IgE cross-reactivity between the major peanut allergen Ara h 2 and the nonhomologous allergens Ara h 1 and Ara h 3

Journal of Allergy and Clinical Immunology

Volumn 132, Issue 1, 2013, Pages

  Bublin, Merima ^a   Kostadinova, Maria ^a   Radauer, Christian ^a   Hafner, Christine ^b   Szépfalusi, Zsolt ^c   Varga, Eva Maria ^d   Maleki, Soheila J ^a   Hoffmann Sommergruber, Karin ^e   Breiteneder, Heimo ^a  

^a MEDICAL UNIVERSITY OF VIENNA   (Austria)

^b Karl Landsteiner Institute for Dermatological Research   (Austria)

^c UNIV KLIN KINDER JUGENDHEILKUNDE   (Austria)

^d MEDICAL UNIVERSITY OF GRAZ   (Austria)

^e SOUTHERN REGIONAL RESEARCH CENTER   (United States)

Author keywords

Allergens; Food allergy; IgE cross reactivity; Peanut allergy

Indexed keywords

ALBUMIN; ARA H 1; ARA H 2; ARA H 3; FOOD ALLERGEN; IMMUNOGLOBULIN E; UNCLASSIFIED DRUG;

ALLERGENICITY; ANTIGEN BINDING; ARTICLE; CLINICAL ARTICLE; COMPUTER MODEL; CROSS REACTION; DISEASE SEVERITY; ENZYME LINKED IMMUNOSORBENT ASSAY; HUMAN; PEANUT; PRIORITY JOURNAL; PROTEIN ANALYSIS; SEQUENCE HOMOLOGY;

EID: 84882862050     PISSN: 00916749     EISSN: 10976825     Source Type: Journal    
DOI: 10.1016/j.jaci.2013.01.022     Document Type: Article

References (45)

