The molecular basis of peanut allergy topical collection on allergens

Current Allergy and Asthma Reports

Volumn 14, Issue 5, 2014, Pages

  Mueller, Geoffrey A ^a   Maleki, Soheila J ^b   Pedersen, Lars C ^a  

^a NATIONAL INSTITUTE OF ENVIRONMENTAL HEALTH SCIENCES   (United States)

^b SOUTHERN REGIONAL RESEARCH CENTER   (United States)

Author keywords

Cross reactivity; Major allergens; Minor allergens; Molecular basis; Molecular modifications; Peanut allergens; Peanut allergy; Protein structures

Indexed keywords

EPITOPE; FOOD ALLERGEN; IMMUNOGLOBULIN E; ALLERGEN; VEGETABLE PROTEIN;

AMINO ACID SEQUENCE; ANTIGEN RECOGNITION; ARTICLE; CROSS REACTION; DIGESTION; HUMAN; IMMUNE RESPONSE; INNATE IMMUNITY; NONHUMAN; PEANUT ALLERGY; ANIMAL; CHEMISTRY; IMMUNOLOGY; PEANUT;

ALLERGENS; ANIMALS; ARACHIS HYPOGAEA; CROSS REACTIONS; HUMANS; IMMUNOGLOBULIN E; PEANUT HYPERSENSITIVITY; PLANT PROTEINS;

EID: 84898774862     PISSN: 15297322     EISSN: 15346315     Source Type: Journal    
DOI: 10.1007/s11882-014-0429-5     Document Type: Article

References (81)

