Official reprint from UpToDate®
www.uptodate.com ©2017 UpToDate, Inc. and/or its affiliates. All Rights Reserved.

Molecular features of food allergens

Heimo Breiteneder, PhD
Section Editor
Scott H Sicherer, MD, FAAAAI
Deputy Editor
Elizabeth TePas, MD, MS


Many of the allergen-containing protein families, and, consequently, their individual members, possess characteristic molecular features that promote allergenicity [1-5].

A food allergen must possess certain structural and physicochemical properties that prevent it from being destroyed by the digestive process in order for a predisposed individual to become sensitized via exposure through the gastrointestinal tract [6]. These properties ensure that enough of the protein survives in a sufficiently intact form to be taken up by the gut and to be recognized by the mucosal immune system. Processing may alter the allergenicity of food [7,8].

In addition, food allergens must possess the ability to induce a T helper cell type 2 (Th2)-biased, allergen-specific immune response via certain structural features of the allergen or association of the allergen with ligand molecules that can act as adjuvants [9]. Studies of the interaction of allergens and the innate immune system have highlighted the roles of pattern recognition receptors in initiating Th2-biased immune responses [10-12]. Several members of major allergen families bind lipid ligands via hydrophobic cavities or electrostatic or hydrophobic interactions [13]. These lipids, either present in the allergen source or originating from microbial contaminations, modulate the immune response of predisposed individuals by interacting with their innate immune system.

This topic reviews the structural and physicochemical features common to food allergens. The European Academy of Allergy and Clinical Immunology (EAACI) published the EAACI Molecular Allergology User’s Guide in May 2016, which is freely available online and contains a wealth of information on molecular features of allergens [14]. The clinical features and cross-reactivity of food allergens and the pathogenesis of food allergy are discussed separately. (See "Food allergens: Overview of clinical features and cross-reactivity" and "Pathogenesis of food allergy".)

A list of protein families that contain allergens can be accessed from the AllFam database of allergen families website [4]. The World Health Organization (WHO)/International Union of Immunological Societies (IUIS) Allergen Nomenclature database contains information on all officially recognized allergens. This database is supplemented by data from AllergenOnline. The protein family classification is based upon the Pfam database.

To continue reading this article, you must log in with your personal, hospital, or group practice subscription. For more information on subscription options, click below on the option that best describes you:

Subscribers log in here

Literature review current through: Nov 2017. | This topic last updated: Nov 22, 2016.
The content on the UpToDate website is not intended nor recommended as a substitute for medical advice, diagnosis, or treatment. Always seek the advice of your own physician or other qualified health care professional regarding any medical questions or conditions. The use of this website is governed by the UpToDate Terms of Use ©2017 UpToDate, Inc.
  1. Breiteneder H, Radauer C. A classification of plant food allergens. J Allergy Clin Immunol 2004; 113:821.
  2. 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.
  3. Jenkins JA, Griffiths-Jones S, Shewry PR, et al. Structural relatedness of plant food allergens with specific reference to cross-reactive allergens: an in silico analysis. J Allergy Clin Immunol 2005; 115:163.
  4. Radauer C, Bublin M, Wagner S, et al. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol 2008; 121:847.
  5. Jenkins JA, Breiteneder H, Mills EN. Evolutionary distance from human homologs reflects allergenicity of animal food proteins. J Allergy Clin Immunol 2007; 120:1399.
  6. Breiteneder H, Clare Mills EN. Plant food allergens--structural and functional aspects of allergenicity. Biotechnol Adv 2005; 23:395.
  7. Mills EN, Mackie AR. The impact of processing on allergenicity of food. Curr Opin Allergy Clin Immunol 2008; 8:249.
  8. Nowak-Wegrzyn A, Fiocchi A. Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity. Curr Opin Allergy Clin Immunol 2009; 9:234.
  9. Ruiter B, Shreffler WG. Innate immunostimulatory properties of allergens and their relevance to food allergy. Semin Immunopathol 2012; 34:617.
  10. Minnicozzi M, Sawyer RT, Fenton MJ. Innate immunity in allergic disease. Immunol Rev 2011; 242:106.
  11. Pulendran B, Artis D. New paradigms in type 2 immunity. Science 2012; 337:431.
  12. Thomas WR. Allergen ligands in the initiation of allergic sensitization. Curr Allergy Asthma Rep 2014; 14:432.
  13. Bublin M, Eiwegger T, Breiteneder H. Do lipids influence the allergic sensitization process? J Allergy Clin Immunol 2014; 134:521.
