Food Allergens: Molecular and Immunological Characteristics

Food Allergy: Adverse Reactions to Foods and Food Additives, Fourth Edition

Volumn , Issue , 2009, Pages 43-61

  Breiteneder, Heimo ^a   Mills, E N Clare ^b  

^a MEDICAL UNIVERSITY OF VIENNA   (Austria)

^b INSTITUTE OF FOOD RESEARCH   (United Kingdom)

Author keywords

Animal food allergen family and parvalbumins; Arginine kinases and invertebrate allergens; Cupin superfamily; Cysteine protease superfamily; Food allergen protein families; Food allergens molecular and immunological characteristics; Kunitz bovine pancreatic trypsin inhibitor family; non specific lipid transfer proteins(nsLTPs)

Indexed keywords

EID: 84889770682     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9781444300062.ch4     Document Type: Chapter

References (207)

1. Jenkins JA, Griffiths-Jones S, Shewry PR, et al. Structural relatedness of plant food allergens with specific reference to crossreactive allergens: an in silico analysis. J Allergy Clin Immunol 2005;115:163-70.
2. Radauer C, Breiteneder H. Pollen allergens are restricted to few protein families and show distinct patterns of species distribution. J Allergy Clin Immunol 2006;117:141-7.
3. Dunwell JM, Purvis A, Khuri S. Cupins: the most functionally diverse protein superfamily? Phytochemistry 2004;65:7-17.
4. Mills EN, Jenkins JA, Alcocer MJ, Shewry PR. Structural, biological, and evolutionary relationships of plant food allergens sensitizing via the gastrointestinal tract. Crit Rev Food Sci Nutr 2004;44:379-407.
5. Rodin J, Rask L. Characterization of matteuccin, the 2.2S storage protein of the ostrich fern. Evolutionary relationship to angiosperm seed storage proteins. Eur J Biochem 1990;28;192:101-7.
6. Shatters Jr RG, Boykin LM, Lapointe SL, et al. Phylogenetic and structural relationships of the PR5 gene family reveal an ancient multigene family conserved in plants and select animal taxa. J Mol Evol 2006;63:12-29.
7. Liscombe DK, MacLeod BP, Loukanina N, et al. Evidence for the monophyletic evolution of benzylisoquinoline alkaloid biosynthesis in angiosperms. Phytochemistry 2005;66:2501-20.
8. Bateman A, Coin L, Durbin R, et al. The Pfam protein families database. Nucleic Acids Res 2004;1:32(Database issue):D138-41.
9. Gendel SM, Jenkins JA. Allergen sequence databases. Mol Nutr Food Res 2006;50:633-7.
10. Jenkins JA, Breiteneder H, Mills EN. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. DOI information: 10.1016/j.jaci.2007.08.019.
11. Breiteneder H, Radauer C. A classification of plant food allergens. J Allergy Clin Immunol 2004;113:821-30.
12. Aalberse RC. Structural biology of allergens. J Allergy Clin Immunol 2000;106:228-38.
13. MacLeod AR. Genetic origin of diversity of human cytoskeletal tropomyosins. Bioessays 1987;6:208-12.
14. Li Y, Mui S, Brown JH, et al. The crystal structure of the C-terminal fragment of striated-muscle alpha-tropomyosin reveals a key troponin T recognition site. Proc Natl Acad Sci USA 2002;99:7378-83.
15. Gunning PW, Schevzov G, Kee AJ, Hardeman EC. Tropomyosin isoforms: divining rods for actin cytoskeleton function. Trends Cell Biol 2005;15:333-41.
16. Shanti KN, Martin BM, Nagpal S, et al. Identification of tropomyosin as the major shrimp allergen and characterization of its IgE-binding epitopes. J Immunol 1993;151:5354-63.
17. Daul CB, Slattery M, Reese G, Lehrer SB. Identification of the major brown shrimp (Penaeus aztecus) allergen as the muscle protein tropomyosin. Int Arch Allergy Immunol 1994;105:49-55.
18. Leung PS, Chu KH, Chow WK, et al. Cloning, expression, and primary structure of Metapenaeus ensis tropomyosin, the major heat-stable shrimp allergen. J Allergy Clin Immunol 1994;94:882-90.
19. Reese G, Ayuso R, Lehrer SB. Tropomyosin: an invertebrate pan-allergen. Int Arch Allergy Immunol 1999;119:247-58.
20. Motoyama K, Ishizaki S, Nagashima Y, Shiomi K. Cephalopod tropomyosins: identification as major allergens and molecular cloning. Food Chem Toxicol 2006;44:1997-2002.
21. Naqpal S, Rajappa L, Metcalfe DD, Rao PV. Isolation and characterization of heat-stable allergens from shrimp (Penaeus indicus). J Allergy Clin Immunol 1989;83:26-36.
22. Lehrer SB, Ibanez MD, McCants ML, et al. Characterization of water-soluble shrimp allergens released during boiling. J Allergy Clin Immunol 1990;85:1005-13.
23. Lewit-Bentley A, Rety S. EF-hand calcium-binding proteins. Curr Opin Struct Biol 2000;10:637-43.
24. Ikura M. Calcium binding and conformational response in EF-hand proteins. Trends Biochem Sci 1996;21:14-17.
25. Declercq JP, Tinant B, Parello J, Rambaud J. Ionic interactions with parvalbumins. Crystal structure determination of pike 4.10 parvalbumin in four different ionic environments. J Mol Biol 1991;220:1017-39.