1. Liu AH, Jaramillo R, Sicherer SH, Wood RA, Bock SA, Burks AW, et al. National prevalence and risk factors for food allergy and relationship to asthma: results from the National Health and Nutrition Examination Survey 2005-2006. J Allergy Clin Immunol. 2010;126(4):798 e13-806 e13.
2. Aalberse RC, Crameri R. IgE-binding epitopes: a reappraisal. Allergy. 2011 Oct;66(10):1261-74. Thought-provoking summary of IgE antibodies.
3. Dall'antonia F, Pavkov-Keller T, Zangger K, Keller W. Structure of allergens and structure based epitope predictions. Methods. 2013 Jul 23. Excellent review of the structural biology of allergens and in particular the mapping the IgE epitopes.
4. Pomes A, Relevant B. Cell epitopes in allergic disease. Int Arch Allergy Immunol. 2010;152(1):1-11.
5. Radauer C, Breiteneder H. Evolutionary biology of plant food allergens. J Allergy Clin Immunol. 2007;120(3):518-25.
6. Breiteneder H, Radauer C. A classification of plant food allergens. J Allergy Clin Immunol. 2004;113(5):821-30.
7. Chruszcz M, Maleki SJ, Majorek KA, Demas M, Bublin M, Solberg R, et al. Structural and immunologic characterization of Ara h 1, a major peanut allergen. J Biol Chem. 2011 Nov 11;286(45):39318-27. First structures of Ara h 1 and Ara h 3.
8. Cabanos C, Urabe H, Tandang-Silvas MR, Utsumi S, Mikami B, Maruyama N. Crystal structure of the major peanut allergen Ara h 1. Mol Immunol. 2011 Oct-Nov;49(1-2):115-23. First structures of Ara h 1 and Ara h 3.
9. Mueller GA, Gosavi RA, Pomes A, Wunschmann S, Moon AF, London RE, et al. Ara h 2: crystal structure and IgE binding distinguish two subpopulations of peanut allergic patients by epitope diversity. Allergy. 2011;66(7):878-85.
10. Lehmann K, Schweimer K, Reese G, Randow S, Suhr M, Becker WM, et al. Structure and stability of 2S albumin-type peanut allergens: implications for the severity of peanut allergic reactions. Biochem J. 2006;395(3):463-72.
11. Wang Y, Fu TJ, Howard A, Kothary MH, McHugh TH, Zhang YZ. Crystal structure of peanut (Arachis hypogaea) Allergen Ara h 5. J Agric Food Chem. 2013;61(7):1573-8.
12. Hurlburt BK, Offermann LR, McBride JK, Majorek KA, Maleki SJ, Chruszcz M. Structure and function of the peanut panallergen Ara h 8. J Biol Chem. 2013 Nov 19.
13. Jin T, Guo F, Chen YW, Howard A, Zhang YZ. Crystal structure of Ara h 3, a major allergen in peanut. Mol Immunol. 2009;46(8-9):1796-804.
14. Dunwell JM. Cupins: a new superfamily of functionally diverse proteins that include germins and plant storage proteins. Biotechnol Genet Eng. 1998;15:1-32.
15. Dunwell JM, Purvis A, Khuri S. Cupins: the most functionally diverse protein superfamily? Phytochemistry. 2004;65(1):7-17.
16. Van Boxtel EL, Van Beers MMC, Koppelman SJ, Van den Broek LAM, Gruppen H. Allergen Ara h 1 occurs in peanuts as a large oligomer rather than as a trimer. J Agric Food Chem. 2006;54(19):7180-6.
17. 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(4):763-8.
18. Dodo HW, Viquez OM, Maleki SJ, Konan KN. cDNA clone of a putative peanut (Arachis hypogaea L.) trypsin inhibitor has homology with peanut allergens Ara h 3 and Ara h 4. J Agr. Food Chem. 2004;52(5):1404-9.
19. Guo B, Liang X, Chung SY, Maleki SJ. Proteomic screening points to the potential importance of Ara h 3 basic subunit in allergenicity of peanut. Inflamm Allergy Drug Targets. 2008;7(3):163-6.
20. Guo BZ, Liang XQ, Chung SY, Holbrook CC, Maleki SJ. Proteomic analysis of peanut seed storage proteins and genetic variation in a potential peanut allergen. Protein Pept Lett. 2008;15(6):567-77.
21. Breiteneder H, Mills ENC. Plant food allergens - structural and functional aspects of allergenicity. Biotechnol Adv. 2005;23(6):395-9.