  14. Matricardi PM, Kleine-Tebbe J, Hoffmann HJ, et al. EAACI Molecular Allergology User's Guide. Pediatr Allergy Immunol 2016; 27 Suppl 23:1.
  15. Fass D. Disulfide bonding in protein biophysics. Annu Rev Biophys 2012; 41:63.
  16. 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.
  17. AllFam is a database of allergen-containing protein families that is available on the web at www.meduniwien.ac.at/allergens/allfam/ (Accessed on February 11, 2010).
  18. Domínguez J, Cuevas M, Ureña V, et al. Purification and characterization of an allergen of mustard seed. Ann Allergy 1990; 64:352.
  19. Pantoja-Uceda D, Palomares O, Bruix M, et al. Solution structure and stability against digestion of rproBnIb, a recombinant 2S albumin from rapeseed: relationship to its allergenic properties. Biochemistry 2004; 43:16036.
  20. Moreno FJ, Maldonado BM, Wellner N, Mills EN. Thermostability and in vitro digestibility of a purified major allergen 2S albumin (Ses i 1) from white sesame seeds (Sesamum indicum L.). Biochim Biophys Acta 2005; 1752:142.
  21. Murtagh GJ, Archer DB, Dumoulin M, et al. In vitro stability and immunoreactivity of the native and recombinant plant food 2S albumins Ber e 1 and SFA-8. Clin Exp Allergy 2003; 33:1147.
  22. 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.
  23. Koppelman SJ, Nieuwenhuizen WF, Gaspari M, et al. Reversible denaturation of Brazil nut 2S albumin (Ber e1) and implication of structural destabilization on digestion by pepsin. J Agric Food Chem 2005; 53:123.
  24. Suhr M, Wicklein D, Lepp U, Becker WM. Isolation and characterization of natural Ara h 6: evidence for a further peanut allergen with putative clinical relevance based on resistance to pepsin digestion and heat. Mol Nutr Food Res 2004; 48:390.
  25. Lehmann K, Schweimer K, Reese G, et al. Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem J 2006; 395:463.
  26. Masthoff LJ, Mattsson L, Zuidmeer-Jongejan L, et al. Sensitization to Cor a 9 and Cor a 14 is highly specific for a hazelnut allergy with objective symptoms in Dutch children and adults. J Allergy Clin Immunol 2013; 132:393.
  27. Pfeifer S, Bublin M, Dubiela P, et al. Cor a 14, the allergenic 2S albumin from hazelnut, is highly thermostable and resistant to gastrointestinal digestion. Mol Nutr Food Res 2015; 59:2077.
  28. Cabanillas B, Crespo JF, Maleki SJ, et al. Pin p 1 is a major allergen in pine nut and the first food allergen described in the plant group of gymnosperms. Food Chem 2016; 210:70.
  29. Downs ML, Baumert JL, Taylor SL, Mills EN. Mass spectrometric analysis of allergens in roasted walnuts. J Proteomics 2016; 142:62.
  30. Downs ML, Simpson A, Custovic A, et al. Insoluble and soluble roasted walnut proteins retain antibody reactivity. Food Chem 2016; 194:1013.
  31. Yeats TH, Rose JK. The biochemistry and biology of extracellular plant lipid-transfer proteins (LTPs). Protein Sci 2008; 17:191.
  32. van Ree R. Clinical importance of non-specific lipid transfer proteins as food allergens. Biochem Soc Trans 2002; 30:910.
  33. 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.
  34. Duffort OA, Polo F, Lombardero M, et al. Immunoassay to quantify the major peach allergen Pru p 3 in foodstuffs. Differential allergen release and stability under physiological conditions. J Agric Food Chem 2002; 50:7738.
  35. Gaier S, Marsh J, Oberhuber C, et al. Purification and structural stability of the peach allergens Pru p 1 and Pru p 3. Mol Nutr Food Res 2008; 52 Suppl 2:S220.
  36. Prandi B, Farioli L, Tedeschi T, et al. Simulated gastrointestinal digestion of Pru ar 3 apricot allergen: assessment of allergen resistance and characterization of the peptides by ultra-performance liquid chromatography/electrospray ionisation mass spectrometry. Rapid Commun Mass Spectrom 2012; 26:2905.
