatac 480 acatctaagt ctggtctgct gataagcagt gagaaggaag gtttgtcatt aaaagcccct 540 gaatatggtg tagaaaaact atattacgat agacgtaaac ttgagattcg ggttgctttc 600 tggatggttg gaaaaacatg tggtatttgt ggaaaatatg atgctgagaa gaaaagggag 660 tatcaaatgc ccagtggata tttagctaaa gatgcagtga gttttgctca gtcctgggtc 720 atctcagaag acacgtgtac tggagcttgc aagctgcaga ggaaatttgt caaaattgag 780 aagccggttg catttaacaa aaaggcctca aaatgctttt ccattgagcc agttttacgc 840 tgtgcagaag gctgttcagc aaccaggact gttcctgtct ctgtgggttt ccactgtgtc 900 ccatctgact ccacactcga gctggaggaa gagcaggtga ggttagacca gaagtctgag 960 gacttggtga gcagggtcga tgcccatacg gcgtgttcct gcgcccagca gctgtgctca 1020 gcg 1023 <210> 47 <211> 341 <212> PRT <213> Chicken (Gallus gallus) <400> 47 Gly Pro Ser His Gln Ala Ala Met Val Met Ala Leu Thr Ser Pro Arg 1 5 10 15 Thr Cys Asp Val Val Leu Lys Leu Pro Glu Leu Thr Val Tyr Asn Arg 20 25 30 Ala Ile Arg Leu Pro Leu Pro Leu Pro Ser Ser Ser Asp Thr Pro Thr 35 40 45 Ser Thr Leu Pro Ser Ser Lys Trp Asn Val Phe Tyr Gln Ala Ala Phe 50 55 60 Ser Ile Ile Glu Asn Leu Lys Ala Arg Cys Ser Val Ser Gln Asn Met 65 70 75 80 Ile Thr Thr Phe Asn Gly Val Glu Phe Asn Tyr Ser Met Pro Ala Asn 85 90 95 Cys Tyr His Ile Leu Ala Gln Asp Cys Ser Pro Glu Leu Lys Phe Leu 100 105 110 Val Met Met Lys Arg Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile Ser 115 120 125 Val Arg Leu Ala Ser His Glu Val Asp Met Tyr Val Ser Asn Gly Leu 130 135 140 Ile Gln Leu Lys Ile Asn Gly Val Gln Thr Pro Thr Asp Val Pro Tyr 145 150 155 160 Thr Ser Lys Ser Gly Leu Leu Ile Ser Ser Glu Lys Glu Gly Leu Ser 165 170 175 Leu Lys Ala Pro Glu Tyr Gly Val Glu Lys Leu Tyr Tyr Asp Arg Arg 180 185 190 Lys Leu Glu Ile Arg Val Ala Phe Trp Met Val Gly Lys Thr Cys Gly 195 200 205 Ile Cys Gly Lys Tyr Asp Ala Glu Lys Lys Arg Glu Tyr Gln Met Pro 210 215 220 Ser Gly Tyr Leu Ala Lys Asp Ala Val Ser Phe Ala Gln Ser Trp Val 225 230 235 240 Ile Ser Glu Asp Thr Cys Thr Gly Ala Cys Lys Leu Gln Arg Lys Phe 245 250 255 Val Lys Ile Glu Lys Pro Val Ala Phe Asn Lys Lys Ala Ser Lys Cys 260 265 270 Phe Ser Ile Glu Pro Val Leu Arg Cys Ala Glu Gly Cys Ser Ala Thr 275 280 285 Arg Thr Val Pro Val Ser Val Gly Phe His Cys Val Pro Ser Asp Ser 290 295 300 Thr Leu Glu Leu Glu Glu Glu Gln Val Arg Leu Asp Gln Lys Ser Glu 305 310 315 320 Asp Leu Val Ser Arg Val Asp Ala His Thr Ala Cys Ser Cys Ala Gln 325 330 335 Gln Leu Cys Ser Ala 340 <210> 48 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 48 Ala Pro Glu Tyr Gly Val Glu Lys 1 5 <210> 49 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 49 Ile Glu Lys Pro Val Ala Phe 1 5 <210> 50 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 50 Ile Asn Gly Val Gln Thr Pro Thr Asp Val Pro Tyr Thr Ser Lys 1 5 10 15 <210> 51 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 51 Leu Gly Glu Ser Ala Asp Leu Thr Ala Ile Ser Val Arg 1 5 10 <210> 52 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 52 Leu Pro Glu Leu Thr Val Tyr Asn Arg 1 5 <210> 53 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 53 Leu Pro Leu Pro Leu Pro Ser Ser Ser Asp Thr Pro Thr Ser Thr Leu 1 5 10 15 <210> 54 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 54 Pro Ser Asp Ser Thr Leu Glu Leu Glu Glu Glu Gln 1 5 10 <210> 55 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 55 Ser Gly Leu Leu Ile Ser Ser Glu Lys 1 5 <210> 56 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 56 Ser Ile Glu Pro Val Leu Arg 1 5 <210> 57 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 57 Thr Val Pro Val Ser Val Gly Phe His 1 5 <210> 58 <211> 3363 <212> DNA <213> Chicken (Gallus gallus) <400> 58 atgaggggga tcatactggc attagtgctc acccttgtag gcagccagaa gtttgacatt 60 gacccaggat tcaatagcag aaggagttac ctgtacaact atgaaggttc tatgttgaat 120 gggcttcaag acagaagttt gggcaagct ggtgtgcgct tgagcagca gctagagatc 180 agtgggctac cagagaatgc ttaccctc aaggtccgct ctccacagt ggaggagtac 240 aatggggtct ggcccaggga tcctcact cgatcttcca aaatcaccca agtgatctca 300 tcgtgtttca cccggctctt caatttgaa tacagcagtg gacggatcgg aacatttat 360 gccccagaag actcccaga tctgtgtgtt aacatagtga gaggaatatt gaacatgttc 420 cagatgacca ttaaaaaatc acagaacgtc tacgaattac aagaggctgg aattggaggt 480 atttgtcatg caagtatgt cattcaggaa gagaga atagccgaat ctatgttacc 540 agaactgtgg acttgaataa ttgccaggaa aaggtgcaaa aaagcattgg aatggcttac 600 atctatccct gccctgtgga cgtgatgaaa gaaaggctca ccaagggac caccgctttc 660 tcctacaagc tgaagcagtc agacagcggc acgctgatca cagatgtctc gtcgcggcag 720 gtgtatcaga tctccccatt caatgagccc actggggtgg ctgtcatgga agcagacag 780 cagctcactt tggtcgaggt gagaagtgag cggggcagtg ccccagatgt cccatgcag 840 aactatggca gccttcgcta ccgcttccca gccgtactgc cacagatgcc acttcagctg 900 atcaagacaa aaaaccctga gcaacggata gtagaaacgc tgcagcacat agtcctgaat 960 aaccaacaag atttccatga cgatgtttca tacagattct tagaggtggt ccagctttgc 1020 cggatagcaa atgctgacaa tcttgagtct atctggagac aagtttcaga taaacctcgt 1080 tacaggcgat ggctcctgag cgcagtttct gcgagtggca ccacagaaac actaaaattc 1140 cttaagaaca gaattcgcaa tgatgacctc aactacattc agacccttct aactgtttct 1200 ttgactcttc atttattgca agctgatgaa cacacacttc caatagcagc agatttaatg 1260 accagctctc gaattcagaa aaatcctgtg cttcagcaag tggcctgctt gggatatagc 1320 tctgtagtca acagatactg ctctcagacc tcagcatgtc ctaaggaagc tcttcagccc 1380 atccatgacc tggcagatga agcaatcagc aggggccgtg aagacaaaat gaaattagct 1440 ctaaagtgca ttggtaacat gggagaacca gccagcttaa agcgcatcct gaagttcctt 1500 ccaatatctt catccagtgc tgctgatatc ccagtccaca ttcagataga tgccataacg 1560 gccttgaaaa agatagcttg gaaggacccc aaaacagtgc agggctatct catccagatc 1620 cttgcagacc aatcacttcc ccctgaggtg cgaatgatgg cttgtgctgt tatctttgag 1680 acaagcctg cccttgcttt gatacgact atagctaacg tggcaatgaa ggagagcaat 1740 atgcaagtgg ccagttttgt atattcccac atgaagtctt tgtcaagg cagattgcca 1800 tttatgtaca acatactctc cgcttgtaac attgcctta agctccctgtc cccaactg 1860 gagtatga gctatcggta cagcaggtc attcgagcag acacttactt tgataactat 1920 agagttggtg ctactggaga aatctttgtt gtgaacagcc CAagaactat gttcccatca 1980 gcaataattt ccaaattgat ggcaattct gcaggttcag tggctgat ggtagaggtt 2040 ggcatccgag tggaggcct cgcagatgtc ataatgaaaa gaaacatccc atttgctgaa 2100 tatcccacat aaaggagctt ggaaaagctc tgcagggatg gaaagagctg 2160 ccgacagaaa cccctttggt atcagcctac ttgaaaatac ttggccaaga agtggccttc 2220 atcacatca aaaggaact cctgcaacag gtcatgaaga ctgtagtgga acctgctgat 2280 cgaaacgcag caataaagag aatcgccaac cagatccgca acagcattgc agggcagtgg 2340 acgcagccgg tgtggatggg agagctgcga tacgtggttc ccagctgtct cggcctgccg 2400 ctggagtacg ggtcctacac caccgccctg gcacgagctg cagtcagcgt tgagggaaag 2460 atgacgccgc ctttaaccgg agatttcaga ctttctcagt tgcttgaatc caccatgcag 2520 attcggtctg acttaaagcc cagtttatat gtgcatacag ttgcaacgat gggtgtcaac 2580 agaatact ttcaacatgc tgttgaaatt caaggcgagg tccagacaag aatgccaatg 2640 aagtttgatg ccaagataga tgtgaaattg aaaaacctta agattgaaac gaacccatgc 2700 cgtgaggaaa ctgagatagt ggttggagaa cataaggctt ttgctgtatc aaagaacata 2760 ggagaactag gtgttgaaaa gaggacctca attctgccgg aagatgctcc attagatgtt 2820 acagagaac ctttccaaac atcagaga gcttccaggg aacacttcgc aatgcaaggg 2880 cctgacagca tgccaaggaa acagtcccat agttctcgag aagatcttcg ccgtagcaca 2940 ggaaaaagag cacataaacg agacatttgc ctcaaaatgc atcatattgg ttgccagctt 3000 tgcttttcca gaaggtcaag agatgccagt ttcatacaga atacgtattt gcacaaatta 3060 attggagaac atgaagctaa aatagttttg atgccagttc atacagatgc tgatattgac 3120 aaaattcagc tggagattca ggcaggatct agagcagctg ccagaataat tactgaggta 3180 aacccagagt ctgaggaaga ggatgaatca tctccatatg aggacattca agctaaactg 3240 aagaggattc taggcattga cagtatgttc aaggttgcaa acaaaacacg gcacccgaaa 3300 aatcgaccat ctaagaaagg aaacactgtg ctagcagagt ttgggacaga gcctgatgca 3360 aaa 3363 <210> 59 <211> 1121 <212> PRT <213> Chicken (Gallus gallus) <400> 59 Met Arg Gly Ile Ile Leu Ala Leu Val Leu Thr Leu Val Gly Ser Gln 1 5 10 15 Lys Phe Asp Ile Asp Pro Gly Phe Asn Ser Arg Arg Ser Tyr Leu Tyr 20 25 30 Asn Tyr Glu Gly Ser Met Leu Asn Gly Leu Gln Asp Arg Ser Leu Gly 35 40 45 Lys Ala Gly Val Arg Leu Ser Ser Lys Leu Glu Ile Ser Gly Leu Pro 50 55 60 Glu Asn Ala Tyr Leu Leu Lys Val Arg Ser Pro Gln Val Glu Glu Tyr 65 70 75 80 Asn Gly Val Trp Pro Arg Asp Pro Phe Thr Arg Ser Ser Lys Ile Thr 85 90 95 Gln Val Ile Ser Ser Cys Phe Thr Arg Leu Phe Lys Phe Glu Tyr Ser 100 105 110 Ser Gly Arg Ile Gly Asn Ile Tyr Ala Pro Glu Asp Cys Pro Asp Leu 115 120 125 Cys Val Asn Ile Val Arg Gly Ile Leu Asn Met Phe Gln Met Thr Ile 130 135 140 Lys Lys Ser Gln Asn Val Tyr Glu Leu Gln Glu Ala Gly Ile Gly Gly 145 150 155 160 Ile Cys His Ala Arg Tyr Val Ile Gln Glu Asp Arg Lys Asn Ser Arg 165 170 175 Ile Tyr Val Thr Arg Thr Val Asp Leu Asn Asn Cys Gln Glu Lys Val 180 185 190 Gln Lys Ser Ile Gly Met Ala Tyr Ile Tyr Pro Cys Pro Val Asp Val 195 200 205 Met Lys Glu Arg Leu Thr Lys Gly Thr Thr Ala Phe Ser Tyr Lys Leu 210 215 220 Lys Gln Ser Asp Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg Gln 225 230 235 240 Val Tyr Gln Ile Ser Pro Phe Asn Glu Pro Thr Gly Val Ala Val Met 245 250 255 Glu Ala Arg Gln Gln Leu Thr Leu Val Glu Val Arg Ser Glu Arg Gly 260 265 270 Ser Ala Pro Asp Val Pro Met Gln Asn Tyr Gly Ser Leu Arg Tyr Arg 275 280 285 Phe Pro Ala Val Leu Pro Gln Met Pro Leu Gln Leu Ile Lys Thr Lys 290 295 300 Asn Pro Glu Gln Arg Ile Ile Glu Thr Leu Gln His Ile Val Leu Asn 305 310 315 320 Asn Gln Gln Asp Phe His Asp Asp Val Ser Tyr Arg Phe Leu Glu Val 325 330 335 Val Gln Leu Cys Arg Ile Ala Asn Ala Asp Asn Leu Glu Ser Ile Trp 340 345 350 Arg Gln Val Ser Asp Lys Pro Arg Tyr Arg Arg Trp Leu Leu Ser Ala 355 360 365 Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys Phe Leu Lys Asn Arg 370 375 380 Ile Arg Asn Asp Asp Leu Asn Tyr Ile Gln Thr Leu Leu Thr Val Ser 385 390 395 400 Leu Thr Leu His Leu Leu Gln Ala Asp Glu His Thr Leu Pro Ile Ala 405 410 415 Ala Asp Leu Met Thr Ser Ser Arg Ile Gln Lys Asn Pro Val Leu Gln 420 425 430 Gln Val Ala Cys Leu Gly Tyr Ser Ser Val Val Asn Arg Tyr Cys Ser 435 440 445 Gln Thr Ser Ala Cys Pro Lys Glu Ala Leu Gln Pro Ile His Asp Leu 450 455 460 Ala Asp Glu Ala Ile Ser Arg Gly Arg Glu Asp Lys Met Lys Leu Ala 465 470 475 480 Leu Lys Cys Ile Gly Asn Met Gly Glu Pro Ala Ser Leu Lys Arg Ile 485 490 495 Leu Lys Phe Leu Pro Ile Ser Ser Ser Ser Ala Ala Asp Ile Pro Val 500 505 510 His Ile Gln Ile Asp Ala Ile Thr Ala Leu Lys Lys Ile Ala Trp Lys 515 520 525 Asp Pro Lys Thr Val Gln Gly Tyr Leu Ile Gln Ile Leu Ala Asp Gln 530 535 540 Ser Leu Pro Pro Glu Val Arg Met Met Ala Cys Ala Val Ile Phe Glu 545 550 555 560 Thr Arg Pro Ala Leu Ala Leu Ile Thr Thr Ile Ala Asn Val Ala Met 565 570 575 Lys Glu Ser Asn Met Gln Val Ala Ser Phe Val Tyr Ser His Met Lys 580 585 590 Ser Leu Ser Lys Ser Arg Leu Pro Phe Met Tyr Asn Ile Ser Ser Ala 595 600 605 Cys Asn Ile Ala Leu Lys Leu Leu Ser Pro Lys Leu Asp Ser Met Ser 610 615 620 Tyr Arg Tyr Ser Lys Val Ile Arg Ala Asp Thr Tyr Phe Asp Asn Tyr 625 630 635 640 Arg Val Gly Ala Thr Gly Glu Ile Phe Val Val Asn Ser Pro Arg Thr 645 650 655 Met Phe Pro Ser Ala Ile Ile Ser Lys Leu Met