26. Pauls TL, Cox JA, Berchtold MW. The Ca2+(-)binding proteins parvalbumin and oncomodulin and their genes: new structural and functional findings. Biochim Biophys Acta 1996;1306:39-54.
27. Bugajska-Schretter A, Elfman L, Fuchs T, et al. Parvalbumin, a cross-reactive fish allergen, contains IgE-binding epitopes sensitive to periodate treatment and Ca2+ depletion. J Allergy Clin Immunol 1998;101:67-74.
28. Bugajska-Schretter A, Grote M, Vangelista L, et al. Purification, biochemical, and immunological characterisation of a major food allergen: different immunoglobulin E recognition of the apo-and calcium-bound forms of carp parvalbumin. Gut 2000;46:661-9.
29. Filimonov VV, Pfeil W, Tsalkova TN, Privalov PL. Thermodynamic investigations of proteins. IV. Calcium binding protein parval-bumin. Biophys Chem 1978;8:117-22.
30. Elsayed S, Aas K. Characterization of a major allergen (cod). Observations on effect of denaturation on the allergenic activity. J Allergy 1971;47:283-91.
31. Aas K, Jebsen JW. Studies of hypersensitivity to fish. Partial purification and crystallization of a major allergenic component of cod. Int Arch Allergy Appl Immunol 1967;32:1-20.
32. Elsayed S, Bennich H. The primary structure of allergen M from cod. Scand J Immunol 1975;4:203-8.
33. Bernhisel-Broadbent J, Scanlon SM, Sampson HA. Fish hypersensitivity. I. in vitro and oral challenge results in fish-allergic patients. J Allergy Clin Immunol 1992;89:730-7.
34. Hilger C, Thill L, Grigioni F, et al. IgE antibodies of fish allergic patients cross-react with frog parvalbumin. Allergy 2004;59:653-60.
35. Hilger C, Grigioni F, Thill L, et al. Severe IgE-mediated anaphylaxis following consumption of fried frog legs: definition of alpha-parvalbumin as the allergen in cause. Allergy 2002;57:1053-8.
36. Tuinier R, de Kruif CG. Stability of casein micelles in milk. J Chem Phys 2002;117:1290-5.
37. Kawasaki K, Weiss KM. Mineralized tissue and vertebrate evolution: the secretory calcium-binding phosphoprotein gene cluster. Proc Natl Acad Sci USA 2003;100:4060-5.
38. Natale M, Bisson C, Monti G, et al. Cow's milk allergens identification by two-dimensional immunoblotting and mass spectrometry. Mol Nutr Food Res 2004;48:363-9.
39. Reese G, Tracey D, Daul CB, et al. IgE and monoclonal antibody reactivities to the major shrimp allergen Pen a 1 (tropomyosin) and vertebrate tropomyosins. Adv Exp Med Biol 1996;409:225-30.
40. Yu CJ, Lin YF, Chiang BL, Chow LP. Proteomics and immunological analysis of a novel shrimp allergen, Pen m 2. J Immunol 2003;170:445-53.
41. Asturias JA, Eraso E, Arilla MC, et al. Cloning, isolation, and IgE-binding properties of Helix aspersa (brown garden snail) tropomyosin. Int Arch Allergy Immunol 2002;128:90-6.
42. Miyazawa H, Fukamachi H, Inagaki Y, et al. Identification of the first major allergen of a squid (Todarodes pacificus). J Allergy Clin Immunol 1996;98:948-53.
43. Leung PS, Chu KH. cDNA cloning and molecular identification of the major oyster allergen from the Pacific oyster Crassostrea gigas. Clin Exp Allergy 2001;31:1287-94.
44. Leung PS, Chen YC, Gershwin ME, et al. Identification and molecular characterization of Charybdis feriatus tropomyosin, the major crab allergen. J Allergy Clin Immunol 1998;102:847-52.
45. Chu KH, Wong SH, Leung PS. Tropomyosin is the major mol-lusk allergen: reverse transcriptase polymerase chain reaction, Expression and IgE Reactivity. Mar Biotechnol (NY) 2000;2:499-509.
46. Van Do T, Hordvik I, Endresen C, et al. The major allergen (par-valbumin) of codfish is encoded by at least two isotypic genes: cDNA cloning, expression and antibody binding of the recombinant allergens. Mol Immunol 2003;39:595-602.
47. Swoboda I, Bugajska-Schretter A, Verdino P, et al. Recombinant carp parvalbumin, the major cross-reactive fish allergen: a tool for diagnosis and therapy of fish allergy. J Immunol 2002;168:4576-84.
48. Lindstrom CD, van Do T, Hordvik I, et al. Cloning of two distinct cDNAs encoding parvalbumin, the major allergen of Atlantic salmon (Salmo salar). Scand J Immunol 1996;44:335-44.
49. Shiomi K, Hamada Y, Sekiguchi K, et al. Two classes of allergens, parvalbumins and higher molecular weight substances, in Japanese eel and bigeye tuna. Fish Sci 1999;65:943-8.
50. Bernard H, Creminon C, Yvon M, et al. Specificity of the human IgE response to the different purified caseins in allergy to cow's milk proteins. Int Arch Allergy Immunol 1998;115:235-44.