  37. Palacin A, Varela J, Quirce S, et al. Recombinant lipid transfer protein Tri a 14: a novel heat and proteolytic resistant tool for the diagnosis of baker's asthma. Clin Exp Allergy 2009; 39:1267.
  38. Pastorello EA, Pompei C, Pravettoni V, et al. Lipid-transfer protein is the major maize allergen maintaining IgE-binding activity after cooking at 100 degrees C, as demonstrated in anaphylactic patients and patients with positive double-blind, placebo-controlled food challenge results. J Allergy Clin Immunol 2003; 112:775.
  39. Scheurer S, Lauer I, Foetisch K, et al. Strong allergenicity of Pru av 3, the lipid transfer protein from cherry, is related to high stability against thermal processing and digestion. J Allergy Clin Immunol 2004; 114:900.
  40. Schocker F, Lüttkopf D, Müller U, et al. IgE binding to unique hazelnut allergens: identification of non pollen-related and heat-stable hazelnut allergens eliciting severe allergic reactions. Eur J Nutr 2000; 39:172.
  41. Schocker F, Lüttkopf 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.
  42. Vejvar E, Himly M, Briza P, et al. Allergenic relevance of nonspecific lipid transfer proteins 2: Identification and characterization of Api g 6 from celery tuber as representative of a novel IgE-binding protein family. Mol Nutr Food Res 2013; 57:2061.
  43. Mamone G, Nitride C, Picariello G, et al. Tracking the fate of pasta (T. Durum semolina) immunogenic proteins by in vitro simulated digestion. J Agric Food Chem 2015; 63:2660.
  44. Pastorello EA, Farioli L, Conti A, et al. Wheat IgE-mediated food allergy in European patients: alpha-amylase inhibitors, lipid transfer proteins and low-molecular-weight glutenins. Allergenic molecules recognized by double-blind, placebo-controlled food challenge. Int Arch Allergy Immunol 2007; 144:10.
  45. Junker Y, Zeissig S, Kim SJ, et al. Wheat amylase trypsin inhibitors drive intestinal inflammation via activation of toll-like receptor 4. J Exp Med 2012; 209:2395.
  46. Consolini M, Sega M, Zanetti C, et al. Emulsification of simulated gastric fluids protects wheat alpha-amylase inhibitor 0.19 epitopes from digestion. Food Analy Methods 2012; 5:234.
  47. Thompson CE, Fernandes CL, de Souza ON, et al. Molecular modeling of pathogenesis-related proteins of family 5. Cell Biochem Biophys 2006; 44:385.
  48. Roberts WK, Selitrennikoff CP. Zeamatin, an antifungal protein from maize with membrane-permeabilizing activity. J Gen Microbiol 1990; 136:1771.
  49. 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.
  50. Smole U, Bublin M, Radauer C, et al. Mal d 2, the thaumatin-like allergen from apple, is highly resistant to gastrointestinal digestion and thermal processing. Int Arch Allergy Immunol 2008; 147:289.
  51. 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.
  52. Gavrović-Jankulović M, ćIrković T, Vucković O, et al. Isolation and biochemical characterization of a thaumatin-like kiwi allergen. J Allergy Clin Immunol 2002; 110:805.
  53. Bublin M, Radauer C, Knulst A, et al. Effects of gastrointestinal digestion and heating on the allergenicity of the kiwi allergens Act d 1, actinidin, and Act d 2, a thaumatin-like protein. Mol Nutr Food Res 2008; 52:1130.
  54. 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.
  55. Palacín A, Tordesillas L, Gamboa P, et al. Characterization of peach thaumatin-like proteins and their identification as major peach allergens. Clin Exp Allergy 2010; 40:1422.
  56. Muñoz-García E, Luengo-Sánchez O, Haroun-Díaz E, et al. Identification of thaumatin-like protein and aspartyl protease as new major allergens in lettuce (Lactuca sativa). Mol Nutr Food Res 2013; 57:2245.
  57. Hegde VL, Ashok Kumar HG, Sreenath K, et al. Identification and characterization of a basic thaumatin-like protein (TLP 2) as an allergen in sapodilla plum (Manilkara zapota). Mol Nutr Food Res 2014; 58:894.