22. Holm L, Kaariainen S, Rosenstrom P, Schenkel A. Searching protein structure databases with DaliLite v. 3. Bioinformatics. 2008;24(23):2780-1.
23. Maleki SJ, Viquez O, Jacks T, Dodo H, Champagne ET, Chung SY, et al. The major peanut allergen, Ara h 2, functions as a trypsin inhibitor, and roasting enhances this function. J Allergy Clin Immunol. 2003;112(1):190-5.
24. Koppelman SJ, Wensing M, Ertmann M, Knulst AC, Knol EF. Relevance of Ara h1, Ara h2 and Ara h3 in peanut-allergic patients, as determined by immunoglobulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen. Clin Exp Allergy. 2004;34(4):583-90.
25. Palmer GW, Dibbern DA, Burks AW, Bannon GA, Bock SA, Porterfield HS, et al. Comparative potency of Ara h 1 and Ara h 2 in immunochemical and functional assays of allergenicity. Clin Immunol. 2005;115(3):302-12.
26. Stanley JS, King N, Burks AW, Huang SK, Sampson H, Cockrell G, 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(2):244-53.
27. Chen XN, Wang Q, El-Mezayen R, Zhuang YH, Dreskin SC. Ara h 2 and Ara h 6 have similar allergenic activity and are substantially redundant. Int Arch Allergy Immunol. 2013;160(3):251-8.
28. Koid AE, Chapman MD, Hamilton RG, Van Ree R, Versteeg SA, Dreskin SC, et al. Ara h 6 complements Ara h 2 as an important marker for IgE reactivity to peanut. J Agric Food Chem. 2013 Dec 11.
29. Birbach A. Profilin, a multi-modal regulator of neuronal plasticity. Bioessays. 2008;30(10):994-1002.
30. Ramachandran S, Christensen HEM, Ishimaru Y, Dong CH, Chao-Ming W, Cleary AL, et al. Profilin plays a role in cell elongation, cell shape maintenance, and flowering in arabidopsis. Plant Physiol. 2000;124(4):1637-47.
31. Hauser M, Roulias A, Ferreira F, Egger M. Panallergens and their impact on the allergic patient. Allergy Asthma Clin Immunol. 2010;6(1):1.
32. Fernandes H, Michalska K, Sikorski M, Jaskolski M. Structural and functional aspects of PR-10 proteins. FEBS J. 2013;280(5):1169-99.
33. Kofler S, Asam C, Eckhard U, Wallner M, Ferreira F, Brandstetter H. Crystallographically mapped ligand binding differs in high and low IgE binding isoforms of birch pollen Allergen Bet v 1. J Mol Biol. 2012;422(1):109-23.
34. Flicker S, Steinberger P, Norderhaug L, Sperr WR, Majlesi Y, Valent P, et al. Conversion of grass pollen allergen-specific human IgE into a protective IgG(1) antibody. Eur J Immunol. 2002;32(8):2156-62.
35. Sicherer SH, Wood RA, Immunology SA. Allergy testing in childhood: using allergen-specific IgE tests. Pediatrics. 2012;129(1):193-7.
36. Gupta RS, Dyer AA, Jain N, Greenhawt MJ. Childhood food allergies: current diagnosis, treatment, and management strategies. Mayo Clin Proc. 2013;88(5):512-26.
37. 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(1):141-7.
38. Bublin M, Kostadinova M, Radauer C, Hafner C, Szepfalusi Z, Varga EM, et al. IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3. J Allergy Clin Immunol. 2013 Jul;132(1):118-U212. This represents a new paradigm in the cross-reactivity of peanut allergens. It will be interesting to see if this generalizes to other allergen groups besides nuts and legumes.
39. Maleki SJ, Teuber SS, Cheng H, Chen D, Comstock SS, Ruan S, et al. Computationally predicted IgE epitopes of walnut allergens contribute to cross-reactivity with peanuts. Allergy. 2011;66(12):1522-9.
40. Schein CH, Ivanciuc O, Braun W. Common physical-chemical properties correlate with similar structure of the IgE epitopes of peanut allergens. J Agric Food Chem. 2005;53(22):8752-9.
41. Astier C, Morisset M, Roitel O, Codreanu F, Jacquenet S, Franck P, et al. Predictive value of skin prick tests using recombinant allergens for diagnosis of peanut allergy. J Allergy Clin Immunol. 2006;118(1):250-6.