51. Bellioni-Businco B, Paganelli R, Lucenti P, et al. Allergenicity of goat's milk in children with cow's milk allergy. J Allergy Clin Immunol 1999;103:1191-4.
52. Spuergin P, Walter M, Schiltz E, et al. Allergenicity of alpha-caseins from cow, sheep, and goat. Allergy 1997;52:293-8.
53. Businco L, Giampietro PG, Lucenti P, et al. Allergenicity of mare's milk in children with cow's milk allergy. J Allergy Clin Immunol 2000;105:1031-4.
54. Restani P, Gaiaschi A, Plebani A, et al. Cross-reactivity between milk proteins from different animal species. Clin Exp Allergy 1999;29:997-1004.
55. Flower DR. The lipocalin protein family: structure and function. Biochem J 1996;318:1-14.
56. Virtanen T. Lipocalin allergens. Allergy 2001;56:48-51.
57. Nitta K, Sugai S. The evolution of lysozyme and alpha-lactalbu-min. Eur J Biochem 1989;182:111-8.
58. Aabin B, Poulsen LK, Ebbehoj K, et al. Identification of IgE-binding egg white proteins: comparison of results obtained by different methods. Int Arch Allergy Immunol 1996;109:50-7.
59. Holen E, Elsayed S. Characterization of four major allergens of hen egg-white by IEF/SDS-PAGE combined with electrophoretic transfer and IgE-immunoautoradiography. Int Arch Allergy Appl Immunol 1990;91:136-41.
60. van Gent D, Sharp P, Morgan K, Kalsheker N. Serpins: structure, function and molecular evolution. Int J Biochem Cell Biol 2003;35:1536-47.
61. Bernhisel-Broadbent J, Dintzis HM, Dintzis RZ, Sampson HA. Allergenicity and antigenicity of chicken egg ovomucoid (Gal d III) compared with ovalbumin (Gal d I) in children with egg allergy and in mice. J Allergy Clin Immunol 1994;93:1047-59.
62. Binder M, Mahler V, Hayek B, et al. Molecular and immunological characterization of arginine kinase from the Indianmeal moth, Plodia interpunctella, a novel cross-reactive invertebrate pan-allergen. J Immunol 2001;167:5470-7.
63. Laskowski Jr M, Kato I, Ardelt W, et al. Ovomucoid third domains from 100 avian species: isolation, sequences, and hypervariability of enzyme-inhibitor contact residues. Biochemistry 1987;26:202-21.
64. Kato I, Schrode J, Kohr WJ, Laskowski Jr. M. Chicken ovomucoid: determination of its amino acid sequence, determination of the trypsin reactive site, and preparation of all three of its domains. Biochemistry 1987;26:193-201.
65. Cooke SK, Sampson HA. Allergenic properties of ovomucoid in man. J Immunol 1997;159:2026-32.
66. Kreis M, Forde BG, Rahman S, et al. Molecular evolution of the seed storage proteins of barley, rye and wheat. J Mol Biol 1985;183:499-502.
67. Palosuo K, Alenius H, Varjonen E, et al. A novel wheat glia-din as a cause of exercise-induced anaphylaxis. J Allergy Clin Immunol 1999;103:912-17.
68. Palosuo K, Varjonen E, Kekki OM, et al. Wheat omega-5 glia-din is a major allergen in children with immediate allergy to ingested wheat. J Allergy Clin Immunol 2001;108:634-8.
69. Maruyama N, Ichise K, Katsube T, et al. Identification of major wheat allergens by means of the Escherichia coli expression system. Eur J Biochem 1998;255:739-45.
70. Sanchez-Monge R, Lombardero M, Garcia-Selles FJ, et al. Lipid-transfer proteins are relevant allergens in fruit allergy. J Allergy Clin Immunol 1999;103:514-9.
71. Pastorello EA, D'Ambrosio FP, Pravettoni V, et al. Evidence for a lipid transfer protein as the major allergen of apricot. J Allergy Clin Immunol 2000;105:371-7.
72. Scheurer S, Pastorello EA, Wangorsch A, et al. Recombinant allergens Pru av 1 and Pru av 4 and a newly identified lipid transfer protein in the in vitro diagnosis of cherry allergy. J Allergy Clin Immunol 2001;107:724-31.
73. Pastorello EA, Farioli L, Pravettoni V, et al. The major allergen of peach (Prunus persica) is a lipid transfer protein. J Allergy Clin Immunol 1999;103:520-6.
74. Pastorello EA, Farioli L, Pravettoni V, et al. Characterization of the major allergen of plum as a lipid transfer protein. J Chromatogr B Biomed Sci Appl 2001;756:95-103.
75. Zuidmeer L, Salentijn E, Rivas MF, et al. The role of profilin and lipid transfer protein in strawberry allergy in the Mediterranean area. Clin Exp Allergy 2006;36:666-75.
76. Ahrazem O, Ibanez MD, Lopez-Torrejon G, et al. Orange germin-like glycoprotein Cit s 1: an equivocal allergen. Int Arch Allergy Immunol 2006;139:96-103.
77. Pastorello EA, Farioli L, Pravettoni V, et al. Identification of grape and wine allergens as an endochitinase 4, a lipid-transfer protein, and a thaumatin. J Allergy Clin Immunol 2003;111:350-9.
78. Sanchez-Monge R, Blanco C, Lopez-Torrejon G, et al. Differential allergen sensitization patterns in chestnut allergy with or without associated latex-fruit syndrome. J Allergy Clin Immunol 2006;118:705-10.