  58. Flamini R, De Rosso M. Mass spectrometry in the analysis of grape and wine proteins. Expert Rev Proteomics 2006; 3:321.
  59. Torres M, Alvarez-García E, Bartra J, et al. The allergenic structure of the thaumatin-like protein Ole e 13 is degraded by processing of raw olive fruits. J Investig Allergol Clin Immunol 2014; 24:162.
  60. Volpicella M, Leoni C, Fanizza I, et al. Overview of plant chitinases identified as food allergens. J Agric Food Chem 2014; 62:5734.
  61. Dìaz-Perales A, Sánchez-Monge R, Blanco C, et al. What is the role of the hevein-like domain of fruit class I chitinases in their allergenic capacity? Clin Exp Allergy 2002; 32:448.
  62. Díaz-Perales A, Blanco C, Sánchez-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.
  63. Roychaudhuri R, Sarath G, Zeece M, Markwell J. Stability of the allergenic soybean Kunitz trypsin inhibitor. Biochim Biophys Acta 2004; 1699:207.
  64. Tamburrini M, Cerasuolo I, Carratore V, et al. Kiwellin, a novel protein from kiwi fruit. Purification, biochemical characterization and identification as an allergen*. Protein J 2005; 24:423.
  65. Helenius A, Aebi M. Intracellular functions of N-linked glycans. Science 2001; 291:2364.
  66. Wormald MR, Dwek RA. Glycoproteins: glycan presentation and protein-fold stability. Structure 1999; 7:R155.
  67. Wang C, Eufemi M, Turano C, Giartosio A. Influence of the carbohydrate moiety on the stability of glycoproteins. Biochemistry 1996; 35:7299.
  68. Opdenakker G, Rudd PM, Ponting CP, Dwek RA. Concepts and principles of glycobiology. FASEB J 1993; 7:1330.
  69. van Ree R. Carbohydrate epitopes and their relevance for the diagnosis and treatment of allergic diseases. Int Arch Allergy Immunol 2002; 129:189.
  70. Altmann F. The role of protein glycosylation in allergy. Int Arch Allergy Immunol 2007; 142:99.
  71. Commins SP, Satinover SM, Hosen J, et al. Delayed anaphylaxis, angioedema, or urticaria after consumption of red meat in patients with IgE antibodies specific for galactose-alpha-1,3-galactose. J Allergy Clin Immunol 2009; 123:426.
  72. Commins SP, Platts-Mills TA. Anaphylaxis syndromes related to a new mammalian cross-reactive carbohydrate determinant. J Allergy Clin Immunol 2009; 124:652.
  73. Steinke JW, Platts-Mills TA, Commins SP. The alpha-gal story: lessons learned from connecting the dots. J Allergy Clin Immunol 2015; 135:589.
  74. Commins SP, Jerath MR, Cox K, et al. Delayed anaphylaxis to alpha-gal, an oligosaccharide in mammalian meat. Allergol Int 2016; 65:16.
  75. Picariello G, Amigo-Benavent M, del Castillo MD, Ferranti P. Structural characterization of the N-glycosylation of individual soybean β-conglycinin subunits. J Chromatogr A 2013; 1313:96.
  76. Amigo Benavent M, Clemente A, Ferranti P, et al. Digestibility and immunoreactivity of soybean beta-conglycinin and its deglycosylated form. Food Chem 2011; 129:1598.
  77. van Ree R, Cabanes-Macheteau M, Akkerdaas J, et al. Beta(1,2)-xylose and alpha(1,3)-fucose residues have a strong contribution in IgE binding to plant glycoallergens. J Biol Chem 2000; 275:11451.
  78. Sanchez-Monge R, Lopez-Torrejón G, Pascual CY, et al. Vicilin and convicilin are potential major allergens from pea. Clin Exp Allergy 2004; 34:1747.
  79. Pedrosa C, De Felice FG, Trisciuzzi C, Ferreira ST. Selective neoglycosylation increases the structural stability of vicilin, the 7S storage globulin from pea seeds. Arch Biochem Biophys 2000; 382:203.
  80. Garrido-Arandia M, Murua-García A, Palacin A, et al. The role of N-glycosylation in kiwi allergy. Food Sci Nutr 2014; 2:260.