Ala Asn Ser Ala Gly 660 665 670 Ser Val Ala Asp Leu Val Glu Val Gly Ile Arg Val Glu Gly Leu Ala 675 680 685 Asp Val Ile Met Lys Arg Asn Ile Pro Phe Ala Glu Tyr Pro Thr Tyr 690 695 700 Lys Gln Ile Lys Glu Leu Gly Lys Ala Leu Gln Gly Trp Lys Glu Leu 705 710 715 720 Pro Thr Glu Thr Pro Leu Val Ser Ala Tyr Leu Lys Ile Leu Gly Gln 725 730 735 Glu Val Ala Phe Ile Asn Ile Asn Lys Glu Leu Leu Gln Gln Val Met 740 745 750 Lys Thr Val Val Glu Pro Ala Asp Arg Asn Ala Ala Ile Lys Arg Ile 755 760 765 Ala Asn Gln Ile Arg Asn Ser Ile Ala Gly Gln Trp Thr Gln Pro Val 770 775 780 Trp Met Gly Glu Leu Arg Tyr Val Val Pro Ser Cys Leu Gly Leu Pro 785 790 795 800 Leu Glu Tyr Gly Ser Tyr Thr Thr Ala Leu Ala Arg Ala Ala Val Ser 805 810 815 Val Glu Gly Lys Met Thr Pro Pro Leu Thr Gly Asp Phe Arg Leu Ser 820 825 830 Gln Leu Leu Glu Ser Thr Met Gln Ile Arg Ser Asp Leu Lys Pro Ser 835 840 845 Leu Tyr Val His Thr Val Ala Thr Met Gly Val Asn Thr Glu Tyr Phe 850 855 860 Gln His Ala Val Glu Ile Gln Gly Glu Val Gln Thr Arg Met Pro Met 865 870 875 880 Lys Phe Asp Ala Lys Ile Asp Val Lys Leu Lys Asn Leu Lys Ile Glu 885 890 895 Thr Asn Pro Cys Arg Glu Glu Thr Glu Ile Val Val Gly Arg His Lys 900 905 910 Ala Phe Ala Val Ser Arg Asn Ile Gly Glu Leu Gly Val Glu Lys Arg 915 920 925 Thr Ser Ile Leu Pro Glu Asp Ala Pro Leu Asp Val Thr Glu Glu Pro 930 935 940 Phe Gln Thr Ser Glu Arg Ala Ser Arg Glu His Phe Ala Met Gln Gly 945 950 955 960 Pro Asp Ser Met Pro Arg Lys Gln Ser His Ser Ser Arg Glu Asp Leu 965 970 975 Arg Arg Ser Thr Gly Lys Arg Ala His Lys Arg Asp Ile Cys Leu Lys 980 985 990 Met His His Ile Gly Cys Gln Leu Cys Phe Ser Arg Arg Ser Arg Asp 995 1000 1005 Ala Ser Phe Ile Gln Asn Thr Tyr Leu His Lys Leu Ile Gly Glu 1010 1015 1020 His Glu Ala Lys Ile Val Leu Met Pro Val His Thr Asp Ala Asp 1025 1030 1035 Ile Asp Lys Ile Gln Leu Glu Ile Gln Ala Gly Ser Arg Ala Ala 1040 1045 1050 Ala Arg Ile Ile Thr Glu Val Asn Pro Glu Ser Glu Glu Glu Asp 1055 1060 1065 Glu Ser Ser Pro Tyr Glu Asp Ile Gln Ala Lys Leu Lys Arg Ile 1070 1075 1080 Leu Gly Ile Asp Ser Met Phe Lys Val Ala Asn Lys Thr Arg His 1085 1090 1095 Pro Lys Asn Arg Pro Ser Lys Lys Gly Asn Thr Val Leu Ala Glu 1100 1105 1110 Phe Gly Thr Glu Pro Asp Ala Lys 1115 1120 <210> 60 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 60 Ala Asp Gln Ser Leu Pro Pro Glu Val Arg 1 5 10 <210> 61 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 61 Ala Asp Thr Tyr Phe Asp Asn Tyr Arg 1 5 <210> 62 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 62 Ala Val Ile Phe Glu Thr Arg 1 5 <210> 63 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 63 Asp Ala Ser Phe Ile Gln Asn Thr Tyr Leu His Lys 1 5 10 <210> 64 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 64 Asp Leu Ala Asp Glu Ala Ile Ser Arg 1 5 <210> 65 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 65 Glu Ala Leu Gln Pro Ile His Asp Leu Ala Asp Glu Ala Ile Ser Arg 1 5 10 15 <210> 66 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 66 Glu Glu Thr Glu Ile Val Val Gly Arg 1 5 <210> 67 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 67 Glu Ile Phe Val Val Asn Ser Pro Arg 1 5 <210> 68 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 68 Glu Leu Pro Thr Glu Thr Pro Leu Val Ser Ala Tyr Leu Lys 1 5 10 <210> 69 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 69 Phe Asp Ile Asp Pro Gly Phe Asn Ser Arg 1 5 10 <210> 70 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 70 Phe Glu Tyr Ser Ser Gly Arg 1 5 <210> 71 <211> 25 <212> PRT <213> Chicken (Gallus gallus) <400> 71 Phe Leu Pro Ile Ser Ser Ser Ser Ala Ala Asp Ile Pro Val His Ile 1 5 10 15 Gln Ile Asp Ala Ile Thr Ala Leu Lys 20 25 <210> 72 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 72 Gly Tyr Ser Ser Val Val Asn Arg 1 5 <210> 73 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 73 Ile Ala Asn Ala Asp Asn Leu Glu Ser Ile Trp Arg 1 5 10 <210> 74 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 74 Ile Asp Ala Ile Thr Ala Leu Lys 1 5 <210> 75 <211> 24 <212> PRT <213> Chicken (Gallus gallus) <400> 75 Ile Ile Thr Glu Val Asn Pro Glu Ser Glu Glu Glu Asp Glu Ser Ser 1 5 10 15 Pro Tyr Glu Asp Ile Gln Ala Lys 20 <210> 76 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 76 Ile Leu Ala Asp Gln Ser Leu Pro Pro Glu Val Arg 1 5 10 <210> 77 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 77 Ile Leu Gly Gln Glu Val Ala Phe Ile Asn Ile Asn Lys 1 5 10 <210> 78 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 78 Ile Gln Leu Glu Ile Gln Ala Gly Ser Arg 1 5 10 <210> 79 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 79 Ile Arg Asn Asp Asp Leu Asn Tyr Ile Gln Thr Leu Leu 1 5 10 <210> 80 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 80 Leu Ala Asp Glu Ala Ile Ser Arg 1 5 <210> 81 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 81 Leu Glu Ile Ser Gly Leu Pro Glu Asn Ala Tyr Leu Leu Lys 1 5 10 <210> 82 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 82 Leu Gly Tyr Ser Ser Val Val Asn Arg 1 5 <210> 83 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 83 Leu Ile Gln Ile Leu Ala Asp Gln Ser Leu Pro Pro Glu Val Arg 1 5 10 15 <210> 84 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 84 Leu Lys Gln Ser Asp Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg 1 5 10 15 <210> 85 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 85 Leu Leu Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 15 <210> 86 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 86 Leu Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 87 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 87 Asn Ile Pro Phe Ala Glu Tyr Pro Thr Tyr Lys 1 5 10 <210> 88 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 88 Pro Ala Leu Ala Leu Ile Thr Thr Ile Ala Asn 1 5 10 <210> 89 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 89 Pro Pro Leu Thr Gly Asp Phe Arg 1 5 <210> 90 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 90 Gln Gln Leu Thr Leu Val Glu Val Arg 1 5 <210> 91 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 91 Gln Ser Asp Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg 1 5 10 <210> 92 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 92 Arg Asn Ile Pro Phe Ala Glu Tyr Pro Thr Tyr Lys 1 5 10 <210> 93 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 93 Ser Ala Gly Ser Val Ala Asp Leu Val Glu Val Gly Ile Arg 1 5 10 <210> 94 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 94 Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 95 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 95 Ser Asp Leu Lys Pro Ser Leu Tyr 1 5 <210> 96 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 96 Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg 1 5 10 <210> 97 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 97 Ser Pro Gln Val Glu Glu Tyr Asn Gly Val Trp Pro Arg 1 5 10 <210> 98 <211> 22 <212> PRT <213> Chicken (Gallus gallus) <400> 98 Thr Ser Ile Leu Pro Glu Asp Ala Pro Leu Asp Val Thr Glu Glu Pro 1 5 10 15 Phe Gln Thr Ser Glu Arg 20 <210> 99 <211> 20 <212> PRT <213> Chicken (Gallus gallus) <400> 99 Thr Val Gln Gly Tyr Leu Ile Gln Ile Leu Ala Asp Gln Ser Leu Pro 1 5 10 15 Pro Glu Val Arg 20 <210> 100 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 100 Thr Val Val Glu Pro Ala Asp Arg 1 5 <210> 101 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 101 Val Gly Ala Thr Gly Glu Ile Phe Val Val Asn Ser Pro Arg 1 5 10 <210> 102 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 102 Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 103 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 103 Trp Leu Leu Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 15 <210> 104 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 104 Tyr Val Ile Gln Glu Asp Arg Lys 1 5 <210> 105 <211> 5550 <212> DNA <213> Chicken (Gallus gallus) <400> 105 atgaggggga tcatactggc attagtgctc acccttgtag gcagccagaa gtttgacatt 60 gacccaggat tcaatagcag aaggagttac ctgtacaact atgaaggttc tatgttgaat 120 gggcttcaag acagaagttt gggcaaagct ggtgtgcgct tgagcagcaa gctagagatc 180 agtgggctac cagagaatgc ttacctcctc aaggtccgct ctccacaagt ggaggagtac 240 aatggggtct ggcccaggga tcccttcact cgatcttcca aaatcaccca agtgatctca 300 tcgtgtttca cccggctctt caaatttgaa tacagcagtg gacggatcgg aaacatttat 360 gccccagaag actgcccaga tctgtgtgtt aacatagtga gaggaatatt gaacatgttc 420 cagatgacca ttaaaaaatc acagaacgtc tacgaattac aagaggctgg aattggaggt 480 atttgtcatg caaggtatgt cattcaggaa gacaggaaga atagccgaat ctatgttacc 540 agaactgtgg acttgaataa ttgccaggaa aaggtgcaaa aaagcattgg aatggcttac 600 atctatccct gccctgtgga cgtgatgaaa gaaaggctca ccaaagggac caccgctttc 660 tcctacaagc tgaagcagtc agacagcggc acgctgatca cagatgtctc gtcgcggcag 720 gtgtatcaga tctccccatt caatgagccc actggggtgg ctgtcatgga agcaagacag 780 cagctcactt tggtcgaggt gagaagtgag cggggcagtg ccccagatgt ccccatgcag 840 aactatggca gccttcgcta ccgcttccca gccgtactgc cacagatgcc acttcagctg 900 atcaagacaa aaaaccctga gcaacggata gtagaaacgc tgcagcacat agtcctgaat 960 aaccaacaag atttccatga cgatgtttca tacagattct tagaggtggt ccagctttgc 1020 cggatagcaa atgctgacaa tcttgagtct atctggagac aagtttcaga taaacctcgt 1080 tacaggcgat ggctcctgag cgcagtttct gcgagtggca ccacagaaac actaaaattc 1140 cttaagaaca gaattcgcaa tgatgacctc aactacattc agacccttct aactgtttct 1200 ttgactcttc atttattgca agctgatgaa cacacacttc caatagcagc agatttaatg 1260 accagctctc gaattcagaa aaatcctgtg cttcagcaag tggcctgctt gggatatagc 1320 tctgtagtca acagatactg ctctcagacc tcagcatgtc ctaaggaagc tcttcagccc 1380 atccatgacc tggcagatga agcaatcagc aggggccgtg aagacaaat gaaattagct 1440 ctaaagtgca ttggtacat gggagaacca gccagcttaa agcgcatcct gaagttcctt 1500 ccaatatctt catccagtgc tgctgatatc ccagtccaca ttcagataga tgccataacg 1560 gccttgaaaa agatagcttg gaaggacccc aaaacagtgc agggctatct catccagatc 1620 cttgcagacc aatcacttcc ccctgaggtg cgaatgatgg cttgtgctgt tatctttgag 1680 acaagcctg cccttgcttt gatacgact atagctaacg tggcaatgaa ggagagcaat 1740 atgcaagtgg ccagttttgt atattcccac atgaagtctt tgtcaagg cagattgcca 1800 tttatgtaca acatactctc cgcttgtaac attgcctta agctccctgtc cccaactg 1860 gagtatga gctatcggta cagcaggtc attcgagcag acacttactt tgataactat 1920 agagttggtg ctactggaga aatctttgtt gtgaacagcc CAagaactat gttcccatca 1980 gcaataattt ccaaattgat ggcaattct gcaggttcag tggctgat ggtagaggtt 2040 ggcatccgag tggaggcct cgcagatgtc ataatgaaaa gaaacatccc atttgctgaa 2100 tatcccacat aaagcagat aaaggagctt ggaaaagctc tgcagggatg gaaagagctg 2160 ccgacagaaa cccctttggt atcagcctac ttgaaaatac ttggccaaga agtggccttc 2220 2280 cgaaacgcag caataaagag aatcgccaac cagatccgca acagcattgc agggcagtgg 2340 acgcagccgg tgtggatggg agagctgcga tacgtggttc ccagctgtct cggcctgccg 2400 ctggagtacg ggtcctacac caccgccctg gcacgagctg cagtcagcgt tgagggaaag 2460 atgacgccgc ctttaaccgg agatttcaga ctttctcagt tgcttgaatc caccatgcag 2520 attcggtctg acttaaagcc cagtttatat gtgcatacag ttgcaacgat gggtgtcaac 2580 agaatact ttcaacatgc