79. Asero R, Mistrello G, Roncarolo D, et al. Allergy to minor allergens of Brazil nut. Allergy 2002;57:1080-1.
80. Pastorello EA, Farioli L, Pravettoni V, et al. Lipid transfer protein and vicilin are important walnut allergens in patients not allergic to pollen. J Allergy Clin Immunol 2004;114:908-14.
81. Schocker F, Luttkopf D, Scheurer S, et al. Recombinant lipid transfer protein Cor a 8 from hazelnut: a new tool for in vitro diagnosis of potentially severe hazelnut allergy. J Allergy Clin Immunol 2004;113:141-7.
82. Diaz-Perales A, Tabar AI, Sanchez-Monge R, et al. Characterization of asparagus allergens: a relevant role of lipid transfer proteins. J Allergy Clin Immunol 2002;110:790-6.
83. San Miguel-Moncin M, Krail M, Scheurer S, et al. Lettuce anaphylaxis: identification of a lipid transfer protein as the major allergen. Allergy 2003;58:511-7.
84. Palacin A, Cumplido J, Figueroa J, et al. Cabbage lipid transfer protein Bra o 3 is a major allergen responsible for cross-reactivity between plant foods and pollens. J Allergy Clin Immunol 2006;117:1423-9.
85. Pastorello EA, Farioli L, Pravettoni V, et al. The maize major allergen, which is responsible for food-induced allergic reactions, is a lipid transfer protein. J Allergy Clin Immunol 2000;106:744-51.
86. Curioni A, Santucci B, Cristaudo A, et al. Urticaria from beer: an immediate hypersensitivity reaction due to a 10-kDa protein derived from barley. Clin Exp Allergy 1999;29:407-13.
87. Nakase M, Adachi T, Urisu A, et al. Rice (Oryza sativa L.) alpha amylase inhibitors of 14-16 kDa are potential allergens and products of a multi gene family. JAgric Food Chem 1996;44:2624-8.
88. Alvarez AM, Adachi T, Nakase M, et al. Classification of rice allergenic protein cDNAs belonging to the alpha-amylase/trypsin inhibitor gene family. Biochim Biophys Acta 1995;1251:201-4.
89. Izumi H, Adachi T, Fujii N, et al. Nucleotide sequence of a cDNA clone encoding a major allergenic protein in rice seeds. Homology of the deduced amino acid sequence with members of alpha-amylase/trypsin inhibitor family. FEBS Lett 1992;302:213-16.
90. Teuber SS, Dandekar AM, Peterson WR, Sellers CL. Cloning and sequencing of a gene encoding a 2S albumin seed storage protein precursor from English walnut (Juglans regia), a major food allergen. J Allergy Clin Immunol 1998;101:807-14.
91. Poltronieri P, Cappello MS, Dohmae N, et al. Identification and characterisation of the IgE-binding proteins 2S albumin and conglutin gamma in almond (Prunus dulcis) seeds. Int Arch Allergy Immunol 2002;128:97-104.
92. Pastorello EA, Farioli L, Pravettoni V, et al. Sensitization to the major allergen of Brazil nut is correlated with the clinical expression of allergy. J Allergy Clin Immunol. 1998;102:1021-7.
93. Robotham JM, Wang F, Seamon V, et al. Ana o 3, an important cashew nut (Anacardium occidentale L.) allergen of the 2S albumin family. J Allergy Clin Immunol 2005;115:1284-90.
94. Menendez-Arias L, Moneo I, Dominguez J, Rodriguez R. Primary structure of the major allergen of yellow mustard (Sinapis alba L.) seed, Sin a I. Eur J Biochem 1988;177:159-66.
95. Monsalve RI, Gonzalez de la Pena MA, Menendez-Arias L, et al. Characterization of a new oriental-mustard (Brassica juncea) allergen, Bra j IE: detection of an allergenic epitope. Biochem J 1993;293:625-32.
96. Vioque J, Sanchez-Vioque R, Clemente A, et al. Purification and partial characterization of chickpea 2S albumin. J Agric Food Chem 1999;47:1405-9.
97. Burks AW, Williams LW, Connaughton C, et al. Identification and characterization of a second major peanut allergen, Ara h II, with use of the sera of patients with atopic dermatitis and positive peanut challenge. J Allergy Clin Immunol 1992;90:962-9.
98. Kleber-Janke T, Crameri R, Appenzeller U, et al. Selective cloning of peanut allergens, including profilin and 2S albumins, by phage display technology. Int Arch Allergy Immunol 1999;119:265-74.
99. Stanley JS, King N, Burks AW, et al. Identification and mutational analysis of the immunodominant IgE binding epitopes of the major peanut allergen Ara h 2. Arch Biochem Biophys 1997;342:244-53.
100. Pastorello EA, Varin E, Farioli L, et al. The major allergen of sesame seeds (Sesamum indicum) is a 2S albumin. J Chromatogr B Biomed Sci Appl 2001;756:85-93.
101. Beyer K, Bardina L, Grishina G, Sampson HA. Identification of sesame seed allergens by 2-dimensional proteomics and Edman sequencing: seed storage proteins as common food allergens. J Allergy Clin Immunol 2002;110:154-9.
102. Kelly JD, Hlywka JJ, Hefle SL. Identification of sunflower seed IgE-binding proteins. Int Arch Allergy Immunol 2000;121:19-24.