  81. Dunker AK, Babu MM, Barbar E, et al. What's in a name? Why these proteins are intrinsically disordered: Why these proteins are intrinsically disordered. Intrinsically Disord Proteins 2013; 1:e24157.
  82. Dunker AK, Lawson JD, Brown CJ, et al. Intrinsically disordered protein. J Mol Graph Model 2001; 19:26.
  83. Holt C, Sawyer L. Caseins as rheomorphic proteins: interpretation of the primary and secondary structures of alpha S1 - beta- and kappa- caseins. J Chem Soc Farad Trans 1993; 89:2683.
  84. Morisawa Y, Kitamura A, Ujihara T, et al. Effect of heat treatment and enzymatic digestion on the B cell epitopes of cow's milk proteins. Clin Exp Allergy 2009; 39:918.
  85. Oldfield CJ, Dunker AK. Intrinsically disordered proteins and intrinsically disordered protein regions. Annu Rev Biochem 2014; 83:553.
  86. Shewry PR, Tatham AS. The characterisation, structures and evolutionary relationships of prolamins, Kluwer Academic Publishers, Dordrecht 1999.
  87. Berin MC, Sampson HA. Mucosal immunology of food allergy. Curr Biol 2013; 23:R389.
  88. Terras FR, Schoofs HM, De Bolle MF, et al. Analysis of two novel classes of plant antifungal proteins from radish (Raphanus sativus L.) seeds. J Biol Chem 1992; 267:15301.
  89. Terras F, Schoofs H, Thevissen K, et al. Synergistic Enhancement of the Antifungal Activity of Wheat and Barley Thionins by Radish and Oilseed Rape 2S Albumins and by Barley Trypsin Inhibitors. Plant Physiol 1993; 103:1311.
  90. Oñaderra M, Monsalve RI, Mancheño JM, et al. Food mustard allergen interaction with phospholipid vesicles. Eur J Biochem 1994; 225:609.
  91. Zachowski A. Phospholipids in animal eukaryotic membranes: transverse asymmetry and movement. Biochem J 1993; 294 ( Pt 1):1.
  92. Burnett GR, Rigby NM, Mills EN, et al. Characterization of the emulsification properties of 2S albumins from sunflower seed. J Colloid Interface Sci 2002; 247:177.
  93. Pantoja-Uceda D, Shewry PR, Bruix M, et al. Solution structure of a methionine-rich 2S albumin from sunflower seeds: relationship to its allergenic and emulsifying properties. Biochemistry 2004; 43:6976.
  94. Moreno FJ, Rubio LA, Olano A, Clemente A. Uptake of 2S albumin allergens, Ber e 1 and Ses i 1, across human intestinal epithelial Caco-2 cell monolayers. J Agric Food Chem 2006; 54:8631.
  95. Price DB, Ackland ML, Burks W, et al. Peanut allergens alter intestinal barrier permeability and tight junction localisation in Caco-2 cell cultures. Cell Physiol Biochem 2014; 33:1758.
  96. Wal JM. Cow's milk allergens. Allergy 1998; 53:1013.
  97. Moreno FJ, Mackie AR, Mills EN. Phospholipid interactions protect the milk allergen alpha-lactalbumin from proteolysis during in vitro digestion. J Agric Food Chem 2005; 53:9810.
  98. Kader JC. Lipid-transfer proteins: A puzzling family of plant proteins. Trends Plant Sci 1997; 2:66.
  99. Subirade M, Salesse C, Marion D, Pézolet M. Interaction of a nonspecific wheat lipid transfer protein with phospholipid monolayers imaged by fluorescence microscopy and studied by infrared spectroscopy. Biophys J 1995; 69:974.
  100. Douliez JP, Sy D, Vovelle F, Marion D. Interaction of surfactants and polymer-grafted lipids with a plant lipid transfer protein, LTP1. Langmuir 2002; 18:7309.
  101. Tordesillas L, Gómez-Casado C, Garrido-Arandia M, et al. Transport of Pru p 3 across gastrointestinal epithelium - an essential step towards the induction of food allergy? Clin Exp Allergy 2013; 43:1374.
  102. Leone P, Menu-Bouaouiche L, Peumans WJ, et al. Resolution of the structure of the allergenic and antifungal banana fruit thaumatin-like protein at 1.7-A. Biochimie 2006; 88:45.