42. Flinterman AE, Knol EF, Lencer DA, Bardina L, Jager CFDH, Lin J, et al. Peanut epitopes for IgE and IgG4 in peanut-sensitized children in relation to severity of peanut allergy. J Allergy Clin Immunol. 2008;121(3):737-43.
43. Peeters KABM, Koppelman SJ, van Hoffen E, van der Tas CWH, Jager CFD, Penninks AH, et al. Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy? Clin Exp Allergy. 2007;37(1):108-15.
44. Altmann F. The role of protein glycosylation in allergy. Int Arch Allergy Immunol. 2007;142(2):99-115.
45. Aalberse RC, Koshte V, Clemens JGJ. Immunoglobulin-E antibodies that crossreact with vegetable foods, pollen, and hymenoptera venom. J Allergy Clin Immunol. 1981;68(5):356-64.
46. Malandain H. IgE-reactive carbohydrate epitopes-classification, cross-reactivity, and clinical impact. Eur Ann Allergy Clin Immunol. 2005;37(4):122-8.
47. van Ree R, Cabanes-Macheteau M, Akkerdaas J, Milazzo JP, Loutelier-Bourhis C, Rayon C, 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(15):11451-8.
48. van der Veen MJ, van Ree R, Aalberse RC, Akkerdaas J, Koopelman SJ, Jansen HM, et al. Poor biologic activity of cross-reactive IgE directed to carbohydrate determinants of glycoproteins. J Allergy Clin Immunol. 1997;100(3):327-34.
49. Kochuyt AM, Van Hoeyveld EM, Stevens EAM. Prevalence and clinical relevance of specific immunoglobulin E to pollen caused by sting-induced specific immunoglobulin E to cross-reacting carbohydrate determinants in Hymenoptera venoms. Clin Exp Allergy. 2005;35(4):441-7.
50. Dell A, Haslam SM, Morris HR, Khoo KH. Immunogenic glycoconjugates implicated in parasitic nematode diseases. Biochim Biophys Acta (BBA) - Mol Basis Dis. 1999;1455(2-3):353-62.
51. van Die I, Gomord V, Kooyman FNJ, van den Berg TK, Cummings RD, Vervelde L. Core alpha 1 -> 3-fucose is a common modification of N-glycans in parasitic helminths and constitutes an important epitope for IgE from Haemonchus contortus infected sheep. FEBS Lett. 1999;463(1-2):189-93.
52. Shreffler WG, Castro RR, Kucuk ZY, Charlop-Powers Z, Grishina G, Yoo S, et al. The major glycoprotein allergen from Arachis hypogaea, Ara h 1, is a ligand of dendritic cell-specific ICAM-grabbing nonintegrin and acts as a Th2 adjuvant in vitro. J Immunol. 2006;177(6):3677-85.
53. Royer PJ, Emara M, Yang CX, Al-Ghouleh A, Tighe P, Jones N, et al. The mannose receptor mediates the uptake of diverse native allergens by dendritic cells and determines allergen-induced T cell polarization through modulation of IDO activity. J Immunol. 2010;185(3):1522-31.
54. Wills-Karp M. Allergen-specific pattern recognition receptor pathways. Curr Opin Immunol. 2010;22(6):777-82.
55. Hodge JE. The Amadori rearrangement. Adv Carbohydr Chem. 1955;10:169-205.
56. Rabbani N, Thornalley PJ. Glycation research in amino acids: a place to call home. Amino Acids. 2012;42(4):1087-96.
57. Uribarri J, Woodruff S, Goodman S, Cai WJ, Chen X, Pyzik R, et al. Advanced glycation end products in foods and a practical guide to their reduction in the diet. J Am Diet Assoc. 2010;110(6):911-6.
58. Chung SY, Champagne ET. Association of end-product adducts with increased IgE binding of roasted peanuts. J Agric Food Chem. 2001;49(8):3911-6.
59. Mueller GA, Maleki SJ, Johnson K, Hurlburt BK, Cheng H, Ruan S, et al. Indentification of Maillard reaction products on panut allergens that influence binding to the receptor for advanced glycation end products. Allergy. 2013.
60. Chassaigne H, Norgaard JV, van Hengel AJ. Proteomics-based approach to detect and identify major allergens in processed peanuts by capillary LC-Q-TOF (MS/MS). J Agric Food Chem. 2007;55(11):4461-73.
61. 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. 2012 Oct 16.
62. Petersen A, Rennert S, Kull S, Becker WM, Notbohm H, Goldmann T, et al. Roasting and lipid binding provide allergenic and proteolytic stability to the peanut Allergen Ara H 8. Biol Chem. 2013 Sep 21.