103. Vanek-Krebitz M, Hoffmann-Sommergruber K, Laimer da Camara Machado M, et al. Cloning and sequencing of Mal d 1, the major allergen from apple (Malus domestica), and its immunological relationship to Bet v 1, the major birch pollen allergen. Biochem Biophys Res Commun 1995;214:538-51.
104. Karamloo F, Scheurer S, Wangorsch A, et al. Pyr c 1, the major allergen from pear (Pyrus communis), is a new member of the Bet v 1 allergen family. J Chromatogr B Biomed Sci Appl 2001;756:281-93.
105. Scheurer S, Metzner K, Haustein D, et al. Molecular cloning, expression and characterization of Pru a 1, the major cherry allergen. Mol Immunol 1997;34:619-29.
106. Karlsson AL, Alm R, Ekstrand B, et al. Bet v 1 homologues in strawberry identified as IgE-binding proteins and presumptive allergens. Allergy 2004;59:1277-84.
107. Hoffmann-Sommergruber K, O'Riordain G, Ahorn H, et al. Molecular characterization of Dau c 1, the Bet v 1 homologous protein from carrot and its cross-reactivity with Bet v 1 and Api g 1. Clin Exp Allergy 1999;29:840-7.
108. Breiteneder H, Hoffmann-Sommergruber K, O'Riordain G, et al. Molecular characterization of Api g 1, the major allergen of celery (Apium graveolens), and its immunological and structural relationships to a group of 17-kDa tree pollen allergens. Eur J Biochem 1995;233:484-9.
109. Luttkopf D, Muller U, Skov PS, et al. Comparison of four variants of a major allergen in hazelnut (Corylus avellana) Cor a 1.04 with the major hazel pollen allergen Cor a 1.01. Mol Immunol 2002;38:515-25.
110. Mittag D, Vieths S, Vogel L, et al. Soybean allergy in patients allergic to birch pollen: clinical investigation and molecular characterization of allergens. J Allergy Clin Immunol 2004;113:148-54.
111. Burks AW, Williams LW, Helm RM, et al. Identification of a major peanut allergen, Ara h I, in patients with atopic dermatitis and positive peanut challenges. J Allergy Clin Immunol 1991;88:172-9.
112. Ogawa T, Bando N, Tsuji H, et al. Alpha-subunit of beta-conglycinin, an allergenic protein recognized by IgE antibodies of soybean-sensitive patients with atopic dermatitis. Biosci Biotechnol Biochem 1995;59:831-3.
113. Kondo Y, Urisu A, Wada E, et al. [Allergen analysis of buckwheat by the immunoblotting method]. Arerugi 1993;42:142-8.
114. Teuber SS, Jarvis KC, Dandekar AM, et al. Identification and cloning of a complementary DNA encoding a vicilin-like proprotein, jug r 2, from English walnut kernel (Juglans regia), a major food allergen. J Allergy Clin Immunol 1999;104:1311-20.
115. Lauer I, Foetisch K, Kolarich D, et al. Hazelnut (Corylus avel-lana) vicilin Cor a 11: molecular characterization of a glycoprotein and its allergenic activity. Biochem J 2004;383:327-34.
116. Wang F, Robotham JM, Teuber SS, et al. Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family. J Allergy Clin Immunol 2002;110:160-6.
117. Rabjohn P, Helm EM, Stanley JS, et al. Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 1999;103:535-42.
118. Beardslee TA, Zeece MG, Sarath G, et al. Soybean glycinin G1 acidic chain shares IgE epitopes with peanut allergen Ara h 3. Int Arch Allergy Immunol 2000;123:299-307.
119. Garcia-Mas J, Messeguer R, Arus P, et al. Molecular characterization of cDNAs corresponding to genes expressed during almond (Prunusamygdalus Batsch) seed development. Plant Mol Biol 1995;27:205-10.
120. Roux KH, Teuber SS, Robotham JM, et al. Detection and stability of the major almond allergen in foods. J Agric Food Chem 2001;49:2131-6.
121. Wang F, Robotham JM, Teuber SS, et al. Ana o 2, a major cashew (Anacardium occidentale L.) nut allergen of the legumin family. Int Arch Allergy Immunol 2003;132:27-39.
122. Pastorello EA, Conti A, Pravettoni V, et al. Identification of acti-nidin as the major allergen of kiwi fruit. J Allergy Clin Immunol 1998;101:531-7.
123. Ogawa T, Tsuji H, Bando N, et al. Identification of the soybean allergenic protein, Gly m Bd 30K, with the soybean seed 34-kDa oil-body-associated protein. Biosci Biotechnol Biochem 1993;57:1030-3.
124. Tassin-Moindrot S, Caille A, Douliez JP, et al. The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2. Eur J Biochem 2000;267:1117-24.
125. Douliez JP, Jegou S, Pato C, et al. Binding of two mono-acylated lipid monomers by the barley lipid transfer protein, LTP1, as viewed by fluorescence, isothermal titration calorimetry and molecular modelling. Eur J Biochem 2001;268:384-8.
126. Pastorello EA, Pompei C, Pravettoni V, et al. Lipid-transfer protein is the major maize allergen maintaining IgE-bind-ing activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive doubleblind, placebo-controlled food challenge results. J Allergy Clin Immunol 2003;112:775-83.