  103. Vigers AJ, Roberts WK, Selitrennikoff CP. A new family of plant antifungal proteins. Mol Plant Microbe Interact 1991; 4:315.
  104. Batalia MA, Monzingo AF, Ernst S, et al. The crystal structure of the antifungal protein zeamatin, a member of the thaumatin-like, PR-5 protein family. Nat Struct Biol 1996; 3:19.
  105. Anzlovar S, Dalla Serra M, Dermastia M, Menestrina G. Membrane permeabilizing activity of pathogenesis-related protein linusitin. Mol Plant Microbe Interact 1998; 11:610.
  106. Radauer C, Lackner P, Breiteneder H. The Bet v 1 fold: an ancient, versatile scaffold for binding of large, hydrophobic ligands. BMC Evol Biol 2008; 8:286.
  107. Kleine-Tebbe J, Vogel L, Crowell DN, et al. Severe oral allergy syndrome and anaphylactic reactions caused by a Bet v 1- related PR-10 protein in soybean, SAM22. J Allergy Clin Immunol 2002; 110:797.
  108. Berkner H, Neudecker P, Mittag D, et al. Cross-reactivity of pollen and food allergens: soybean Gly m 4 is a member of the Bet v 1 superfamily and closely resembles yellow lupine proteins. Biosci Rep 2009; 29:183.
  109. Mogensen JE, Ferreras M, Wimmer R, et al. The major allergen from birch tree pollen, Bet v 1, binds and permeabilizes membranes. Biochemistry 2007; 46:3356.
  110. de Jong AJ, Kloppenburg M, Toes RE, Ioan-Facsinay A. Fatty acids, lipid mediators, and T-cell function. Front Immunol 2014; 5:483.
  111. Douliez JP, Jégou 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.
  112. Douliez JP, Michon T, Marion D. Steady-state tyrosine fluorescence to study the lipid-binding properties of a wheat non-specific lipid-transfer protein (nsLTP1). Biochim Biophys Acta 2000; 1467:65.
  113. 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.
  114. Pato C, Le Borgne M, Le Baut G, et al. Potential application of plant lipid transfer proteins for drug delivery. Biochem Pharmacol 2001; 62:555.
  115. Sy D, Le Gravier Y, Goodfellow J, Vovelle F. Protein stability and plasticity of the hydrophobic cavity in wheat ns-LTP. J Biomol Struct Dyn 2003; 21:15.
  116. 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.
  117. Abdullah SU, Alexeev Y, Johnson PE, et al. Ligand binding to an Allergenic Lipid Transfer Protein Enhances Conformational Flexibility resulting in an Increase in Susceptibility to Gastroduodenal Proteolysis. Sci Rep 2016; 6:30279.
  118. Dearman RJ, Alcocer MJ, Kimber I. Influence of plant lipids on immune responses in mice to the major Brazil nut allergen Ber e 1. Clin Exp Allergy 2007; 37:582.
  119. Ikura M. Calcium binding and conformational response in EF-hand proteins. Trends Biochem Sci 1996; 21:14.
  120. 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.
  121. Zuidmeer-Jongejan L, Huber H, Swoboda I, et al. Development of a hypoallergenic recombinant parvalbumin for first-in-man subcutaneous immunotherapy of fish allergy. Int Arch Allergy Immunol 2015; 166:41.
  122. 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.
  123. 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.
  124. Hilger C, Thill L, Grigioni F, et al. IgE antibodies of fish allergic patients cross-react with frog parvalbumin. Allergy 2004; 59:653.
  125. Elsayed S, Aas K. Characterization of a major allergen (cod). Observations on effect of denaturation on the allergenic activity. J Allergy 1971; 47:283.
  126. 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.
  127. Pervaiz S, Brew K. Homology of beta-lactoglobulin, serum retinol-binding protein, and protein HC. Science 1985; 228:335.
  128. O'Neill TE, Kinsella JE. Binding of alkanone flavours to beta-lactoglobulin: Effects of conformational and chemical modification. J Agric Food Chem 1987; 35:770.
  129. Takagi K, Teshima R, Okunuki H, Sawada J. Comparative study of in vitro digestibility of food proteins and effect of preheating on the digestion. Biol Pharm Bull 2003; 26:969.
  130. Taheri-Kafrani A, Gaudin JC, Rabesona H, et al. Effects of heating and glycation of beta-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. J Agric Food Chem 2009; 57:4974.