tgttgaaatt caaggcgagg tccagacaag aatgccaatg 2640 aagtttgatg ccaagataga tgtgaaattg aaaaacctta agattgaaac gaacccatgc 2700 cgtgaggaaa ctgagatagt ggttggagaa cataaggctt ttgctgtatc aaagaacata 2760 ggagaactag gtgttgaaaa gaggacctca attctgccgg aagatgctcc attagatgtt 2820 acagagaac ctttccaaac atcagaga gcttccaggg aacacttcgc aatgcaaggg 2880 cctgacagca tgccaaggaa acagtcccat agttctcgag aagatcttcg ccgtagcaca 2940 ggaaaaagag cacataaacg agacatttgc ctcaaaatgc atcatattgg ttgccagctt 3000 tgcttttcca gaaggtcaag agatgccagt ttcatacaga atacgtattt gcacaaatta 3060 3120 aaaattcagc tggagattca ggcaggatct agagcagctg ccagaataat tactgaggta 3180 3240 aagaggattc taggcattga cagattagttc aaggttgcaa acaaaacacg gcacccgaaa 3300 aatcgaccat ctaagaaagg aaacactgtg ctagcagagt ttgggacaga gcctgatgca 3360 aaaacttcct ccagctcatc ttctgcctcc tcaactgcca cctcttcttc ctcatcatct 3420 gcctcctctc ctaatcgtaa aaagcctatg gatgaagagg agaatgatca agtaaagcaa 3480 caagaaaca aagatgcaag cagcagcagc aggagcagca agagcagtaa cagcagcaag 3540 agaagcagca ccaagagcag taacagcagc aagagaagca ccagagcag tagcagtagc 3600 agtagcagca gcaggagcag cagcagtagc agcagtagta gacgtaacag caagaccagc 3660 agtagcagca ccaagagcag cataggagcagc agcagggaca gaagcagcag caagagcagc 3720 3780 agcagcagca gcaagtcaag cagtcaccat agccatagcc atcattcagg gcatctaaat 3840 ggcagcagca gcagcagcag cagcagcagg tcagtgagtc accacagcca tgagcatcac 3900 tcaggacatc tggagaatga cagcagtagc agcagcagca gcagcgtgct ttccaaaata 3960 tggggcgtc atgagattta tcagtatcgc tttagatcag cacagaca agagttcccc 4020 aaaagaaaac tcccaggtga ccgcgctacc agcagatact cctctaccag atccagccat 4080 gacacatccc gagctgcttc ctggcctaag tttctgggtg acatcaaaac cccagtgtta 4140 gctgcttttc tccatggcat tagtaacaat aagaagacag gaggcctcca gcttgtggta 4200 tatgctgata ccgactcggt caggccgcgg gtgcaggtat ttgtgacaaa cctcacagat 4260 tcgagcaagt ggaagctctg cgcagatgct tcggtccgca atgctcacaa ggcagtggcc 4320 tacgtgaaat ggggctggga ctgccgggac tacaaggttt ctactgagct ggtaactggg 4380 cggtttgctg ggcaccctgc tgcacaagtg aagctggagt ggcccaaggt tccttcgaat 4440 gtcagatcag tggttgaatg gttttacgag tttgtccctg gggctgcatt tatgctgggt 4500 ttctctgaga gaatggacaa gaatccttct cgacaagcca ggatggttgt ggctctaact 4560 tctccgagga catgtgatgt tgttgtcaag ctgcctgata taatcctcta tcaaaaagcc 4620 gtgaggcttc ctctatcact ccctgtgggt ccaaggatcc cagcttcaga gctgcagcct 4680 ccaatctgga acgtctttgc tgaagccccc tctgccgtgc tcgagaattt gaaagctcgc 4740 tgctcagttt cgtacaacaa gatcaaaacc tttaatgaag tcaagttcaa ctactcgatg 4800 cccgcaaact gctatcacat cttggttcag gattgcagct ctgaacttaa gttcctggtg 4860 atgatgaaaa gtgctggaga agctacaaac cttaaagcca tcaacatcaa gattggcagt 4920 catgaaattg atatgcatcc tgtgaatgga caggtgaaac tgctggtaga tggggctgag 4980 agccccacag ccaacatttc cctcatatct gctggtgctt ctctgtggat tcacaatgaa 5040 aaccaagggt ttgcacttgc tgccccaggc catggtatcg ataaattgta cttcgatgga 5100 aaaacaatca cgattcaagt tcctttatgg atggcaggga aaacatgtgg aatctgtgga 5160 aaatatgatg cagaatgcga acaggagtat cggatgccca atggatatct agctaaaaat 5220 gccgtgagct ttggtcattc ttggatcttg gaagaagcgc cctgtagagg agcttgtaaa 5280 ctgcatcgtt cattcgtgaa gcttgagaag acggttcagc tggcgggtgt tgattccaag 5340 tgctactcta cagagcctgt gctgcgctgt gcaaagggat gctctgctac caagacaact 5400 ccagtaactg ttggcttcca ctgcctccca gctgattcag ctaacagcct aactgacaaa 5460 cagatgaagt acgaccagaa gtcagaagac atgcaggata ctgttgatgc acacacaacg 5520 tgttcatgtg agaatgagga atgcagtaca 5550 <210> 106 <211> 1850 <212> PRT <213> Chicken (Gallus gallus) <400> 106 Met Arg Gly Ile Ile Leu Ala Leu Val Leu Thr Leu Val Gly Ser Gln 1 5 10 15 Lys Phe Asp Ile Asp Pro Gly Phe Asn Ser Arg Arg Ser Tyr Leu Tyr 20 25 30 Asn Tyr Glu Gly Ser Met Leu Asn Gly Leu Gln Asp Arg Ser Leu Gly 35 40 45 Lys Ala Gly Val Arg Leu Ser Ser Lys Leu Glu Ile Ser Gly Leu Pro 50 55 60 Glu Asn Ala Tyr Leu Leu Lys Val Arg Ser Pro Gln Val Glu Glu Tyr 65 70 75 80 Asn Gly Val Trp Pro Arg Asp Pro Phe Thr Arg Ser Ser Lys Ile Thr 85 90 95 Gln Val Ile Ser Ser Cys Phe Thr Arg Leu Phe Lys Phe Glu Tyr Ser 100 105 110 Ser Gly Arg Ile Gly Asn Ile Tyr Ala Pro Glu Asp Cys Pro Asp Leu 115 120 125 Cys Val Asn Ile Val Arg Gly Ile Leu Asn Met Phe Gln Met Thr Ile 130 135 140 Lys Lys Ser Gln Asn Val Tyr Glu Leu Gln Glu Ala Gly Ile Gly Gly 145 150 155 160 Ile Cys His Ala Arg Tyr Val Ile Gln Glu Asp Arg Lys Asn Ser Arg 165 170 175 Ile Tyr Val Thr Arg Thr Val Asp Leu Asn Asn Cys Gln Glu Lys Val 180 185 190 Gln Lys Ser Ile Gly Met Ala Tyr Ile Tyr Pro Cys Pro Val Asp Val 195 200 205 Met Lys Glu Arg Leu Thr Lys Gly Thr Thr Ala Phe Ser Tyr Lys Leu 210 215 220 Lys Gln Ser Asp Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg Gln 225 230 235 240 Val Tyr Gln Ile Ser Pro Phe Asn Glu Pro Thr Gly Val Ala Val Met 245 250 255 Glu Ala Arg Gln Gln Leu Thr Leu Val Glu Val Arg Ser Glu Arg Gly 260 265 270 Ser Ala Pro Asp Val Pro Met Gln Asn Tyr Gly Ser Leu Arg Tyr Arg 275 280 285 Phe Pro Ala Val Leu Pro Gln Met Pro Leu Gln Leu Ile Lys Thr Lys 290 295 300 Asn Pro Glu Gln Arg Ile Val Glu Thr Leu Gln His Ile Val Leu Asn 305 310 315 320 Asn Gln Gln Asp Phe His Asp Asp Val Ser Tyr Arg Phe Leu Glu Val 325 330 335 Val Gln Leu Cys Arg Ile Ala Asn Ala Asp Asn Leu Glu Ser Ile Trp 340 345 350 Arg Gln Val Ser Asp Lys Pro Arg Tyr Arg Arg Trp Leu Leu Ser Ala 355 360 365 Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys Phe Leu Lys Asn Arg 370 375 380 Ile Arg Asn Asp Asp Leu Asn Tyr Ile Gln Thr Leu Leu Thr Val Ser 385 390 395 400 Leu Thr Leu His Leu Leu Gln Ala Asp Glu His Thr Leu Pro Ile Ala 405 410 415 Ala Asp Leu Met Thr Ser Ser Arg Ile Gln Lys Asn Pro Val Leu Gln 420 425 430 Gln Val Ala Cys Leu Gly Tyr Ser Ser Val Val Asn Arg Tyr Cys Ser 435 440 445 Gln Thr Ser Ala Cys Pro Lys Glu Ala Leu Gln Pro Ile His Asp Leu 450 455 460 Ala Asp Glu Ala Ile Ser Arg Gly Arg Glu Asp Lys Met Lys Leu Ala 465 470 475 480 Leu Lys Cys Ile Gly Asn Met Gly Glu Pro Ala Ser Leu Lys Arg Ile 485 490 495 Leu Lys Phe Leu Pro Ile Ser Ser Ser Ser Ala Ala Asp Ile Pro Val 500 505 510 His Ile Gln Ile Asp Ala Ile Thr Ala Leu Lys Lys Ile Ala Trp Lys 515 520 525 Asp Pro Lys Thr Val Gln Gly Tyr Leu Ile Gln Ile Leu Ala Asp Gln 530 535 540 Ser Leu Pro Pro Glu Val Arg Met Met Ala Cys Ala Val Ile Phe Glu 545 550 555 560 Thr Arg Pro Ala Leu Ala Leu Ile Thr Thr Ile Ala Asn Val Ala Met 565 570 575 Lys Glu Ser Asn Met Gln Val Ala Ser Phe Val Tyr Ser His Met Lys 580 585 590 Ser Leu Ser Lys Ser Arg Leu Pro Phe Met Tyr Asn Ile Ser Ser Ala 595 600 605 Cys Asn Ile Ala Leu Lys Leu Leu Ser Pro Lys Leu Asp Ser Met Ser 610 615 620 Tyr Arg Tyr Ser Lys Val Ile Arg Ala Asp Thr Tyr Phe Asp Asn Tyr 625 630 635 640 Arg Val Gly Ala Thr Gly Glu Ile Phe Val Val Asn Ser Pro Arg Thr 645 650 655 Met Phe Pro Ser Ala Ile Ile Ser Lys Leu Met Ala Asn Ser Ala Gly 660 665 670 Ser Val Ala Asp Leu Val Glu Val Gly Ile Arg Val Glu Gly Leu Ala 675 680 685 Asp Val Ile Met Lys Arg Asn Ile Pro Phe Ala Glu Tyr Pro Thr Tyr 690 695 700 Lys Gln Ile Lys Glu Leu Gly Lys Ala Leu Gln Gly Trp Lys Glu Leu 705 710 715 720 Pro Thr Glu Thr Pro Leu Val Ser Ala Tyr Leu Lys Ile Leu Gly Gln 725 730 735 Glu Val Ala Phe Ile Asn Ile Asn Lys Glu Leu Leu Gln Gln Val Met 740 745 750 Lys Thr Val Val Glu Pro Ala Asp Arg Asn Ala Ala Ile Lys Arg Ile 755 760 765 Ala Asn Gln Ile Arg Asn Ser Ile Ala Gly Gln Trp Thr Gln Pro Val 770 775 780 Trp Met Gly Glu Leu Arg Tyr Val Val Pro Ser Cys Leu Gly Leu Pro 785 790 795 800 Leu Glu Tyr Gly Ser Tyr Thr Thr Ala Leu Ala Arg Ala Ala Val Ser 805 810 815 Val Glu Gly Lys Met Thr Pro Pro Leu Thr Gly Asp Phe Arg Leu Ser 820 825 830 Gln Leu Leu Glu Ser Thr Met Gln Ile Arg Ser Asp Leu Lys Pro Ser 835 840 845 Leu Tyr Val His Thr Val Ala Thr Met Gly Val Asn Thr Glu Tyr Phe 850 855 860 Gln His Ala Val Glu Ile Gln Gly Glu Val Gln Thr Arg Met Pro Met 865 870 875 880 Lys Phe Asp Ala Lys Ile Asp Val Lys Leu Lys Asn Leu Lys Ile Glu 885 890 895 Thr Asn Pro Cys Arg Glu Glu Thr Glu Ile Val Val Gly Arg His Lys 900 905 910 Ala Phe Ala Val Ser Arg Asn Ile Gly Glu Leu Gly Val Glu Lys Arg 915 920 925 Thr Ser Ile Leu Pro Glu Asp Ala Pro Leu Asp Val Thr Glu Glu Pro 930 935 940 Phe Gln Thr Ser Glu Arg Ala Ser Arg Glu His Phe Ala Met Gln Gly 945 950 955 960 Pro Asp Ser Met Pro Arg Lys Gln Ser His Ser Ser Arg Glu Asp Leu 965 970 975 Arg Arg Ser Thr Gly Lys Arg Ala His Lys Arg Asp Ile Cys Leu Lys 980 985 990 Met His His Ile Gly Cys Gln Leu Cys Phe Ser Arg Arg Ser Arg Asp 995 1000 1005 Ala Ser Phe Ile Gln Asn Thr Tyr Leu His Lys Leu Ile Gly Glu 1010 1015 1020 His Glu Ala Lys Ile Val Leu Met Pro Val His Thr Asp Ala Asp 1025 1030 1035 Ile Asp Lys Ile Gln Leu Glu Ile Gln Ala Gly Ser Arg Ala Ala 1040 1045 1050 Ala Arg Ile Ile Thr Glu Val Asn Pro Glu Ser Glu Glu Glu Asp 1055 1060 1065 Glu Ser Ser Pro Tyr Glu Asp Ile Gln Ala Lys Leu Lys Arg Ile 1070 1075 1080 Leu Gly Ile Asp Ser Met Phe Lys Val Ala Asn Lys Thr Arg His 1085 1090 1095 Pro Lys Asn Arg Pro Ser Lys Lys Gly Asn Thr Val Leu Ala Glu 1100 1105 1110 Phe Gly Thr Glu Pro Asp Ala Lys Thr Ser Ser Ser Ser Ser 1115 1120 1125 Wing Being Being Thr Wing Thr Being Being Being Being Being Wing Being Being Being 1130 1135 1140 Pro Asn Arg Lys Lys Pro Met Asp Glu Glu Glu Asn Asp Gln Val 1145 1150 1155 Lys Gln Ala Arg Asn Lys Asp Ala Being Being Being Being Arg Being Being 1160 1165 1170 Lys Being Being Asn Being Being Lys Arg Being Being Being Lys Being Being Asn 1175 1180 1185 To Be To Be Lys Arg To Be To Be To Be To Be To Be To Be To Be To Be To Be 1190 1195 1200 Be Arg Be Be Be Be Be Be Be Be Be Be Be Be Asn Be Lys 1205 1210 1215 To Be To Be To Be To Be Lys To Be To Be To Be To Be Arg To Be 1220 1225 1230 Arg Be Be Be Lys Be Be Be Be Be Be Be Be Be Be Be Be 1235 1240 1245 To Be To Be To Be Lys To Be To Be To Be Arg To Be To Be To Be To Be 1250 1255 1260 See Light See See See His His See His See His His See Gly His 1265 1270 1275 Leu Asn Gly See See See See See See See See Arg See Val See 1280 1285 1290 His His Ser His Glu His His Ser Gly His Leu Glu Asp Asp Ser 1295 1300 1305 Ser Ser Ser Ser Ser Ser Val Leu Ser Lys Ile Trp Gly Arg 1310 1315 1320 His Glu Ile Tyr Gln Tyr Arg Phe Arg Ser Ala His Arg Gln Glu 1325 1330 1335 Phe Pro Lys Arg Lys Leu Pro Gly Asp Arg Ala Thr Ser Arg Tyr 1340 1345 1350 Ser Ser Thr Arg Ser Ser His Asp Thr Ser Arg Ala Ala Ser Trp 1355 1360 1365 Pro Lys Phe Leu Gly Asp Ile Lys Thr Pro Val Leu Ala Ala Phe 1370 1375 1380 Leu His Gly Ile Ser Asn Asn Lys Lys Thr Gly Gly Leu Gln Leu 1385 1390 1395 Val Val Tyr Ala Asp Thr Asp Ser Val Arg Pro Arg Val Gln Val 1400 1405 1410 Phe Val Thr Asn Leu Thr Asp Ser Ser Lys Trp Lys Leu Cys Ala 1415 1420 1425 Asp Ala Ser Val Arg Asn Ala His Lys Ala Val Ala Tyr Val Lys 1430 1435 1440 Trp Gly Trp Asp Cys Arg Asp Tyr Lys Val Ser Thr Glu Leu Val 1445 1450 1455 Thr Gly Arg Phe Ala Gly His Pro Ala Ala Gln Val Lys Leu Glu 1460 1465 1470 Trp Pro Lys Val Pro Ser Asn Val Arg Ser Val Val Glu Trp Phe 1475 1480 1485 Tyr Glu Phe Val Pro Gly Ala Ala Phe Met Leu Gly Phe Ser Glu 1490 1495 1500 