127. Sancho AI, Rigby NM, Zuidmeer L, et al. The effect of thermal processing on the IgE reactivity of the non-specific lipid transfer protein from apple, Mal d 3. Allergy 2005;60:1262-8.
128. Moreno FJ, Mellon FA, Wickham MS, et al. Stability of the major allergen Brazil nut 2S albumin (Ber e 1) to physiologically relevant in vitro gastrointestinal digestion. FEBS J 2005;272:341-52.
129. Asero R, Mistrello G, Roncarolo D, et al. Lipid transfer protein: a pan-allergen in plant-derived foods that is highly resistant to pepsin digestion. Int Arch Allergy Immunol 2000;122:20-32.
130. Vassilopoulou E, Rigby N, Moreno FJ, et al. Effect of in vitro gastric and duodenal digestion on the allergenicity of grape lipid transfer protein. J Allergy Clin Immunol 2006;118:473-80.
131. Shewry PR, Halford NG, Belton PS, Tatham AS. The structure and properties of gluten: an elastic protein from wheat grain. Philos Trans Roy Soc Lond B Biol Sci 2002;357:133-42.
132. Matsuo H, Morita E, Tatham AS, et al. Identification of the IgE-binding epitope in omega-5 gliadin, a major allergen in wheat-dependent exercise-induced anaphylaxis. J Biol Chem 2004;279:12135-40.
133. Watanabe M, Tanabe S, Suzuki T, et al. Primary structure of an allergenic peptide occurring in the chymotryptic hydrolysate of gluten. Biosci Biotechnol Biochem 1995;59:1596-7.
134. Tanabe S, Arai S, Yanagihara Y, et al. A major wheat allergen has a Gln-Gln-Gln-Pro-Pro motif identified as an IgE-binding epitope. Biochem Biophys Res Commun 1996;219:290-3.
135. Simonato B, Pasini G, Giannattasio M, et al. Food allergy to wheat products: the effect of bread baking and in vitro digestion on wheat allergenic proteins. A study with bread dough, crumb, and crust. JAgricFood Chem 2001;49:5668-73.
136. Simonato B, De Lazzari F, Pasini G, et al. IgE binding to soluble and insoluble wheat flour proteins in atopic and non-atopic patients suffering from gastrointestinal symptoms after wheat ingestion. Clin Exp Allergy 2001;31:1771-8.
137. Carbonero P, García-Olmedo F. A Multigene Family of Trypsin/Alpha-Amylase Inhibitors from Cereals. Dordrecht, The Netherlands: Kluwer Academic Publishers, 1999.
138. James JM, Sixbey JP, Helm RM, et al. Wheat alpha-amylase inhibitor: a second route of allergic sensitization. J Allergy Clin Immunol 1997;99:239-44.
139. Shewry PR, Pandya MJ. The 2S Albumin Storage Proteins. Dordrecht, The Netherlands: Kluwer Academic Publishers, 1999.
140. Shibasaki M, Suzuki S, Tajima S, et al. Allergenicity of major component proteins of soybean. Int Arch Allergy Appl Immunol 1980;61:441-8.
141. Duro G, Colombo P, Costa MA, et al. cDNA cloning, sequence analysis and allergological characterization of Par j 2.0101, a new major allergen of the Parietaria judaica pollen. FEBS Lett 1996;399:295-8.
142. Tejera ML, Villalba M, Batanero E, Rodriguez R. Identification, isolation, and characterization of Ole e 7, a new allergen of olive tree pollen. J Allergy Clin Immunol 1999;104:797-802.
143. Pastorello EA, Farioli L, Robino AM, et al. A lipid transfer protein involved in occupational sensitization to spelt. J Allergy Clin Immunol 2001;108:145-6.
144. Pastorello EA, Vieths S, Pravettoni V, et al. Identification of hazelnut major allergens in sensitive patients with positive double-blind, placebo-controlled food challenge results. J Allergy Clin Immunol 2002;109:563-70.
145. Mills ENC, Jenkins JA, Bannon GA. Plant Seed Globulin Allergens. Oxford: Blackwell Publishing, 2004.
146. Burks Jr AW, Brooks JR, Sampson HA. Allergenicity of major component proteins of soybean determined by enzyme-linked immunosorbent assay (ELISA) and immunoblotting in children with atopic dermatitis and positive soy challenges. J Allergy Clin Immunol 1988;81:1135-42.
147. Lopez-Torrejon G, Salcedo G, Martin-Esteban M, et al. Len c 1, a major allergen and violin from lentil seeds: protein isolation and cDNA cloning. J Allergy Clin Immunol 2003;112:1208-15.
148. Roux KH, Teuber SS, Sathe SK. Tree nut allergens. Int Arch Allergy Immunol 2003;131:234-44.
149. Beyer K, Grishina G, Bardina L, et al. Identification of an 11S globulin as a major hazelnut food allergen in hazelnut-induced systemic reactions. J Allergy Clin Immunol 2002;110:517-23.
150. Mills EN, Huang L, Noel TR, et al. Formation of thermally induced aggregates of the soya globulin beta-conglycinin. Biochim Biophys Acta 2001;1547:339-50.
151. Mills EN, Marigheto NA, Wellner N, et al. Thermally induced structural changes in glycinin, the 11S globulin of soya bean (Glycine max)-an in situ spectroscopic study. Biochim Biophys Acta 2003;1648:105-14.