  131. Seutter von Loetzen C, Hoffmann T, Hartl MJ, et al. Secret of the major birch pollen allergen Bet v 1: identification of the physiological ligand. Biochem J 2014; 457:379.
  132. Pasternak O, Bujacz GD, Fujimoto Y, et al. Crystal structure of Vigna radiata cytokinin-specific binding protein in complex with zeatin. Plant Cell 2006; 18:2622.
  133. Hurlburt BK, Offermann LR, McBride JK, et al. Structure and function of the peanut panallergen Ara h 8. J Biol Chem 2013; 288:36890.
  134. Chirino AJ, Ary ML, Marshall SA. Minimizing the immunogenicity of protein therapeutics. Drug Discov Today 2004; 9:82.
  135. Wolf WJ, Nelsen TC. Partial purification and characterization of the 15S globulin of soybeans, a dimer of glycinin. J Agric Food Chem 1996; 44:785.
  136. Yamauchi F, Yamagishi T, Iwabuchi S. Molecular understanding of heat-induced phenomena of soybean protein. Food Rev Internat 1991; 7:283.
  137. 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.
  138. 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.
  139. Buttari B, Profumo E, Capozzi A, et al. Advanced glycation end products of human β₂ glycoprotein I modulate the maturation and function of DCs. Blood 2011; 117:6152.
  140. Maleki SJ, Chung SY, Champagne ET, Raufman JP. The effects of roasting on the allergenic properties of peanut proteins. J Allergy Clin Immunol 2000; 106:763.
  141. Chung SY, Butts CL, Maleki SJ, Champagne ET. Linking peanut allergenicity to the processes of maturation, curing, and roasting. J Agric Food Chem 2003; 51:4273.
  142. Gekko K, Timasheff SN. Mechanism of protein stabilization by glycerol: preferential hydration in glycerol-water mixtures. Biochemistry 1981; 20:4667.
  143. Koppelman SJ, Bruijnzeel-Koomen CA, Hessing M, de Jongh HH. Heat-induced conformational changes of Ara h 1, a major peanut allergen, do not affect its allergenic properties. J Biol Chem 1999; 274:4770.
  144. Gruber P, Becker WM, Hofmann T. Influence of the maillard reaction on the allergenicity of rAra h 2, a recombinant major allergen from peanut (Arachis hypogaea), its major epitopes, and peanut agglutinin. J Agric Food Chem 2005; 53:2289.
  145. Ilchmann A, Burgdorf S, Scheurer S, et al. Glycation of a food allergen by the Maillard reaction enhances its T-cell immunogenicity: role of macrophage scavenger receptor class A type I and II. J Allergy Clin Immunol 2010; 125:175.
  146. Hebling CM, McFarland MA, Callahan JH, Ross MM. Global proteomic screening of protein allergens and advanced glycation endproducts in thermally processed peanuts. J Agric Food Chem 2013; 61:5638.
  147. Mueller GA, Maleki SJ, Johnson K, et al. Identification of Maillard reaction products on peanut allergens that influence binding to the receptor for advanced glycation end products. Allergy 2013; 68:1546.
  148. Teodorowicz M, Fiedorowicz E, Kostyra H, et al. Effect of Maillard reaction on biochemical properties of peanut 7S globulin (Ara h 1) and its interaction with a human colon cancer cell line (Caco-2). Eur J Nutr 2013; 52:1927.
  149. Mattison CP, Dinter J, Berberich MJ, et al. In vitro evaluation of digestive and endolysosomal enzymes to cleave CML-modified Ara h 1 peptides. Food Sci Nutr 2015; 3:273.
  150. MacLeod AR. Genetic origin of diversity of human cytoskeletal tropomyosins. Bioessays 1987; 6:208.
  151. Brown JH, Kim KH, Jun G, et al. Deciphering the design of the tropomyosin molecule. Proc Natl Acad Sci U S A 2001; 98:8496.
  152. 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.
  153. Usui M, Harada A, Ishimaru T, et al. Contribution of structural reversibility to the heat stability of the tropomyosin shrimp allergen. Biosci Biotechnol Biochem 2013; 77:948.
  154. Brett GM, Mills ENC, Goodfellow BJ, et al. Epitope mapping studies of broad specificity monoclonal antibodies to cereal prolamins. J Cereal Sci 1999; 29:117.