Arg Met Asp Lys Asn Pro Ser Arg Gln Ala Arg Met Val Val Ala 1505 1510 1515 Leu Thr Ser Pro Arg Thr Cys Asp Val Val Val Lys Leu Pro Asp 1520 1525 1530 Ile Ile Leu Tyr Gln Lys Ala Val Arg Leu Pro Leu Ser Leu Pro 1535 1540 1545 Val Gly Pro Arg Ile Pro Ala Ser Glu Leu Gln Pro Pro Ile Trp 1550 1555 1560 Asn Val Phe Ala Glu Ala Pro Ser Ala Val Leu Glu Asn Leu Lys 1565 1570 1575 Ala Arg Cys Ser Val Ser Tyr Asn Lys Ile Lys Thr Phe Asn Glu 1580 1585 1590 Val Lys Phe Asn Tyr Ser Met Pro Ala Asn Cys Tyr His Ile Leu 1595 1600 1605 Val Gln Asp Cys Ser Ser Glu Leu Lys Phe Leu Val Met Met Lys 1610 1615 1620 Ser Ala Gly Glu Ala Thr Asn Leu Lys Ala Ile Asn Ile Lys Ile 1625 1630 1635 Gly Ser His Glu Ile Asp Met His Pro Val Asn Gly Gln Val Lys 1640 1645 1650 Leu Leu Val Asp Gly Ala Glu Ser Pro Thr Ala Asn Ile Ser Leu 1655 1660 1665 Ile Ser Ala Gly Ala Ser Leu Trp Ile His Asn Glu Asn Gln Gly 1670 1675 1680 Phe Ala Leu Ala Ala Pro Gly His Gly Ile Asp Lys Leu Tyr Phe 1685 1690 1695 Asp Gly Lys Thr Ile Thr Ile Gln Val Pro Leu Trp Met Ala Gly 1700 1705 1710 Lys Thr Cys Gly Ile Cys Gly Lys Tyr Asp Ala Glu Cys Glu Gln 1715 1720 1725 Glu Tyr Arg Met Pro Asn Gly Tyr Leu Ala Lys Asn Ala Val Ser 1730 1735 1740 Phe Gly His Ser Trp Ile Leu Glu Glu Ala Pro Cys Arg Gly Ala 1745 1750 1755 Cys Lys Leu His Arg Ser Phe Val Lys Leu Glu Lys Thr Val Gln 1760 1765 1770 Leu Ala Gly Val Asp Ser Lys Cys Tyr Ser Thr Glu Pro Val Leu 1775 1780 1785 Arg Cys Ala Lys Gly Cys Ser Ala Thr Lys Thr Thr Pro Val Thr 1790 1795 1800 Val Gly Phe His Cys Leu Pro Ala Asp Ser Ala Asn Ser Leu Thr 1805 1810 1815 Asp Lys Gln Met Lys Tyr Asp Gln Lys Ser Glu Asp Met Gln Asp 1820 1825 1830 Thr Val Asp Ala His Thr Thr Cys Ser Cys Glu Asn Glu Glu Cys 1835 1840 1845 Ser Thr 1850 <210> 107 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 107 Ala Asp Thr Tyr Phe Asp Asn Tyr Arg 1 5 <210> 108 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 108 Ala Glu Phe Gly Thr Glu Pro Asp Ala Lys 1 5 10 <210> 109 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 109 Ala Glu Tyr Pro Thr Tyr Lys 1 5 <210> 110 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 110 Ala Thr Gly Glu Ile Phe Val Val Asn Ser Pro Arg 1 5 10 <210> 111 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 111 Ala Val Glu Ile Gln Gly Glu Val Gln Thr Arg 1 5 10 <210> 112 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 112 Ala Val Ile Phe Glu Thr Arg 1 5 <210> 113 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 113 Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 114 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 114 Glu Ala Leu Gln Pro Ile His Asp Leu Ala Asp Glu Ala Ile Ser Arg 1 5 10 15 <210> 115 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 115 Glu Glu Thr Glu Ile Val Val Gly Arg 1 5 <210> 116 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 116 Glu Leu Pro Thr Glu Thr Pro Leu Val Ser Ala Tyr Leu Lys 1 5 10 <210> 117 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 117 Phe Asp Ile Asp Pro Gly Phe Asn Ser Arg 1 5 10 <210> 118 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 118 Phe Glu Tyr Ser Ser Gly Arg 1 5 <210> 119 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 119 Gly Thr Thr Ala Phe Ser Tyr Lys 1 5 <210> 120 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 120 Ile Ala Asn Ala Asp Asn Leu Glu Ser Ile 1 5 10 <210> 121 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 121 Ile Leu Ala Asp Gln Ser Leu Pro Pro Glu Val Arg 1 5 10 <210> 122 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 122 Ile Leu Gly Gln Glu Val Ala Phe Ile Asn Ile Asn Lys 1 5 10 <210> 123 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 123 Ile Gln Leu Glu Ile Gln Ala Gly Ser Arg 1 5 10 <210> 124 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 124 Leu Glu Ile Ser Gly Leu Pro Glu Asn Ala Tyr Leu Leu Lys 1 5 10 <210> 125 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 125 Leu Gly Tyr Ser Ser Val Val Asn Arg 1 5 <210> 126 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 126 Leu Ile Gln Ile Leu Ala Asp Gln Ser Leu Pro Pro Glu Val Arg 1 5 10 15 <210> 127 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 127 Leu Lys Gln Ser Asp Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg 1 5 10 15 <210> 128 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 128 Leu Leu Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 15 <210> 129 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 129 Leu Pro Leu Ser Leu Pro Val Gly Pro Arg 1 5 10 <210> 130 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 130 Leu Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 131 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 131 Asn Asp Asp Leu Asn Tyr Ile Gln Thr Leu Leu 1 5 10 <210> 132 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 132 Asn Ile Gly Glu Leu Gly Val Glu Lys 1 5 <210> 133 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 133 Asn Ile Pro Phe Ala Glu Tyr Pro Thr Tyr Lys 1 5 10 <210> 134 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 134 Pro Ala Leu Ala Leu Ile Thr Thr Ile Ala Asn 1 5 10 <210> 135 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 135 Gln Gln Leu Thr Leu Val Glu Val Arg 1 5 <210> 136 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 136 Gln Ser Asp Ser Gly Thr Leu Ile Thr Asp Val Ser Ser Arg 1 5 10 <210> 137 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 137 Ser Ala Gly Ser Val Ala Asp Leu Val Glu Val Gly Ile Arg 1 5 10 <210> 138 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 138 Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 139 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 139 Ser Asp Leu Lys Pro Ser Leu Tyr 1 5 <210> 140 <211> 18 <212> PRT <213> Chicken (Gallus gallus) <400> 140 Thr Gly Gly Leu Gln Leu Val Val Tyr Ala Asp Thr Asp Ser Val Arg 1 5 10 15 Pro Arg <210> 141 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 141 Thr Pro Val Leu Ala Ala Phe Leu His Gly Ile Ser Asn Asn Lys 1 5 10 15 <210> 142 <211> 20 <212> PRT <213> Chicken (Gallus gallus) <400> 142 Thr Val Gln Gly Tyr Leu Ile Gln Ile Leu Ala Asp Gln Ser Leu Pro 1 5 10 15 Pro Glu Val Arg 20 <210> 143 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 143 Thr Val Gln Leu Ala Gly Val Asp Ser Lys 1 5 10 <210> 144 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 144 Thr Val Val Glu Pro Ala Asp Arg 1 5 <210> 145 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 145 Val Glu Ile Gln Gly Glu Val Gln Thr Arg 1 5 10 <210> 146 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 146 Val Gly Ala Thr Gly Glu Ile Phe Val Val Asn Ser Pro Arg 1 5 10 <210> 147 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 147 Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 <210> 148 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 148 Val Ser Thr Glu Leu Val Thr Gly Arg 1 5 <210> 149 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 149 Trp Leu Leu Ser Ala Val Ser Ala Ser Gly Thr Thr Glu Thr Leu Lys 1 5 10 15 <210> 150 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 150 Tyr Val Ile Gln Glu Asp Arg Lys 1 5 <210> 151 <211> 7875 <212> DNA <213> Chicken (Gallus gallus) <400> 151 atgggccctg tgcggctctt gctgctcttg ctgctgctca gcagtggtgt tctcacacag 60 gaaggaacac ctgaaaatgg aaacccagga tgttcaaaag atgcggcccg atttaaaagc 120 cttagaaaat atgtttactt atatgaagca gaacacaa gtgggatcac gggaacagca 180 gattctcgaa gcggttcaaa gatcacctgt aaagttgagt tggaggtacc acagctgtgc 240 cagttcatcc tgaggacaat gcattgctcc ctaagggaga catttggtgt tgacagtgag 300 agaagagcca tgctgaggaa gtcaaagaac tctgatgact ttgcaaatgc catgtccaaa 360 catgagctaa gattcagcac tcaggatgga acaaaagtta aactatatcc agagaaggat 420 gaacctctga atgtcctcaa tctcaagaga ggaattatct cagctctcct tgcaccaaca 480 gaacagagg aaaacataa aacaatttcc atggatactg tatatggaaa gtgtgacagt 540 gaggttgagt tcaaatccag aaggaagt gttgcagaag atatttcaat taacaggaac 600 ctgaaagcct gtgacaactt cagtccaatc agagatatg tcagccctgt tgccattgta 660 aaaggactaa acatcccact atctaccctt ctgagtagca ctcaatcctg tcactacagt 720 attgatgcaa agaaaaagca tatcagagat gttgtctgca gtgaaaaaca cctgtttctg 780 ccttcctcat acaaaatca gtatggtag atgacagaag tcaccagac actgaagctt 840 gagataatc frequency docagaat cctgatgag frequency 900 cttgcactgg aaagcacaga tgctaaattt tccaggcagg gtgatgctgt ttgaaaatt 960 cttcaggagc tgcagaaact tactgcctcc cagcagaacc agcagagagc aaaactctt 1020 tacaaatttg tttctggact tagagttg cacacagca ctcttggctc tcttgtacca 1080 aagatgatgg aaacttcaag ttcatcacg attcaggccc tgatcagtg tgggactcca 1140 gagtgttaca gtgcagtcct tcagatactg agaactggaa acgtaaatcc acttgtgta 1200 gacctggtca cgtataccct gggactctg ccttctccta ctccaagag aatccgggaa 1260 attctttaaca tggcccagta tcagccaagc agagctctct tttatggctt gagtcatgct 1320 gttaccaagt tctataatga gaagatt gtaacagagg aataacaga tgttgctgac 1380 ttcatgtat cactgctcgg cactgactgt ttggagatg ctgaacttac atatctcaca 1440 cttcgggcta ttggaacat gggtgcagta atggaaag ctaacccag cctgaaagct 1500 tctcttaaaa catgtatcag aaatcaagct gcatcacttt cagttcaaaa agcagccata 1560 caggcattcc ggaaaatgac cattacagaa gaggatcgtt cagcacttct gaaagaattc 1620 caggaagggg atgcacctac agataaacgt ctagcaacct atctcatact gatgaagaat 1680 ccttccccag ctgatctcgc aaagattatg agaatcctca caagggagaa gaacgagcaa 1740 gtgaaaagct ttgtcgcttc acacattgcc aacatcctag actctgatga agtaggcatt 1800 gaagatctaa aaagccatgt tgaagaagca ctgaaaggaa atgaggttcc aacagccaaa 1860 gatttcagaa aattctcaca aaattatcaa gtttccaaaa gagtttctgt acctggcctc 1920 aatcccatct ctgccaaagt agaaggaaat gtgatatttg atccaagcag ctatgttcct 1980 aaagaaacta tgctgaaaac caccctgaac ttgtatggtt ttggcccaag tgatatcttt 2040 gagcttggct tggatggaaa gggatttgaa ccaacactgg aagctttgtt tggagagaag 2100 ggatttttcc cagatactgc aagcaaggcc ctgtattggg ttgatggcaa agtgccagag 2160 caggtttcca aggctctctt tgactacttt ggttactccc acgatggcaa gcaggatcag 2220 gagatcacta aagcagtaat tcttaacctt gaaaaactga taaaagaatt gagcaagaag 2280 gaagctcctg aaggaagggc atttctgcga atcctgggag aagagcttgg gtacatgaaa 2340 ctcagtgatt tcaaattgct gggaagcgtg gctctagagt gcattaaaac tcttcagaga 2400 attcctgaaa taattgcaca agccatctcc aaaggtgttg acaaggactt atttgtccac 2460 tatatgttta tggacaatga gtttgaactc ccaactggag caggtttgca actgaagttt 2520 gccttgtctg gaatagtgac acctggggcc aaagtagctg tgaaacttca tcaaaaaagt 2580 atgcaagcag aactcattgc taaaccttca gtagcagttg agtttgtaac acatctagga 2640 ataaacatgc ctgaatttgc tagaagtggt gtggagatga attccaatat attccatgag 2700 tctggaattg aagcacatgt tagtgtgaaa gctggacagc tgaaattcag cattcctgcc 2760 ccgaagaccc caacaaaact cctcagtatc agcaacacac ttcatttggt gtctccagcc 2820 aaaactgaag agattccacc tctgattgag aaccgagaat tctcaacttc gtgcaagcct 2880 ttcatttctg gtctaaattt ctgcactaaa ttatgtact ctaatgccag ttccatggag 2940 gcagctccat attatccctt gactggagaa accagatttg aagttgaaat agtgtccaca 3000 ggggaagtga aagaatactc tgcaagtgca aactatgatc tgcagagaga gggaactgac 3060 ctggtagaca cattaaagtt tgcggtacaa gcagaaggtg taaagcagca tgaagccaca 3120 