1. Bock SA, Munoz-Furlong A, Sampson HA. Further fatalities caused by anaphylac-tic reactions to food, 2001-2006. J Allergy Clin Immunol 2007;119:1016-8.
2. Skolnick HS, Conover-Walker MK, Koerner CB, Sampson HA, Burks W, Wood RA. The natural history of peanut allergy. J Allergy Clin Immunol 2001;107: 367-74.
3. Sicherer SH, Sampson HA. Peanut allergy: emerging concepts and approaches for an apparent epidemic. J Allergy Clin Immunol 2007;120:491-503.
4. Lewis SA, Grimshaw KE, Warner JO, Hourihane JO. The promiscuity of immuno-globulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms. Clin Exp Allergy 2005;35:767-73.
5. Vereda A, van Hage M, Ahlstedt S, Ibanez MD, Cuesta-Herranz J, van Odijk J, et al. Peanut allergy: clinical and immunologic differences among patients from 3 different geographic regions. J Allergy Clin Immunol 2011;127:603-7.
6. Nicolaou N, Murray C, Belgrave D, Poorafshar M, Simpson A, Custovic A. Quantification of specific IgE to whole peanut extract and peanut components in prediction of peanut allergy. J Allergy Clin Immunol 2011;127:684-5.
7. Nicolaou N, Poorafshar M, Murray C, Simpson A, Winell H, Kerry G, et al. Allergy or tolerance in children sensitized to peanut: prevalence and differentiation using component-resolved diagnostics. J Allergy Clin Immunol 2010;125:191-7.
8. Lin J, Bruni FM, Fu Z, Maloney J, Bardina L, Boner AL, et al. A bioinformatics approach to identify patients with symptomatic peanut allergy using peptide micro-array immunoassay. J Allergy Clin Immunol 2012;129:1321-8.
9. Palmer GW, Dibbern DA Jr, 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;115:302-12.
10. 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 immunoglob-ulin E Western blotting, basophil-histamine release and intracutaneous testing: Ara h2 is the most important peanut allergen. Clin Exp Allergy 2004;34:583-90.
11. Porterfield HS, Murray KS, Schlichting DG, Chen X, Hansen KC, Duncan MW, et al. Effector activity of peanut allergens: a critical role for Ara h 2, Ara h 6, and their variants. Clin Exp Allergy 2009;39:1099-108.
12. Blanc F, Adel-Patient K, Drumare MF, Paty E, Wal JM, Bernard H. Capacity of purified peanut allergens to induce degranulation in a functional in vitro assay: Ara h 2 and Ara h 6 are the most efficient elicitors. Clin Exp Allergy 2009;39: 1277-85.
13. Shreffler WG, Beyer K, Chu TH, Burks AW, Sampson HA. Microarray immuno-assay: association of clinical history, in vitro IgE function, and heterogeneity of al-lergenic peanut epitopes. J Allergy Clin Immunol 2004;113:776-82.
14. 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;118:250-6.
15. Flinterman AE, Knol EF, Lencer DA, Bardina L, den Hartog Jager CF, 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;121:737-43.
16. Peeters KA, Koppelman SJ, van Hoffen E, van der Tas CW, den Hartog Jager CF, Penninks AH, et al. Does skin prick test reactivity to purified allergens correlate with clinical severity of peanut allergy? Clin Exp Allergy 2007;37:108-15.
17. Asarnoj A, Moverare R, Ostblom E, Poorafshar M, Lilja G, Hedlin G, et al. IgE to peanut allergen components: relation to peanut symptoms and pollen sensitization in 8-year-olds. Allergy 2010;65:1189-95.
18. Krause S, Latendorf T, Schmidt H, Darcan-Nicolaisen Y, Reese G, Petersen A, et al. Peanut varieties with reduced Ara h 1 content indicating no reduced allerge-nicity. Mol Nutr Food Res 2010;54:381-7.
19. Kulis M, Chen X, Lew J, Wang Q, Patel OP, Zhuang Y, et al. The 2S albumin allergens of Arachis hypogaea, Ara h 2 and Ara h 6, are the major elicitors of ana-phylaxis and can effectively desensitize peanut-allergic mice. Clin Exp Allergy 2012;42:326-36.
20. Marsh J, Rigby N, Wellner K, Reese G, Knulst A, Akkerdaas J, et al. Purification and characterisation of a panel of peanut allergens suitable for use in allergy diagnosis. Mol Nutr Food Res 2008;52(suppl 2):S272-85.
21. Sen M, Kopper R, Pons L, Abraham EC, Burks AW, Bannon GA. Protein structure plays a critical role in peanut allergen stability and may determine immunodomi-nant IgE-binding epitopes. J Immunol 2002;169:882-7.
22. Koppelman SJ, de Jong GA, Laaper-Ertmann M, Peeters KA, Knulst AC, Hefle SL, et al. Purification and immunoglobulin E-binding properties of peanut allergen Ara h 6: evidence for cross-reactivity with Ara h 2. Clin Exp Allergy 2005;35:490-7.
23. Aalberse RC. Structural biology of allergens. J Allergy Clin Immunol 2000;106: 228-38.
24. Ferreira F, Hawranek T, Gruber P, Wopfner N, Mari A. Allergic cross-reactivity: from gene to the clinic. Allergy 2004;59:243-67.
25. Breiteneder H, Radauer C. A classification of plant food allergens. J Allergy Clin Immunol 2004;113:821-30.
26. 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.
27. 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;66:1522-9.
28. Flinterman AE, van Hoffen E, den Hartog Jager CF, Koppelman S, Pasmans SG, Hoekstra MO, et al. Children with peanut allergy recognize predominantly Ara h2 and Ara h6, which remains stable over time. Clin Exp Allergy 2007;37: 1221-8.
29. Burks AW, Shin D, Cockrell G, Stanley JS, Helm RM, Bannon GA. Mapping and mutational analysis of the IgE-binding epitopes on Ara h 1, a legume vicilin protein and a major allergen in peanut hypersensitivity. Eur J Biochem 1997;245:334-9.
30. 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;342:244-53.
31. King N, Helm R, Stanley JS, Vieths S, Luttkopf D, Hatahet L, et al. Allergenic characteristics of a modified peanut allergen. Mol Nutr Food Res 2005;49:963-71.
32. Rabjohn P, Helm EM, Stanley JS, West CM, Sampson HA, Burks AW, et al. Molecular cloning and epitope analysis of the peanut allergen Ara h 3. J Clin Invest 1999;103:535-42.
33. Shin DS, Compadre CM, Maleki SJ, Kopper RA, Sampson H, Huang SK, 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.
34. 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;53:8752-9.
35. Aalberse RC, Crameri R. IgE-binding epitopes: a reappraisal. Allergy 2011;66: 1261-74.
36. Albrecht M, Kuhne Y, Ballmer-Weber BK, Becker WM, Holzhauser T, Lauer I, et al. Relevance of IgE binding to short peptides for the allergenic activity of food allergens. J Allergy Clin Immunol 2009;124:328-36.
37. Jin T, Guo F, Chen YW, Howard A, Zhang YZ. Crystal structure of Ara h 3, a major allergen in peanut. Mol Immunol 2009;46:1796-804.
38. Rouge P, Culerrier R, Sabatier V, Granier C, Rance F, Barre A. Mapping and con-formational analysis of IgE-binding epitopic regions on the molecular surface of the major Ara h 3 legumin allergen of peanut (Arachis hypogaea). Mol Immunol 2009;46:1067-75.
39. Chatchatee P, Jarvinen KM, Bardina L, Vila L, Beyer K, Sampson HA. Identification of IgE and IgG binding epitopes on beta-and kappa-casein in cow's milk allergic patients. Clin Exp Allergy 2001;31:1256-62.
40. Jarvinen KM, Beyer K, Vila L, Chatchatee P, Busse PJ, Sampson HA. B-cell epi-topes as a screening instrument for persistent cow's milk allergy. J Allergy Clin Immunol 2002;110:293-7.
41. 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;49: 115-23.
42. Jin T, Guo F, Chen YW, Howard A, Zhang YZ. Crystal structure of Ara h 3, a major allergen in peanut. Mol Immunol 2009;46:1796-804.
43. 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;395:463-72.
44. Eswar N, Eramian D, Webb B, Shen MY, Sali A. Protein structure modeling with MODELLER. Methods Mol Biol 2008;426:145-59.
45. Pettersen EF, Goddard TD, Huang CC, Couch GS, Greenblatt DM, Meng EC, et al. UCSF Chimera-a visualization system for exploratory research and analysis. J Comput Chem 2004;25:1605-12.