152. Yamauchi F, Yamagishi T, Iwabuchi S. Molecular understanding of heat-induced phenomena of soybean protein. Food Rev Intt 1991;7:283-322.
153. Maleki SJ, Kopper RA, Shin DS, et al. Structure of the major peanut allergen Ara h 1 may protect IgE-binding epitopes from degradation. J Immunol 2000;164:5844-9.
154. Kopper RA, Odum NJ, Sen M, et al. Peanut protein allergens: gastric digestion is carried out exclusively by pepsin. J Allergy Clin Immunol 2004;114:614-8.
155. Shin DS, Compadre CM, Maleki SJ, et al. Biochemical and structural analysis of the IgE binding sites on ara h1, an abundant and highly allergenic peanut protein. J Biol Chem 1998;273:13753-9.
156. Eiwegger T, Rigby N, Mondoulet L, et al. Gastro-duodenal digestion products of the major peanut allergen Ara h 1 retain an allergenic potential. Clin Exp Allergy 2006;36:1281-8.
157. Vieths S, Scheurer S, Ballmer-Weber B. Current understanding of cross-reactivity of food allergens and pollen. Ann NY Acad Sci 2002;964:47-68.
158. Mittag D, Akkerdaas J, Ballmer-Weber BK, et al. Ara h 8, a Bet v 1-homologous allergen from peanut, is a major allergen in patients with combined birch pollen and peanut allergy. J Allergy Clin Immunol 2004;114:1410-17.
159. Mittag D, Vieths S, Vogel L, et al. Birch pollen-related food allergy to legumes: identification and characterization of the Bet v 1 homologue in mungbean (Vigna radiata), Vig r 1. Clin Exp Allergy 2005;35:1049-55.
160. Bolhaar ST, van Ree R, Ma Y, et al. Severe allergy to sharon fruit caused by birch pollen. Int Arch Allergy Immunol 2005;136:45-52.
161. Bolhaar ST, Ree R, Bruijnzeel-Koomen CA, et al. Allergy to jackfruit: a novel example of Bet v 1-related food allergy. Allergy 2004;59:1187-92.
162. Breiteneder H, Pettenburger K, Bito A, et al. The gene coding for the major birch pollen allergen Betv1, is highly homologous to a pea disease resistance response gene. EMBO J 1989;8:1935-8.
163. Hoffmann-Sommergruber K. Plant allergens and pathogenesis-related proteins. What do they have in common? Int Arch Allergy Immunol 2000;122:155-66.
164. Markovic-Housley Z, Degano M, Lamba D, et al. Crystal structure of a hypoallergenic isoform of the major birch pollen allergen Bet v 1 and its likely biological function as a plant steroid carrier. J Mol Biol 2003;325:123-33.
165. Gajhede M, Osmark P, Poulsen FM, et al. X-ray and NMR structure of Bet v 1, the origin of birch pollen allergy. Nat Struct Biol 1996;3:1040-5.
166. Neudecker P, Schweimer K, Nerkamp J, et al. Allergic crossreactivity made visible: solution structure of the major cherry allergen Pru av 1. J Biol Chem 2001;276:22756-63.
167. Schirmer T, Hoffimann-Sommergrube K, Susani M, et al. Crystal structure of the major celery allergen Api g 1: molecular analysis of cross-reactivity. J Mol Biol 2005;351:1101-9.
168. Bohle B, Radakovics A, Jahn-Schmid B, et al. Bet v 1, the major birch pollen allergen, initiates sensitization to Api g 1, the major allergen in celery: evidence at the T cell level. Eur J Immunol 2003;33:3303-10.
169. Reekers R, Busche M, Wittmann M, et al. Birch pollen-related foods trigger atopic dermatitis in patients with specific cutaneous T-cell responses to birch pollen antigens. J Allergy Clin Immunol 1999;104:466-72.
170. Schimek EM, Zwolfer B, Briza P, et al. Gastrointestinal digestion of Bet v 1-homologous food allergens destroys their mediator-releasing, but not T cell-activating, capacity. J Allergy Clin Immunol 2005;116:1327-33.
171. Bohle B, Zwolfer B, Heratizadeh A, et al. Cooking birch pollen-related food: divergent consequences for IgE-and T cell-mediated reactivity in vitro and in vivo. J Allergy Clin Immunol 2006;118:242-9.
172. Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J 1991;280:309-16.
173. Kasprzewska A. Plant chitinases-regulation and function. Cell Mol Biol Lett 2003;8:809-24.
174. Beintema JJ. Structural features of plant chitinases and chitin-binding proteins. FEBS Lett 1994;350:159-63.
175. Salcedo G, Diaz-Perales A, Sanchez-Monge R. The role of plant panallergens in sensitization to natural rubber latex. Curr Opin Allergy Clin Immunol 2001;1:177-83.
176. Sowka S, Hsieh LS, Krebitz M, et al. Identification and cloning of prs a 1, a 32-kDa endochitinase and major allergen of avocado, and its expression in the yeast Pichia pastoris. J Biol Chem 199823;273:28091-7.
177. Sanchez-Monge R, Blanco C, Diaz-Perales A, et al. Isolation and characterization of major banana allergens: identification as fruit class I chitinases. Clin Exp Allergy 1999;29:673-80.
178. Diaz-Perales A, Collada C, Blanco C, et al. Class I chitinases with hevein-like domain, but not class II enzymes, are relevant chestnut and avocado allergens. J Allergy Clin Immunol 1998;102:127-33.