63. Schmitt DA, Nesbit JB, Hurlburt BK, Cheng HP, Maleki SJ. Processing can alter the properties of peanut extract preparations. J Agric Food Chem. 2010;58(2):1138-43.
64. Ilchmann A, Burgdorf S, Scheurer S, Waibler Z, Nagai R, Wellner A, 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(1):175 e1-11-83 e1-11.
65. Buttari B, Profumo E, Capozzi A, Facchiano F, Saso L, Sorice M, et al. Advanced glycation end products of human beta(2) glycoprotein I modulate the maturation and function of DCs. Blood. 2011;117(23):6152-61.
66. Hilmenyuk T, Bellinghausen I, Heydenreich B, Ilchmann A, Toda M, Grabbe S, et al. Effects of glycation of the model food allergen ovalbumin on antigen uptake and presentation by human dendritic cells. Immunology. 2010;129(3):437-45.
67. Zill H, Gunther R, Erbersdobler HF, Folsch UR, Faist V. RAGE expression and AGE-induced MAP kinase activation in Caco-2 cells. Biochem Biophys Res Commun. 2001;288(5):1108-11.
68. Teodorowicz M, Fiedorowicz E, Kostyra H, Wichers H, Kostyra E. 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 Jan 20.
69. Milutinovic PS, Alcorn JF, Englert JM, Crum LT, Oury TD. The receptor for advanced glycation end products is a central mediator of asthma pathogenesis. Am J Pathol. 2012;181(4):1215-25.
70. Sukkar MB, Wood LG, Tooze M, Simpson JL, McDonald VM, Gibson PG, et al. Soluble RAGE is deficient in neutrophilic asthma and COPD. Eur Respir J. 2012;39(3):721-9.
71. Cheng CM, Tsuneyama K, Kominami R, Shinohara H, Sakurai S, Yonekura H, et al. Expression profiling of endogenous secretory receptor for advanced glycation end products in human organs. Mod Pathol. 2005;18(10):1385-96.
72. Chuah YK, Basir R, Talib H, Tie TH, Nordin N. Receptor for advanced glycation end products and its involvement in inflammatory diseases. Int J Inflamm. 2013;2013:403460.
73. Hudson BI, Carter AM, Harja E, Kalea AZ, Arriero M, Yang HJ, et al. Identification, classification, and expression of RAGE gene splice variants. FASEB J. 2008;22(5):1572-80.
74. Mondoulet L, Dioszeghy V, Puteaux E, Ligouis M, Dhelft V, Letourneur F, et al. Intact skin and not stripped skin is crucial for the safety and efficacy of peanut epicutaneous immunotherapy (EPIT) in mice. Clin Transl Allergy. 2012;2(1):22.
75. Beyer KB, Morrow E, Li XM, Bardina L, Bannon GA, Burks AW, et al. Effects of cooking methods on peanut allergenicity. J Allergy Clin Immunol. 2001;107(6):1077-81.
76. Maleki SJ, Casillas AM, Kaza U, Wilson BA, Nesbit JB, Reimoneqnue C, et al. Differences among heat-treated, raw, and commercial peanut extracts by skin testing and immunoblotting. Ann Allergy Asthma Immunol. 2010;105(6):451-7.
77. Pomes A, Butts CL, Chapman MD. Quantification of Ara h 1 in peanuts: why roasting makes a difference. Clin Exp Allergy. 2006;36(6):824-30.
78. Mondoulet L, Paty E, Drumare MF, Ah-Leung S, Scheinmann P, Willemot RM, et al. Influence of thermal processing on the allergenicity of peanut proteins. J Agric Food Chem. 2005;53(11):4547-53.
79. Uribarri J, Cai W, Peppa M, Goodman S, Ferrucci L, Striker G, et al. Circulating glycotoxins and dietary advanced glycation endproducts: two links to inflammatory response, oxidative stress, and aging. J Gerontol A Biol. 2007;62(4):427-33.
80. Kellow NJ, Savige GS. Dietary advanced glycation end-product restriction for the attenuation of insulin resistance, oxidative stress and endothelial dysfunction: a systematic review. Eur J Clin Nutr. 2013;67(3):239-48.
81. Nesbit JB, Hurlburt BK, Schein CH, Cheng HP, Wei H, Maleki SJ. Ara h 1 structure is retained after roasting and is important for enhanced binding to IgE. Mol Nutr Food Res. 2012;56(11):1739-47.