ctaaccttta agtacaatag agacaggaag attctgacca gcgacgtctc cattccagat 3180 gttgatgttg actttggtac taacttcaga atcactgatg aatctgtttc tgggaagaaa 3240 gcatatatct tcgttataga ctttaataac aagaagattt ctgaagtcac tctcactgga 3300 caaataagat atgctgggaat agaagaagca atgctgagag gcaccgtttc tattcctcgt 3360 ctgcaaactg aacttaaaac tgaagcactg gttaattatt cacccaccaa aggatacctt 3420 cagatgagct catctgtagg aacccatggg aacacagttt caaaaagagt tcttctcaga 3480 tatgattctg aaaaagctga gctagagtgg aattcaggtg ccactgctgc tgtgggaaga 3540 atgtcttctg ccttccaagt tgacttttca gactactcaa agactttaga gaagtatgcc 3600 aacgaacttc tggatcggaa agtcgctctt acagatatga caatgcgaca tattgtatca 3660 caatttattg tggcaaccaa cacctggcta caaaaggcat caaaagatgt cccctatgcc 3720 cagactctac aagccaaact aagtggactg caggaactga acattcagaa gattaaactg 3780 cctgttatca ccattcctga agaacttttc ctgaaaagtg aaggccggat caaatatagc 3840 ttcaataaga acagttttct attaatatt ccattaccat ttggtggaag atcgtcccat 3900 gacataagag tgccacagac tgttaaaaca cctcgtctag tatagagtc tatgggaata 3960 aacataccat cacaggaata cagaatgcca acatttactg ttccagaatc ctatcctctt 4020 cttgtgcctt tatttggtgc tttagaggcc tccgccagtg tgcacagcaa ctattacaac 4080 tggacagcag catacacttt gacaatagc agcacagaga aaacagccag aattggaact 4140 acttatgctg tgaatgctga ttctgttttt gagctactat cctacaacat gaaaggttct 4200 ggagaggcat cttctagtag aaatggattc acttgtgcat atgaaaatca tctgaagcac 4260 agactcttaa cttcagattt taaaatgtct aggacaaaga gttatgaacc tacatcagtt 4320 tcaaactgta ccatatttct aatggcatcc agtgctctgg gtcctcagct ttcattttcc 4380 agtgatgttg tttctgaaaa gacaaataac atgaatatta ataatgtcag gatagaaggg 4440 caactggaag tggcttctgt gtttgcaaga agtgtttaca ctatgtcaag ctcatacaat 4500 gaaaagagac gagttttaga agggaagtca aatctgaggt tggattcttc ttaccttcaa 4560 gctaccaatc atctatccgg tagatacact gatggtgtat tttccattac ttcagcttct 4620 gatgtacaaa atggactatt aaagaacaca gcttcactga agtatgaaaa tagccagctg 4680 aaaataacat ctgaaacaaa tggaaggtat ctacatctcg cagctgtcaa taaacttgaa 4740 ttccttttgt caaagaagat ggcagcactt cgttctgagt accaagccac ttacaagcaa 4800 acccaatgtt atgccttgtt cgcaggttct ctcaattccc aggatcttgt tttcaacact 4860 gatttctctc tgactgatca aaggaatcga gctgcacata agtcatcact caatgttaat 4920 cagtatggtc tagccagcag tgcaactaca aatgtacagt ttagtccact gacaatgcag 4980 agtgaaatga atgctaaact tgatacctct ggaggctctg tgtcactgtc atcatctggg 5040 cgctatggaa aaaacaatgc aaaattcaat gtaggtggaa gagtgagctt aacggaaata 5100 acgctgggaa gcgaataatca gagtacaatt ctgggtatgg acataaca tgtcttaaac 5160 ttcagaatta aagaagg actcaagtttt tcaatatt tgcaagggtc attaaagg 5220 attaagctgg agtacacaa tgacttgaat attcctggct tatcctaac atttgttca 5280 aagttagaca acagcttcag ctttgacaag ttccacaagc atgttttga ccttcagctg 5340 cagcccagat cacttacagc taagctgaac ataatatta atacacca aactgaagtt 5400 tccaacaag cagaactgct ccttgagcct ctgaagctga acttgggtgg caatgtgaga 5460 gcagcctatg gaacagatga agtaagacat acctacgcca ttacatatgc tgatctact 5520 gcaaacttta aaacagacac agttgcaaat gtccaaggtg cagcagtgag tcacagagtt 5580 aatctgaatg tggcaggact ggcttcctcc attackatga acacaattg tgattccaaa 5640 tctctccgtt tcagcaatgc tctgcgttcc actatgccc cattcactat cacggctgat 5700 gttcacacca acggtaatgg gaagctgatt gctctgggtg aacatacagg agaccttac 5760 agcaaaatcc tgttcaagc agaacctt gcttcactt tctccactga tccagagga 5820 5880 catatgcttt ttactccatc agagcagtcg agtgcttgga aattgaaaag tcagctaaac 5940 aacaacatat attcacaaga tatcaatgct tacaatgatg cagaaaagat tggtgtggaa 6000 cttagtggaa gagctttagc agatctctct gtggtggata cagcaatcag actaccattc 6060 atgtctgaag aagttaatgt aattgatgta ttaggcctca gggacagtgt gtcagagcct 6120 caagaattca gcatctctgg ctctgtgaag tatgacaaaa ataaagatat gcatgttat 6180 aacctaccat tcttggaaca ctttccagtc tactttgaac aaatcagagg tgccattcta 6240 tccacactgc aggctgtaca gaattacctg aaaaacattg acgtagatca atatatgaaa 6300 aaatacaagg caactttaga tgaattccca cagcacctta atgattacat ggacaaatta 6360 gatctgaaag gcagagctag caccataaaa actaatttga ttgctttcac gaaggactat 6420 agaatacat ctgatgatct cgaaattat ctggaaaaag ccctggataa tcttcaagaa 6480 atactgctcc agcttcaagt ttatcttgtg caaatagagc agtacatcaa agagaattac 6540 gatcagtttg acattaatgc acttattgca caacttcttg acaaaatagt tgaaaaaatg 6600 acagctctag atgaaaaata taagataaga gtgactgtag ttgacactat tcagaagtta 6660 caattttttt taaatcaata ttaccccagc aacattggaa gcaactat gacttggatt 6720 aaaatatag atgatgagta taggatcaca ggtagaataa aggagaacct agaacagctc 6780 aagattcaga ttcagaacat tgatatcaga agctttgcag aaaatttgaa aaggaagatt 6840 aaaatattg atgttaaaca actattagaa aaattaaagc gttcattacc attaaaaaa 6900 atgaaggaag ttcttgaaca aatcaaagac tttattctga gttggatgga ggagtacgaa 6960 gtgtctgaga agatcagtgc tttccgaggt catatgcata aactgattgt aaaatatgaa 7020 attgataagc atgtgtattt tttattggac agaatgatag aactacttaa ccagtacaga 7080 ataagagaaa cggtacggaa aatgacgacc tacctaagaa aaattgacgt gaagacatgc 7140 tttgacaaaa ttgtgtcttt aattgatgat gctgtgaaga aagtgcaaac ctttgattat 7200 gaaatgatga taaagaaact caacaaattc cttgacatga ttataaagaa actcaaatct 7260 tttgactata accagtttgt tgatgacaca aataacaaaa tccaagaaat tatacagaaa 7320 ataaatgagg aactcagaaa tctagaactg ccacagaaag cagaagcatt gaaacagtat 7380 atgagagatt ttaatgctgt agtttcaaaa tacgtagaac aactaaggga caccaagctt 7440 gtcgctataa ttaactggct caaggagctc atcgactcaa caacatttac taatctgaaa 7500 gccaaagtaa atgagcatct ggaaggtctg cgagagagaa tttctgacat ggatatcgcc 7560 aaggaatttg aatggtatct tcaaaagata agccagttct acaattctgt tgtcatatac 7620 atttctgaac agtggaacat agcttttaaa aaaatcgtta ctttggctga gaagtatgac 7680 ctaaaaaatt gggctgaaaa tttaaaccag ttcattgaaa caggatttaa agtccctgaa 7740 ataagaacag ttatagtcac tatacctgcc tttgaattca gtcttcgaag tcttcgggaa 7800 gcaactttcc gaacaccgga cttcattgtt ccactgactg atctgaaaat cccctcctat 7860 gaaataaata ttagg 7875 <210> 152 <211> 2625 <212> PRT <213> Chicken (Gallus gallus) <400> 152 Met Gly Pro Val Arg Leu Leu Leu Leu Leu Leu Leu Leu Ser Ser Gly 1 5 10 15 Val Leu Thr Gln Glu Gly Thr Pro Glu Asn Gly Asn Pro Gly Cys Ser 20 25 30 Lys Asp Ala Ala Arg Phe Lys Ser Leu Arg Lys Tyr Val Tyr Leu Tyr 35 40 45 Glu Ala Glu Thr Ser Ser Gly Ile Thr Gly Thr Ala Asp Ser Arg Ser 50 55 60 Gly Ser Lys Ile Thr Cys Lys Val Glu Leu Glu Val Pro Gln Leu Cys 65 70 75 80 Gln Phe Ile Leu Arg Thr Met His Cys Ser Leu Arg Glu Thr Phe Gly 85 90 95 Val Asp Ser Glu Arg Arg Ala Met Leu Arg Lys Ser Lys Asn Ser Asp 100 105 110 Asp Phe Ala Asn Ala Met Ser Lys His Glu Leu Arg Phe Ser Thr Gln 115 120 125 Asp Gly Thr Lys Val Lys Leu Tyr Pro Glu Lys Asp Glu Pro Leu Asn 130 135 140 Val Leu Asn Leu Lys Arg Gly Ile Ile Ser Ala Leu Leu Ala Pro Thr 145 150 155 160 Glu Thr Glu Glu Asn Ile Lys Thr Ile Ser Met Asp Thr Val Tyr Gly 165 170 175 Lys Cys Asp Ser Glu Val Glu Phe Lys Ser Arg Arg Gly Ser Val Ala 180 185 190 Glu Asp Ile Ser Ile Asn Arg Asn Leu Lys Ala Cys Asp Asn Phe Ser 195 200 205 Pro Ile Arg Asp Tyr Val Ser Pro Val Ala Ile Val Lys Gly Leu Asn 210 215 220 Ile Pro Leu Ser Thr Leu Leu Ser Ser Thr Gln Ser Cys His Tyr Ser 225 230 235 240 Ile Asp Ala Lys Lys Lys His Ile Arg Asp Val Val Cys Ser Glu Lys 245 250 255 His Leu Phe Leu Pro Ser Ser Tyr Lys Asn Gln Tyr Gly Met Met Thr 260 265 270 Glu Val Asn Gln Thr Leu Lys Leu Glu Asp Asn Gln Arg Met Asn Asn 275 280 285 Arg Asn Pro Asp Gly Asp Glu Leu Glu Glu Lys Gly Leu Ala Leu Glu 290 295 300 Ser Thr Asp Ala Lys Phe Ser Arg Gln Gly Asp Ala Val Leu Lys Ile 305 310 315 320 Leu Gln Glu Leu Gln Lys Leu Thr Ala Ser Gln Gln Asn Gln Gln Arg 325 330 335 Ala Lys Leu Phe Tyr Lys Phe Val Ser Gly Leu Arg Ser Leu His Asn 340 345 350 Ser Thr Leu Gly Ser Leu Val Pro Lys Met Met Glu Thr Ser Ser Ser 355 360 365 Ile Thr Ile Gln Ala Leu Ile Gln Cys Gly Thr Pro Glu Cys Tyr Ser 370 375 380 Ala Val Leu Gln Ile Leu Arg Thr Gly Asn Val Asn Pro Leu Val Val 385 390 395 400 Asp Leu Val Thr Tyr Thr Leu Gly Leu Leu Pro Ser Pro Thr Pro Lys 405 410 415 Arg Ile Arg Glu Ile Leu Asn Met Ala Gln Tyr Gln Pro Ser Arg Ala 420 425 430 Ser Phe Tyr Gly Leu Ser His Ala Val Thr Lys Phe Tyr Asn Glu Lys 435 440 445 Met Ile Val Thr Glu Glu Ile Thr Asp Val Ala Asp Phe Met Val Ser 450 455 460 Leu Leu Gly Thr Asp Cys Ser Gly Asp Ala Glu Leu Thr Tyr Leu Thr 465 470 475 480 Leu Arg Ala Ile Gly Asn Met Gly Ala Val Met Glu Lys Ala Lys Pro 485 490 495 Ser Leu Lys Ala Ser Leu Lys Thr Cys Ile Arg Asn Gln Ala Ala Ser 500 505 510 Leu Ser Val Gln Lys Ala Ala Ile Gln Ala Phe Arg Lys Met Thr Ile 515 520 525 Thr Glu Glu Asp Arg Ser Ala Leu Leu Lys Glu Phe Gln Glu Gly Asp 530 535 540 Ala Pro Thr Asp Lys Arg Leu Ala Thr Tyr Leu Ile Leu Met Lys Asn 545 550 555 560 Pro Ser Pro Ala Asp Leu Ala Lys Ile Met Arg Ile Leu Thr Arg Glu 565 570 575 Lys Asn Glu Gln Val Lys Ser Phe Val Ala Ser His Ile Ala Asn Ile 580 585 590 Leu Asp Ser Asp Glu Val Gly Ile Glu Asp Leu Lys Ser His Val Glu 595 600 605 Glu Ala Leu Lys Gly Asn Glu Val Pro Thr Ala Lys Asp Phe Arg Lys 610 615 620 Phe Ser Gln Asn Tyr Gln Val Ser Lys Arg Val Ser Val Pro Gly Leu 625 630 635 640 Asn Pro Ile Ser Ala Lys Val Glu Gly Asn Val Ile Phe Asp Pro Ser 645 650 655 Ser Tyr Val Pro Lys Glu Thr Met Leu Lys Thr Thr Leu Asn Leu Tyr 660 665 670 Gly Phe Gly Pro Ser Asp Ile Phe Glu Leu Gly Leu Asp Gly Lys Gly 675 680 685 Phe Glu Pro Thr Leu Glu Ala Leu Phe Gly Glu Lys Gly Phe Phe Pro 690 695 700 Asp Thr Ala Ser Lys Ala Leu Tyr Trp Val Asp Gly Lys Val Pro Glu 705 710 715 720 Gln Val Ser Lys Ala Leu Phe Asp Tyr Phe Gly Tyr Ser His Asp Gly 725 730 735 Lys Gln Asp Gln Glu Ile Thr Lys Ala Val Ile Leu Asn Leu Glu Lys 740 745 750 Leu Ile Lys Glu Leu Ser Lys Lys Glu Ala Pro Glu Gly Arg Ala Phe 755 760 765 Leu Arg Ile Leu Gly Glu Glu Leu Gly Tyr Met Lys Leu Ser Asp Phe 770 775 780 Lys Leu Leu Gly Ser Val Ala Leu Glu Cys Ile Lys Thr Leu Gln Arg 785 790 795 800 Ile Pro Glu Ile Ile Ala Gln Ala Ile Ser Lys Gly Val Asp Lys Asp 805 810 815 Leu Phe Val His Tyr Met Phe Met Asp Asn Glu Phe Glu Leu Pro Thr 820 825 830 Gly Ala Gly Leu Gln Leu Lys Phe Ala Leu Ser Gly Ile Val Thr Pro 835 840 845 Gly Ala Lys Val Ala Val Lys Leu His Gln Lys Ser Met Gln Ala Glu 850 855 860 Leu Ile Ala Lys Pro Ser Val Ala Val Glu Phe Val Thr His Leu Gly 865 870 875 880 Ile Asn Met Pro Glu Phe Ala Arg Ser Gly Val Glu Met Asn Ser Asn 885 890 895 Ile Phe His Glu Ser Gly Ile Glu Ala His Val Ser Val Lys Ala Gly 900 905 910 Gln Leu Lys Phe Ser Ile Pro Ala Pro Lys Thr Pro Thr Lys Leu Leu 915 920 925 Ser Ile Ser Asn Thr Leu His Leu Val Ser Pro Ala Lys Thr Glu Glu 930 935 940 Ile Pro Pro Leu Ile Glu Asn Arg Glu Phe Ser Thr Ser Cys Lys Pro 945 950 955 960 Phe Ile Ser Gly Leu Asn Phe Cys Thr Lys Leu Leu Tyr Ser Asn Ala 965 970 975 Ser Ser Met Glu Ala Ala Pro Tyr Tyr Pro Leu Thr Gly Glu Thr Arg 980 985 990 Phe Glu Val Glu Ile Val Ser Thr Gly Glu Val Lys Glu Tyr Ser Ala 995 1000 1005 Ser Ala Asn Tyr Asp Leu Gln Arg Glu Gly Thr Asp Leu Val Asp 1010 1015 1020 Thr Leu Lys Phe Ala Val Gln Ala Glu Gly Val Lys Gln His Glu 1025 1030 1035 Ala Thr Leu Thr Phe Lys Tyr Asn Arg Asp Arg Lys Ile Leu Thr 1040 1045 1050 Ser Asp Val Ser Ile Pro Asp Val Asp Val Asp Phe Gly Thr Asn 1055 1060 1065 Phe Arg Ile Thr Asp Glu Ser