179. Diaz-Perales A, Blanco C, Sanchez-Monge R, et al. Analysis of avocado allergen (Prs a 1) IgE-binding peptides generated by simulated gastric fluid digestion. J Allergy Clin Immunol 2003;112:1002-7.
180. Breiteneder H, Mills EN. Molecular properties of food allergens. J Allergy Clin Immunol 2005;115:14-23; quiz 4.
181. Rawlings ND, Barrett AJ. Evolutionary families of peptidases. Biochem J 1993;290:205-18.
182. Kalinski A, Weisemann JM, Matthews BF, et al. Molecular cloning of a protein associated with soybean seed oil bodies that is similar to thiol proteases of the papain family. J Biol Chem 1990;265:13843-8.
183. Radauer C, Willerroider M, Fuchs H, et al. Cross-reactive and
184. Witke W. The role of profilin complexes in cell motility and other cellular processes. Trends Cell Biol 2004;14:461-9.
185. Radauer C, Hoffimann-Sommergrube K. Profilins. Oxford: Blackwell Publishing, 2004.
186. Thorn KS, Christensen HE, Shigeta R, et al. The crystal structure of a major allergen from plants. Structure 1997;5:19-32.
187. Fedorov AA, Ball T, Mahoney NM, et al. The molecular basis for allergen cross-reactivity: crystal structure and IgE-epitope mapping of birch pollen profilin. Structure 1997;5:33-45.
188. Mari A. Multiple pollen sensitization: a molecular approach to the diagnosis. Int Arch Allergy Immunol 2001;125:57-65.
189. Asero R, Mistrello G, Roncarolo D, et al. Detection of clinical markers of sensitization to profilin in patients allergic to plant-derived foods. J Allergy Clin Immunol 2003;112:427-32.
190. Wensing M, Akkerdaas JH, van Leeuwen WA, et al. IgE to Bet v 1 and profilin: cross-reactivity patterns and clinical relevance. J Allergy Clin Immunol 2002;110:435-42.
191. Valenta R, Duchene M, Pettenburger K, et al. Identification of profilin as a novel pollen allergen; IgE autoreactivity in sensitized individuals. Science 1991;253:557-60.
192. Moroz LA, Yang WH. Kunitz soybean trypsin inhibitor: a specific allergen in food anaphylaxis. N Engl J Med 1980;302:1126-8.
193. Burks AW, Cockrell G, Connaughton C, et al. Identification of peanut agglutinin and soybean trypsin inhibitor as minor legume allergens. Int Arch Allergy Immunol 1994;105:143-9.
194. Seppala U, Majamaa H, Turjanmaa K, et al. Identification of four novel potato (Solanum tuberosum) allergens belonging to the family of soybean trypsin inhibitors. Allergy 2001;56:619-26.
195. van Loon LC, Rep M, Pieterse CM. Significance of inducible defense-related proteins in infected plants. Annu Rev Phytopathol 2006;44:135-62.
196. Krebitz M, Wagner B, Ferreira F, et al. Plant-based heterologous expression of Mal d 2, a thaumatin-like protein and allergen of apple (Malus domestica), and its characterization as an antifungal protein. J Mol Biol 2003;329:721-30.
197. Fuchs HC, Hoffmann-Sommergrube K, Wagner B, et al. Heterologous expression in Nicotiana benthamiana of Cap a 1, a thaumatin-like protein and major allergen from bell pepper (Capsicum annuum). J Allergy Clin Immunol 2002;109(S):134-5.
198. Inschlag C, Hoffmann-Sommergruber K, O'Riordain G, et al. Biochemical characterization of Pru a 2, a 23-kD thaumatin-like protein representing a potential major allergen in cherry (Prunus avium). Int Arch Allergy Immunol 1998;116:22-8.
199. Fuchs HC, Bohle B, Dall'Antonia Y, et al. Natural and recombinant molecules of the cherry allergen Pru av 2 show diverse structural and B cell characteristics but similar T cell reactivity. Clin Exp Allergy 2006;36:359-68.
200. Gavrovic-Jankulovic M, cIrkovic T, Vuckovic O, et al. Isolation and biochemical characterization of a thaumatin-like kiwi allergen. J Allergy Clin Immunol 2002;110:805-10.
201. Roberts WK, Selitrennikoff CP. Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity. J Gen Microbiol 1990;136:1771-8.
202. Flamini R, De Rosso M. Mass spectrometry in the analysis of grape and wine proteins. Expert Rev Proteomics 2006;3:321-31.
203. Lack G, Golding J. Peanut and nut allergy. Reduced exposure might increase allergic sensitisation. BMJ 1996;313:300.
204. Strid J, Thomson M, Hourihane J, et al. A novel model of sensitization and oral tolerance to peanut protein. Immunology 2004;113:293-303.
205. Strid J, Hourihane J, Kimber I, et al. Epicutaneous exposure to peanut protein prevents oral tolerance and enhances allergic sensitization. Clin Exp Allergy 2005;35:757-66.
206. Hoffmann-Sommergruber K. Pathogenesis-related (PR)-proteins identified as allergens. Biochem Soc Trans 2002;30:930-5.
207. Van Loon LC, Van Strien EA. The families of pathogenesis related proteins, their activities, and comparative analysis of PR-1-type proteins. Physiol Mol Plant Pathol 1999;5:85-97.