Val Ser Gly Lys Lys Ala Tyr Ile 1070 1075 1080 Phe Val Ile Asp Phe Asn Asn Lys Lys Ile Ser Glu Val Thr Leu 1085 1090 1095 Thr Gly Gln Ile Arg Tyr Ala Gly Ile Glu Glu Ala Met Leu Arg 1100 1105 1110 Gly Thr Val Ser Ile Pro Arg Leu Gln Thr Glu Leu Lys Thr Glu 1115 1120 1125 Ala Leu Val Asn Tyr Ser Pro Thr Lys Gly Tyr Leu Gln Met Ser 1130 1135 1140 Ser Ser Val Gly Thr His Gly Asn Thr Val Ser Lys Arg Val Leu 1145 1150 1155 Leu Arg Tyr Asp Ser Glu Lys Ala Glu Leu Glu Trp Asn Ser Gly 1160 1165 1170 Ala Thr Ala Ala Val Gly Arg Met Ser Ser Ala Phe Gln Val Asp 1175 1180 1185 Phe Ser Asp Tyr Ser Lys Thr Leu Glu Lys Tyr Ala Asn Glu Leu 1190 1195 1200 Leu Asp Arg Lys Val Ala Leu Thr Asp Met Thr Met Arg His Ile 1205 1210 1215 Val Ser Gln Phe Ile Val Ala Thr Asn Thr Trp Leu Gln Lys Ala 1220 1225 1230 Ser Lys Asp Val Pro Tyr Ala Gln Thr Leu Gln Ala Lys Leu Ser 1235 1240 1245 Gly Leu Gln Glu Leu Asn Ile Gln Lys Ile Lys Leu Pro Val Ile 1250 1255 1260 Thr Ile Pro Glu Glu Leu Phe Leu Lys Ser Glu Gly Arg Ile Lys 1265 1270 1275 Tyr Ser Phe Asn Lys Asn Ser Phe Leu Ile Asn Ile Pro Leu Pro 1280 1285 1290 Phe Gly Gly Arg Ser Ser His Asp Ile Arg Val Pro Gln Thr Val 1295 1300 1305 Lys Thr Pro Arg Leu Val Ile Glu Ser Met Gly Ile Asn Ile Pro 1310 1315 1320 Ser Gln Glu Tyr Arg Met Pro Thr Phe Thr Val Pro Glu Ser Tyr 1325 1330 1335 Pro Leu Leu Val Pro Leu Phe Gly Ala Leu Glu Ala Ser Ala Ser 1340 1345 1350 Val His Ser Asn Tyr Tyr Asn Trp Thr Ala Ala Tyr Thr Leu Thr 1355 1360 1365 Asn Ser Ser Thr Glu Lys Thr Ala Arg Ile Gly Thr Thr Tyr Ala 1370 1375 1380 Val Asn Ala Asp Ser Val Phe Glu Leu Leu Ser Tyr Asn Met Lys 1385 1390 1395 Gly Ser Gly Glu Ala Ser Ser Ser Arg Asn Gly Phe Thr Cys Ala 1400 1405 1410 Tyr Glu Asn His Leu Lys His Arg Leu Leu Thr Ser Asp Phe Lys 1415 1420 1425 Met Ser Arg Thr Lys Ser Tyr Glu Pro Thr Ser Val Ser Asn Cys 1430 1435 1440 Thr Ile Phe Leu Met Ala Ser Ser Ala Leu Gly Pro Gln Leu Ser 1445 1450 1455 Phe Ser Ser Asp Val Val Ser Glu Lys Thr Asn Asn Met Asn Ile 1460 1465 1470 Asn Asn Val Arg Ile Glu Gly Gln Leu Glu Val Ala Ser Val Phe 1475 1480 1485 Ala Arg Ser Val Tyr Thr Met Ser Ser Ser Tyr Asn Glu Lys Arg 1490 1495 1500 Arg Val Leu Glu Gly Lys Ser Asn Leu Arg Leu Asp Ser Ser Tyr 1505 1510 1515 Leu Gln Ala Thr Asn His Leu Ser Gly Arg Tyr Thr Asp Gly Val 1520 1525 1530 Phe Ser Ile Thr Ser Ala Ser Asp Val Gln Asn Gly Leu Leu Lys 1535 1540 1545 Asn Thr Ala Ser Leu Lys Tyr Glu Asn Ser Gln Leu Lys Ile Thr 1550 1555 1560 Ser Glu Thr Asn Gly Arg Tyr Leu His Leu Ala Ala Val Asn Lys 1565 1570 1575 Leu Glu Phe Leu Leu Ser Lys Lys Met Ala Ala Leu Arg Ser Glu 1580 1585 1590 Tyr Gln Ala Thr Tyr Lys Gln Thr Gln Cys Tyr Ala Leu Phe Ala 1595 1600 1605 Gly Ser Leu Asn Ser Gln Asp Leu Val Phe Asn Thr Asp Phe Ser 1610 1615 1620 Leu Thr Asp Gln Arg Asn Arg Ala Ala His Lys Ser Ser Leu Asn 1625 1630 1635 Val Asn Gln Tyr Gly Leu Ala Ser Ser Ala Thr Thr Asn Val Gln 1640 1645 1650 Phe Ser Pro Leu Thr Met Gln Ser Glu Met Asn Ala Lys Leu Asp 1655 1660 1665 Thr Ser Gly Gly Ser Val Ser Leu Ser Ser Ser Gly Arg Tyr Gly 1670 1675 1680 Lys Asn Asn Ala Lys Phe Asn Val Gly Gly Arg Val Ser Leu Thr 1685 1690 1695 Glu Ile Thr Leu Gly Ser Glu Tyr Gln Ser Thr Ile Leu Gly Met 1700 1705 1710 Asp Asn Lys His Val Leu Asn Phe Arg Ile Asn Lys Glu Gly Leu 1715 1720 1725 Lys Phe Ser Asn Asn Leu Gln Gly Ser Leu Lys Glu Ile Lys Leu 1730 1735 1740 Glu Tyr Thr Asn Asp Leu Asn Ile Pro Gly Leu Ser Leu Thr Phe 1745 1750 1755 Val Ser Lys Leu Asp Asn Ser Phe Ser Phe Asp Lys Phe His Lys 1760 1765 1770 His Val Phe Asp Leu Gln Leu Gln Pro Arg Ser Leu Thr Ala Lys 1775 1780 1785 Leu Asn Asn Asn Ile Lys Tyr Thr Lys Thr Glu Val Ser Asn Lys 1790 1795 1800 Ala Glu Leu Leu Leu Glu Pro Leu Lys Leu Asn Leu Gly Gly Asn 1805 1810 1815 Val Arg Ala Ala Tyr Gly Thr Asp Glu Val Arg His Thr Tyr Ala 1820 1825 1830 Ile Thr Tyr Ala Asp Leu Thr Ala Asn Phe Lys Thr Asp Thr Val 1835 1840 1845 Ala Asn Val Gln Gly Ala Ala Val Ser His Arg Val Asn Leu Asn 1850 1855 1860 Val Ala Gly Leu Ala Ser Ser Ile Thr Met Asn Thr Asn Cys Asp 1865 1870 1875 Ser Lys Ser Leu Arg Phe Ser Asn Ala Leu Arg Ser Thr Met Ala 1880 1885 1890 Pro Phe Thr Ile Thr Ala Asp Val His Thr Asn Gly Asn Gly Lys 1895 1900 1905 Leu Ile Ala Leu Gly Glu His Thr Gly Asp Leu Tyr Ser Lys Ile 1910 1915 1920 Leu Phe Lys Ala Glu Pro Leu Ala Phe Thr Phe Ser His Asp Tyr 1925 1930 1935 Arg Gly Ser Thr Ser His Ser Phe Lys Ser Met Arg Arg Tyr Ser 1940 1945 1950 Thr Gln Leu Asp Asn Lys Phe His Met Leu Phe Thr Pro Ser Glu 1955 1960 1965 Gln Ser Ser Ala Trp Lys Leu Lys Ser Gln Leu Asn Asn Asn Ile 1970 1975 1980 Tyr Ser Gln Asp Ile Asn Ala Tyr Asn Asp Ala Glu Lys Ile Gly 1985 1990 1995 Val Glu Leu Ser Gly Arg Ala Leu Ala Asp Leu Ser Val Val Asp 2000 2005 2010 Thr Ala Ile Arg Leu Pro Phe Met Ser Glu Glu Val Asn Val Ile 2015 2020 2025 Asp Val Leu Gly Leu Arg Asp Ser Val Ser Glu Pro Gln Glu Phe 2030 2035 2040 Ser Ile Ser Gly Ser Val Lys Tyr Asp Lys Asn Lys Asp Met His 2045 2050 2055 Val Ile Asn Leu Pro Phe Leu Glu His Phe Pro Val Tyr Phe Glu 2060 2065 2070 Gln Ile Arg Gly Ala Ile Leu Ser Thr Leu Gln Ala Val Gln Asn 2075 2080 2085 Tyr Leu Lys Asn Ile Asp Val Asp Gln Tyr Met Lys Lys Tyr Lys 2090 2095 2100 Ala Thr Leu Asp Glu Phe Pro Gln His Leu Asn Asp Tyr Met Asp 2105 2110 2115 Lys Leu Asp Leu Lys Gly Arg Ala Ser Thr Ile Lys Thr Asn Leu 2120 2125 2130 Ile Ala Phe Thr Lys Asp Tyr Arg Ile Thr Ser Asp Asp Leu Glu 2135 2140 2145 Ile Ile Leu Glu Lys Ala Leu Asp Asn Leu Gln Glu Ile Leu Leu 2150 2155 2160 Gln Leu Gln Val Tyr Leu Val Gln Ile Glu Gln Tyr Ile Lys Glu 2165 2170 2175 Asn Tyr Asp Gln Phe Asp Ile Asn Ala Leu Ile Ala Gln Leu Leu 2180 2185 2190 Asp Lys Ile Val Glu Lys Met Thr Ala Leu Asp Glu Lys Tyr Lys 2195 2200 2205 Ile Arg Val Thr Val Val Asp Thr Ile Gln Lys Leu Gln Phe Phe 2210 2215 2220 Leu Asn Gln Tyr Tyr Pro Ser Asn Ile Gly Ser Asn Thr Met Thr 2225 2230 2235 Trp Ile Lys Asn Ile Asp Asp Glu Tyr Arg Ile Thr Gly Arg Ile 2240 2245 2250 Lys Glu Asn Leu Glu Gln Leu Lys Ile Gln Ile Gln Asn Ile Asp 2255 2260 2265 Ile Arg Ser Phe Ala Glu Asn Leu Lys Arg Lys Ile Lys Ile Ile 2270 2275 2280 Asp Val Lys Gln Leu Leu Glu Lys Leu Lys Arg Ser Leu Pro Ile 2285 2290 2295 Lys Met Lys Glu Val Leu Glu Gln Ile Lys Asp Phe Ile Leu 2300 2305 2310 Ser Trp Met Glu Glu Tyr Glu Val Ser Glu Lys Ile Ser Ala Phe 2315 2320 2325 Arg Gly His Met His Lys Leu Ile Val Lys Tyr Glu Ile Asp Lys 2330 2335 2340 His Val Tyr Phe Leu Leu Asp Arg Met Ile Glu Leu Leu Asn Gln 2345 2350 2355 Tyr Arg With Arg Glu Thr Val Arg Lys Met Thr Thr Tyr Leu Arg 2360 2365 2370 Lys Ile Asp Will Lys Thr Cys Phe Asp Lys Ile Will Ser Leu Ile 2375 2380 2385 Asp Asp Ala Val Lys Lys Val Gln Thr Phe Asp Tyr Glu Met Met 2390 2395 2400 Lys Lys Leu Asn Lys Phe Leu Asp Met Lys Lys Leu 2405 2410 2415 Lys Ser Phe Asp Tyr Asn Gln Phe Val Asp Asp Thr Asn Asn Lys 2420 2425 2430 Gln Glu Ile Ile Gln Lys Ile Asn Glu Glu Leu Arg Asn Leu 2435 2440 2445 Glu Leu Pro Gln Lys Ala Glu Ala Leu Lys Gln Tyr Met Arg Asp 2450 2455 2460 Phe Asn Ala Val Val Ser Lys Tyr Val Glu Gln Leu Arg Asp Thr 2465 2470 2475 Lys Leu Val Ala Ile Ile Asn Trp Leu Lys Glu Leu Ile Asp Ser 2480 2485 2490 Thr Thr Phe Thr Asn Leu Lys Ala Lys Val Asn Glu His Leu Glu 2495 2500 2505 Gly Leu Arg Glu Arg Ile Ser Asp Met Asp Ile Ala Lys Glu Phe 2510 2515 2520 Glu Trp Tyr Leu Gln Lys Ile Ser Gln Phe Tyr Asn Ser Val Val 2525 2530 2535 Ile Tyr Ile Ser Glu Gln Trp Asn Ile Ala Phe Lys Lys Ile Val 2540 2545 2550 Thr Leu Ala Glu Lys Tyr Asp Leu Lys Asn Trp Ala Glu Asn Leu 2555 2560 2565 Asn Gln Phe Ile Glu Thr Gly Phe Lys Val Pro Glu Ile Arg Thr 2570 2575 2580 Val Ile Val Thr Ile Pro Ala Phe Glu Phe Ser Leu Arg Ser Leu 2585 ​​2590 2595 Arg Glu Ala Thr Phe Arg Thr Pro Asp Phe Ile Val Pro Leu Thr 2600 2605 2610 Asp Leu Lys Ile Pro Ser Tyr Glu Ile Asn Ile Arg 2615 2620 2625 <210> 153 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 153 Ala Ala Tyr Gly Thr Asp Glu Val Arg 1 5 <210> 154 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 154 Ala Glu Leu Glu Trp Asn Ser Gly Ala Thr Ala Ala Val Gly Arg 1 5 10 15 <210> 155 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 155 Ala Glu Leu Leu Leu Glu Pro Leu Lys 1 5 <210> 156 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 156 Ala Glu Pro Leu Ala Phe Thr Phe 1 5 <210> 157 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 157 Ala Ile Thr Tyr Ala Asp Leu Thr Ala Asn Phe Lys 1 5 10 <210> 158 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 158 Ala Leu Ala Asp Leu Ser Val Val Asp Thr Ala Ile Arg 1 5 10 <210> 159 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 159 Ala Leu Ser Gly Ile Val Thr Pro Gly Ala Lys 1 5 10 <210> 160 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 160 Ala Ser Phe Tyr Gly Leu Ser His Ala Val Thr Lys 1 5 10 <210> 161 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 161 Ala Thr Leu Asp Glu Phe Pro Gln 1 5 <210> 162 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 162 Ala Val Ile Leu Asn Leu Glu Lys 1 5 <210> 163 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 163 Ala Tyr Thr Phe Val Ile Asp Phe Asn Asn Lys 1 5 10 <210> 164 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 164 Asp Glu Pro Leu Asn Val Leu Asn Leu Lys 1 5 10 <210> 165 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 165 Asp Phe Asn Ala Val Val Ser Lys 1 5 <210> 166 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 166 Asp Leu Gln Leu Gln Pro Arg 1 5 <210> 167 <211> 16 <212> PRT <213> Chicken (Gallus gallus) <400> 167 Asp Ser Val Ser Glu Pro Gln Glu Phe Ser Ile Ser Gly Ser Val Lys 1 5 10 15 <210> 168 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 168 Asp Val Pro Tyr Ala Gln Thr Leu Gln Ala Lys 1 5 10 <210> 169 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 169 Asp Tyr Val Ser Pro Val Ala Ile Val Lys 1 5 10 <210> 170 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 170 Glu Phe Gln Glu Gly Asp Ala Pro Thr Asp Lys 1 5 10 <210> 171 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 171 Glu Gly Thr Asp Leu Val Asp Thr Leu Lys 1 5 10 <210> 172 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 172 Glu Leu Glu Trp Asn Ser Gly Ala Thr Ala Ala Val Gly Arg 1 5 10 <210> 173 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 173 Glu Thr Phe Gly Val Asp Ser Glu Arg 1 5 <210> 174 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 174 Glu Tyr Ser Ala Ser Ala Asn Tyr Asp Leu Gln Arg 1 5 10 <210> 175 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 175 Phe Ala Leu Ser Gly Ile Val Thr Pro Gly Ala Lys 1 5 10 <210> 176 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 176 Phe Ala Val Gln Ala Glu Gly Val Lys 1 5 <210> 177 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 177 Phe Glu Val Glu Ile Val Ser Thr Gly Glu Val Lys 1 5 10 <210> 178 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 178 Phe Ser Asn Asn Leu Gln Gly Ser Leu Lys 1 5 10 <210> 179 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 179 Phe Ser Gln Asn Tyr Gln Val Ser Lys 1 5 <210> 180 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 180 Gly Phe Glu Pro Thr Leu Glu Ala Leu Phe Gly Glu Lys 1 5 10 <210> 181 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 181 Gly Phe Phe Pro Asp Thr Ala Ser Lys 1 5 <210> 182 <211> 17 <212> PRT <213> Chicken (Gallus gallus) <400> 182 Gly Ile Ile Ser Ala Leu Leu Ala Pro Thr Glu Thr Glu Glu Asn Ile 1 5 10 15 Lys <210> 183 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 183 Gly Leu Ala Leu Glu Ser Thr Asp Ala Lys 1 5 10 <210> 184 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 184 Gly Ser Val Ala Glu Asp Ile Ser Ile Asn Arg 1 5 10 <210> 185 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 185 Ile Glu Gly Gln Leu Glu Val Ala Ser Val Phe Ala Arg 1 5 10 <210> 186 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 186 Ile Gly Val Glu Leu Ser Gly Arg 1 5 <210> 187 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 187 Ile Lys Leu Pro Val Ile Thr Ile Pro Glu Glu Leu Phe Leu Lys 1 5 10 15 <210> 188 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 188 Ile Leu Gln Glu Leu Gln Lys 1 5 <210> 189 <211> 20 <212> PRT <213> Chicken (Gallus gallus) <400> 189 Ile Leu Thr Ser Asp Val Ser Ile Pro Asp Val Asp Val Asp Phe Gly 1 5 10 15 Thr Asn Phe Arg 20 <210> 190 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 190 Ile Pro Glu Ile Ile Ala Gln Ala Ile Ser Lys 1 5 10 <210> 191 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 191 Ile Pro Ser Tyr Glu Ile Asn Ile Arg 1 5 <210> 192 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 192 Ile Ser Glu Val Thr Leu Thr Gly Gln Ile Arg 1 5 10 <210> 193 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 193 Ile Thr Asp Glu Ser Val Ser Gly Lys 1 5 <210> 194 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 194 Lys Phe Ser Gln Asn Tyr Gln Val Ser Lys 1 5 10 <210> 195 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 195 Lys Ile Ser Glu Val Thr Leu Thr Gly Gln Ile Arg 1 5 10 <210> 196 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 196 Leu Ala Pro Thr Glu Thr Glu Glu Asn Ile Lys 1 5 10 <210> 197 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 197 Leu Asp Asn Ser Phe Ser Phe Asp Lys 1 5 <210> 198 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 198 Leu Asp Ser Ser Tyr Leu Gln Ala Thr Asn His Leu Ser Gly Arg 1 5 10 15 <210> 199 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 199 Leu Asp Thr Ser Gly Gly Ser Val Ser Leu Ser Ser Ser Gly Arg 1 5 10 15 <210> 200 <211> 19 <212> PRT <213> Chicken (Gallus gallus) <400> 200 Leu Glu Tyr Thr Asn Asp Leu Asn Ile Pro Gly Leu Ser Leu Thr Phe 1 5 10 15 Val Ser Lys <210> 201 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 201 Leu Leu Thr Ser Asp Phe Lys 1 5 <210> 202 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 202 Leu Asn Leu Gly Gly Asn Val Arg 1 5 <210> 203 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 203 Leu Pro Val Ile Thr Ile Pro Glu Glu Leu Phe Leu Lys 1 5 10 <210> 204 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 204 Leu Ser Phe Ser Ser Asp Val Val Ser Glu Lys 1 5 10 <210> 205 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 205 Leu Ser Gly Leu Gln Glu Leu Asn Ile Gln Lys 1 5 10 <210> 206 <211> 17 <212> PRT <213> Chicken (Gallus gallus) <400> 206 Leu Tyr Gly Phe Gly Pro Ser Asp Ile Phe Glu Leu Gly Leu Asp Gly 1 5 10 15 Lys <210> 207 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 207 Leu Tyr Pro Glu Lys Asp Glu Pro Leu Asn Val Leu Asn Leu Lys 1 5 10 15 <210> 208 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 208 Asn Ile Asp Asp Glu Tyr Arg 1 5 <210> 209 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 209 Asn Pro Asp Gly Asp Glu Leu Glu Glu Lys 1 5 10 <210> 210 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 210 Asn Pro Ser Pro Ala Asp Leu Ala Lys 1 5 <210> 211 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 211 Asn Gln Ala Ala Ser Leu Ser Val Gln Lys 1 5 10 <210> 212 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 212 Asn Ser Phe Leu Ile Asn Ile Pro Leu Pro Phe Gly Gly Arg 1 5 10 <210> 213 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 213 Gln Val Asp Phe Ser Asp Tyr Ser Lys 1 5 <210> 214 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 214 Arg Gly Ser Val Ala Glu Asp Ile Ser Ile Asn Arg 1 5 10 <210> 215 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 215 Arg Val Ser Val Pro Gly Leu Asn Pro Ile Ser Ala Lys 1 5 10 <210> 216 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 216 Ser Ala Ser Ala Asn Tyr Asp Leu Gln Arg 1 5 10 <210> 217 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 217 Ser Glu Tyr Gln Ala Thr Tyr Lys 1 5 <210> 218 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 218 Ser Phe Val Ala Ser His Ile Ala Asn 1 5 <210> 219 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 219 Ser Gly Ile Val Thr Pro Gly Ala Lys 1 5 <210> 220 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 220 Ser Gln Asp Ile Asn Ala Tyr Asn Asp Ala Glu Lys 1 5 10 <210> 221 <211> 20 <212> PRT <213> Chicken (Gallus gallus) <400> 221 Ser Gln Leu Asn Asn Asn Ile Tyr Ser Gln Asp Ile Asn Ala Tyr Asn 1 5 10 15 Asp Ala Glu Lys 20 <210> 222 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 222 Thr Asp Thr Val Ala Asn Val Gln Gly Ala Ala Val Ser His Arg 1 5 10 15 <210> 223 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 223 Thr Glu Ala Leu Val Asn Tyr Ser Pro Thr Lys 1 5 10 <210> 224 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 224 Thr Glu Glu Ile Pro Pro Leu Ile Glu Asn Arg 1 5 10 <210> 225 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 225 Thr Gly Asn Val Asn Pro Leu Val Val Asp Leu Val Thr Tyr 1 5 10 <210> 226 <211> 25 <212> PRT <213> Chicken (Gallus gallus) <400> 226 Thr Gly Asn Val Asn Pro Leu Val Val Asp Leu Val Thr Tyr Thr Leu 1 5 10 15 Gly Leu Leu Pro Ser Pro Thr Pro Lys 20 25 <210> 227 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 227 Thr Pro Asp Phe Ile Val Pro Leu Thr Asp Leu Lys 1 5 10 <210> 228 <211> 21 <212> PRT <213> Chicken (Gallus gallus) <400> 228 Thr Thr Leu Asn Leu Tyr Gly Phe Gly Pro Ser Asp Ile Phe Glu Leu 1 5 10 15 Gly Leu Asp Gly Lys 20 <210> 229 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 229 Val Glu Gly Asn Val Ile Phe Asp Pro Ser Ser Tyr Val Pro Lys 1 5 10 15 <210> 230 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 230 Val Phe Asp Leu Gln Leu Gln Pro Arg 1 5 <210> 231 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 231 Val Asn Leu Asn Val Ala Gly Leu Ala Ser 1 5 10 <210> 232 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 232 Val Ser Val Pro Gly Leu Asn Pro Ile Ser Ala Lys 1 5 10 <210> 233 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 233 Val Thr Val Val Asp Thr Ile Gln Lys 1 5 <210> 234 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 234 Tyr Ala Asn Glu Leu Leu Asp Arg 1 5 <210> 235 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 235 Tyr Ser Thr Gln Leu Asp Asn Lys 1 5 <210> 236 <211> 927 <212> DNA <213> Chicken (Gallus gallus) <400> 236 atgggccctg tgcggctctt gctgctcttg ctgctgctca gcagtggtgt tctcacacag 60 gaaggaacac ctgaaaatgg aaacccagga tgttcaaaag atgcggcccg atttaaaagc 120 cttagaaaat atgtttactt atatgaagca gaacacaa gtgggatcac gggaacagca 180 gattctcgaa gcggttcaaa gatcacctgt aaagttgagt tggaggtacc acagctgtgc 240 cagttcatcc tgaggacaat gcattgctcc ctaagggaga catttggtgt tgacagtgag 300 agaagagcca tgctgaggaa gtcaaagaac tctgatgact ttgcaaatgc catgtccaaa 360 catgagctaa gattcagcac tcaggatgga acaaaagtta aactatatcc agagaaggat 420 gaacctctga atgtcctcaa tctcaagaga ggaattatct cagctctcct tgcaccaaca 480 gaacagagg aaaacataa aacaatttcc atggatactg tatatggaaa gtgtgacagt 540 gaggttgagt tcaaatccag aaggaagt gttgcagaag atatttcaat taacaggaac 600 ctgaaagcct gtgacaactt cagtccaatc agagatatg tcagccctgt tgccattgta 660 aaaggactaa acatcccact atctaccctt ctgagtagca ctcaatcctg tcactacagt 720 attgatgcaa agaaaaagca tatcagagat gttgtctgca gtgaaaaaca cctgtttctg 780 ccttcctcat acaaaaatca gtatggtatg atgacagaag tcaaccagac actgaagctt 840 gaagataatc agaggatgaa taacagaaat cctgatggag atgaactgga agagaaagga 900 cttgcactgg aaagcacaga tgctaaa 927 <210> 237 <211> 309 <212> PRT <213> Chicken (Gallus gallus) <400> 237 Met Gly Pro Val Arg Leu Leu Leu Leu Leu Leu Leu Leu Ser Ser Gly 1 5 10 15 Val Leu Thr Gln Glu Gly Thr Pro Glu Asn Gly Asn Pro Gly Cys Ser 20 25 30 Lys Asp Ala Ala Arg Phe Lys Ser Leu Arg Lys Tyr Val Tyr Leu Tyr 35 40 45 Glu Ala Glu Thr Ser Ser Gly Ile Thr Gly Thr Ala Asp Ser Arg Ser 50 55 60 Gly Ser Lys Ile Thr Cys Lys Val Glu Leu Glu Val Pro Gln Leu Cys 65 70 75 80 Gln Phe Ile Leu Arg Thr Met His Cys Ser Leu Arg Glu Thr Phe Gly 85 90 95 Val Asp Ser Glu Arg Arg Ala Met Leu Arg Lys Ser Lys Asn Ser Asp 100 105 110 Asp Phe Ala Asn Ala Met Ser Lys His Glu Leu Arg Phe Ser Thr Gln 115 120 125 Asp Gly Thr Lys Val Lys Leu Tyr Pro Glu Lys Asp Glu Pro Leu Asn 130 135 140 Val Leu Asn Leu Lys Arg Gly Ile Ile Ser Ala Leu Leu Ala Pro Thr 145 150 155 160 Glu Thr Glu Glu Asn Ile Lys Thr Ile Ser Met Asp Thr Val Tyr Gly 165 170 175 Lys Cys Asp Ser Glu Val Glu Phe Lys Ser Arg Arg Gly Ser Val Ala 180 185 190 Glu Asp Ile Ser Ile Asn Arg Asn Leu Lys Ala Cys Asp Asn Phe Ser 195 200 205 Pro Ile Arg Asp Tyr Val Ser Pro Val Ala Ile Val Lys Gly Leu Asn 210 215 220 Ile Pro Leu Ser Thr Leu Leu Ser Ser Thr Gln Ser Cys His Tyr Ser 225 230 235 240 Ile Asp Ala Lys Lys Lys His Ile Arg Asp Val Val Cys Ser Glu Lys 245 250 255 His Leu Phe Leu Pro Ser Ser Tyr Lys Asn Gln Tyr Gly Met Met Thr 260 265 270 Glu Val Asn Gln Thr Leu Lys Leu Glu Asp Asn Gln Arg Met Asn Asn 275 280 285 Arg Asn Pro Asp Gly Asp Glu Leu Glu Glu Lys Gly Leu Ala Leu Glu 290 295 300 Ser Thr Asp Ala Lys 305 <210> 238 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 238 Ala Leu Leu Ala Pro Thr Glu Thr Glu Glu Asn Ile Lys 1 5 10 <210> 239 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 239 Asp Tyr Val Ser Pro Val Ala Ile Val Lys 1 5 10 <210> 240 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 240 Glu Thr Phe Gly Val Asp Ser Glu Arg 1 5 <210> 241 <211> 17 <212> PRT <213> Chicken (Gallus gallus) <400> 241 Gly Ile Ile Ser Ala Leu Leu Ala Pro Thr Glu Thr Glu Glu Asn Ile 1 5 10 15 Lys <210> 242 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 242 Gly Ser Val Ala Glu Asp Ile Ser Ile Asn Arg 1 5 10 <210> 243 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 243 His Leu Phe Leu Pro Ser Ser Tyr Lys 1 5 <210> 244 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 244 Leu Ala Pro Thr Glu Thr Glu Glu Asn Ile Lys 1 5 10 <210> 245 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 245 Leu Phe Leu Pro Ser Ser Tyr Lys 1 5 <210> 246 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 246 Leu Leu Ala Pro Thr Glu Thr Glu Glu Asn Ile Lys 1 5 10 <210> 247 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 247 Leu Tyr Pro Glu Lys Asp Glu Pro Leu Asn Val Leu Asn Leu Lys 1 5 10 15 <210> 248 <211> 18 <212> PRT <213> Chicken (Gallus gallus) <400> 248 Arg Gly Ile Ile Ser Ala Leu Leu Ala Pro Thr Glu Thr Glu Glu Asn 1 5 10 15 Ile Lys <210> 249 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 249 Ser Val Ala Glu Asp Ile Ser Ile Asn Arg 1 5 10 <210> 250 <211> 1041 <212> DNA <213> Chicken (Gallus gallus) <400> 250 ctggatggct caaccagttt gacaagaaaa agaggactga agctggccac agcactgtct 60 ctgaataata acaatttct aggaggagt catgacaca gtattagtct catgaagag 120 aacctggaag cttcaatgat aaaatgca aaatcaca caccagtttt taaatgaat 180 ttcagccaag agctttctgg aaatactaaa tctaaaccca ctatttctc agggctaaaa 240 gtaacatatg acttactac tcctaagcat ggcatcagtg ctaagggagg agttgctcac 300 aaacttgctt tagactct tacatcttac ctgtcagtag aaacatcaac aagggaat 360 atcgatggag caatttacac tggaattca tttctggag ctctagacca tgaagcaac 420 acctatctgc atgctaatgg agttcggtca tctctcaagc ttgaggccaa ctccaagta 480 gatgactct ggaacagtga atgaaagaa atacttgcag ttgaagcatc taccagtcgt 540 gtttatgcag tctgggagca caatgggaa aacttgcac gatacacacc tctctcaca 600 acgacaggat ctcagaatg caaagcacc ttcgagctgg ctccttggac agtgtcagca 660 gatcttcaga ttcaggtcac tcagccaat tccttcctgg accagcatc agttaatcaa 720 gttgtcttaa tgaagtcag tcctacagac cagaagttg gctggaaggg tgaggccaa 780 attcagtcat tatctctgag acatgacatg caattatcaa atgaaaaatc aaatgcaaag 840 tttgatattt ctggatcttt ggaagggtac atggacttcc tgaaaagaat taattgtgct 900 atttctaaga agagcttgtg ggatatcttg aagttggatg tcactactgt tgctgacaga 960 aagcactact taaatgcttc agcatccttc atatacagga agagtgatga tggttacttt 1020 ttccctatgc ctgtgattag 1041 <210> 251 <211> 347 <212> PRT <213> Chicken (Gallus gallus) <400> 251 Leu Asp Gly Ser Thr Ser Leu Thr Arg Lys Arg Gly Leu Lys Leu Ala 1 5 10 15 Thr Ala Leu Ser Leu Asn Asn Asn Lys Phe Leu Gly Gly Ser His Asp 20 25 30 Asn Ser Ile Ser Leu Thr Lys Lys Asn Leu Glu Ala Ser Met Ile Thr 35 40 45 Asn Ala Lys Ile Asn Thr Pro Val Phe Lys Met Asn Phe Ser Gln Glu 50 55 60 Leu Ser Gly Asn Thr Lys Ser Lys Pro Thr Ile Ser Ser Gly Leu Lys 65 70 75 80 Val Thr Tyr Asp Phe Thr Thr Pro Lys His Gly Ile Ser Ala Lys Gly 85 90 95 Gly Val Ala His Lys Leu Ala Leu Glu Thr Leu Thr Ser Tyr Leu Ser 100 105 110 Val Glu Thr Ser Thr Lys Gly Asn Ile Asp Gly Ala Ile Tyr Thr Gly 115 120 125 Asn Ser Phe Ser Gly Ala Leu Asp His Glu Ala Asn Thr Tyr Leu His 130 135 140 Ala Asn Gly Val Arg Ser Ser Leu Lys Leu Glu Ala Asn Ser Lys Val 145 150 155 160 Asp Gly Leu Trp Asn Ser Glu Met Lys Glu Ile Leu Ala Val Glu Ala 165 170 175 Ser Thr Ser Arg Val Tyr Ala Val Trp Glu His Asn Gly Lys Asn Phe 180 185 190 Ala Arg Tyr Thr Pro Leu Phe Thr Thr Thr Gly Ser Gln Lys Cys Lys 195 200 205 Ala Thr Phe Glu Leu Ala Pro Trp Thr Val Ser Ala Asp Leu Gln Ile 210 215 220 Gln Val Thr Gln Pro Asn Ser Phe Leu Asp Thr Ala Ser Val Asn Gln 225 230 235 240 Val Val Leu Met Lys Val Ser Pro Thr Asp Gln Lys Val Gly Trp Lys 245 250 255 Gly Glu Gly Gln Ile Gln Ser Leu Ser Leu Arg His Asp Met Gln Leu 260 265 270 Ser Asn Glu Lys Ser Asn Ala Lys Phe Asp Ile Ser Gly Ser Leu Glu 275 280 285 Gly Tyr Met Asp Phe Leu Lys Arg Ile Asn Cys Ala Ile Ser Lys Lys 290 295 300 Ser Leu Trp Asp Ile Leu Lys Leu Asp Val Thr Thr Val Ala Asp Arg 305 310 315 320 Lys His Tyr Leu Asn Ala Ser Ala Ser Phe Ile Tyr Arg Lys Ser Asp 325 330 335 Asp Gly Tyr Phe Phe Pro Met Pro Val Ile Arg 340 345 <210> 252 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 252 Glu Ile Leu Ala Val Glu Ala Ser Thr Ser Arg 1 5 10 <210> 253 <211> 14 <212> PRT <213> Chicken (Gallus gallus) <400> 253 Phe Leu Gly Gly Ser His Asp Asn Ser Ile Ser Leu Thr Lys 1 5 10 <210> 254 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 254 Gly Glu Gly Gln Ile Gln Ser Leu Ser Leu Arg 1 5 10 <210> 255 <211> 7 <212> PRT <213> Chicken (Gallus gallus) <400> 255 Ile Asn Thr Pro Val Phe Lys 1 5 <210> 256 <211> 17 <212> PRT <213> Chicken (Gallus gallus) <400> 256 Leu Ala Leu Glu Thr Leu Thr Ser Tyr Leu Ser Val Glu Thr Ser Thr 1 5 10 15 Lys <210> 257 <211> 11 <212> PRT <213> Chicken (Gallus gallus) <400> 257 Leu Ala Thr Ala Leu Ser Leu Asn Asn Asn Lys 1 5 10 <210> 258 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 258 Leu Asp Gly Ser Thr Ser Leu Thr Arg 1 5 <210> 259 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 259 Pro Thr Ile Ser Ser Gly Leu Lys 1 5 <210> 260 <211> 12 <212> PRT <213> Chicken (Gallus gallus) <400> 260 Tyr Thr Pro Leu Phe Thr Thr Thr Gly Ser Gln Lys 1 5 10 <210> 261 <211> 741 <212> DNA <213> Chicken (Gallus gallus) <400> 261 accccagtgt tagctgcttt tctccatggc attagtaaca ataagaagac aggaggcctc 60 cagcttgtgg tatatgctga taccgactcg gtcaggccgc gggtgcaggt atttgtgaca 120 aacctcacag attcgagcaa gtggaagctc tgcgcagatg cttcggtccg caatgctcac 180 aaggcagtgg cctacgtgaa atggggctgg gactgccggg actacaaggt ttctactgag 240 ctggtaactg ggcggtttgc tgggcaccct gctgcacaag tgaagctgga gtggcccaag 300 gttccttcga atgtcagatc agtggttgaa tggttttacg agtttgtccc tggggctgca 360 tttatgctgg gtttctctga gagaatggac aagaatcctt ctcgacaagc caggatggtt 420 gtggctctaa cttctccgag gacatgtgat gttgttgtca agctgcctga tataatcctc 480 tatcaaaaag ccgtgaggct tcctctatca ctccctgtgg gtccaaggat cccagcttca 540 gagctgcagc ctccaatctg gaacgtcttt gctgaagccc cctctgccgt gctcgagaat 600 ttgaaagctc gctgctcagt ttcgtacaac aagatcaaaa cctttaatga agtcaagttc 660 aactactcga tgcccgcaaa ctgctatcac atcttggttc aggattgcag ctctgaactt 720 aagttcctgg tgatgatgaa a 741 <210> 262 <211> 247 <212> PRT <213> Chicken (Gallus gallus) <400> 262 Thr Pro Val Leu Ala Ala Phe Leu His Gly Ile Ser Asn Asn Lys Lys 1 5 10 15 Thr Gly Gly Leu Gln Leu Val Val Tyr Ala Asp Thr Asp Ser Val Arg 20 25 30 Pro Arg Val Gln Val Phe Val Thr Asn Leu Thr Asp Ser Ser Lys Trp 35 40 45 Lys Leu Cys Ala Asp Ala Ser Val Arg Asn Ala His Lys Ala Val Ala 50 55 60 Tyr Val Lys Trp Gly Trp Asp Cys Arg Asp Tyr Lys Val Ser Thr Glu 65 70 75 80 Leu Val Thr Gly Arg Phe Ala Gly His Pro Ala Ala Gln Val Lys Leu 85 90 95 Glu Trp Pro Lys Val Pro Ser Asn Val Arg Ser Val Val Glu Trp Phe 100 105 110 Tyr Glu Phe Val Pro Gly Ala Ala Phe Met Leu Gly Phe Ser Glu Arg 115 120 125 Met Asp Lys Asn Pro Ser Arg Gln Ala Arg Met Val Val Ala Leu Thr 130 135 140 Ser Pro Arg Thr Cys Asp Val Val Val Lys Leu Pro Asp Ile Ile Leu 145 150 155 160 Tyr Gln Lys Ala Val Arg Leu Pro Leu Ser Leu Pro Val Gly Pro Arg 165 170 175 Ile Pro Ala Ser Glu Leu Gln Pro Pro Ile Trp Asn Val Phe Ala Glu 180 185 190 Ala Pro Ser Ala Val Leu Glu Asn Leu Lys Ala Arg Cys Ser Val Ser 195 200 205 Tyr Asn Lys Ile Lys Thr Phe Asn Glu Val Lys Phe Asn Tyr Ser Met 210 215 220 Pro Ala Asn Cys Tyr His Ile Leu Val Gln Asp Cys Ser Ser Glu Leu 225 230 235 240 Lys Phe Leu Val Met Met Lys 245 <210> 263 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 263 Phe Ala Gly His Pro Ala Ala Gln Val Lys 1 5 10 <210> 264 <211> 19 <212> PRT <213> Chicken (Gallus gallus) <400> 264 Lys Thr Gly Gly Leu Gln Leu Val Val Tyr Ala Asp Thr Asp Ser Val 1 5 10 15 Arg Pro Arg <210> 265 <211> 10 <212> PRT <213> Chicken (Gallus gallus) <400> 265 Leu Pro Leu Ser Leu Pro Val Gly Pro Arg 1 5 10 <210> 266 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 266 Thr Gly Gly Leu Gln Leu Val Val Tyr 1 5 <210> 267 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 267 Ala Asp Thr Asp Ser Val Arg Pro Arg 1 5 <210> 268 <211> 15 <212> PRT <213> Chicken (Gallus gallus) <400> 268 Thr Pro Val Leu Ala Ala Phe Leu His Gly Ile Ser Asn Asn Lys 1 5 10 15 <210> 269 <211> 13 <212> PRT <213> Chicken (Gallus gallus) <400> 269 Val Gln Val Phe Val Thr Asn Leu Thr Asp Ser Ser Lys 1 5 10 <210> 270 <211> 9 <212> PRT <213> Chicken (Gallus gallus) <400> 270 Val Ser Thr Glu Leu Val Thr Gly Arg 1 5 <210> 271 <211> 8 <212> PRT <213> Chicken (Gallus gallus) <400> 271 Val Val Ala Leu Thr Ser Pro Arg 1 5

Claims

1. Use of at least one of the proteins defined in (3) below in the preparation of a diagnostic kit for egg allergy, wherein: The diagnostic kit comprises at least one of the following (3) proteins as an antigen: (3) (3A) A protein comprising the central portion of vitellogenin-1 or the C-terminal portion of lipovitellin-1, which is any one of the following (3A-a) to (3A-b) that is an antigen for egg allergy: (3A-a) a protein having the amino acid sequence shown in SEQ ID NO: 18; or (3A-b) a protein having an amino acid sequence encoded by the base sequence shown in SEQ ID NO: 17; or (3B) A protein comprising at least one of the amino acid sequences selected from the group consisting of SEQ ID NOs: 19 to 45.

2. Use of at least one of the proteins defined in (3) of claim 1 in the preparation of a composition for diagnosing egg allergy, wherein: The diagnostic composition comprises: at least one of the proteins defined as (3) in claim 1 as an antigen.

3. Use of at least one of the proteins defined in (3) of claim 1 as an antigen in the preparation of a kit for providing an index for diagnosing egg allergy in a subject by the following method, the method comprising the following steps: (i) contacting a sample obtained from a subject with an antigen, wherein the sample is a solution containing IgE antibodies; (ii) detecting the binding of IgE antibodies in a sample obtained from the subject to the antigen; (iii) When the binding of the subject's IgE antibody to the antigen is detected, an indicator is provided that the subject is allergic to egg.

4. A processed egg product, characterized in that: This is a processed egg product in which antigens are removed or reduced, and the antigen is at least one of the proteins defined as (3) in claim 1.

5. Use of an antibody that binds to at least one of the proteins specified as (3) in claim 1 in the preparation of a detector for determining the presence or absence of egg antigen in an object, characterized in that: The detector comprises: an antibody that binds to at least one of the proteins defined as (3) in claim 1.

6. Use of a primer having a base sequence complementary to the base sequence shown in SEQ ID NO: 17 in the preparation of a detector for determining the presence or absence of an antigen causing egg allergy in an object, characterized in that: The detector includes: a primer having a base sequence complementary to the base sequence shown in sequence number 17.

7. A method for producing an egg processed product with antigens removed or reduced, comprising the steps of: confirming that the antigens have been removed or reduced during the production process of the processed product, Here, the antigen is at least one of the proteins defined as (3) in claim 1.

8. Use of at least one of the proteins defined in (3) of claim 1 as an antigen derived from egg for non-diagnostic purposes, wherein: The antigen is responsible for the egg allergy.

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