Heterogeneous responses and cross reactivity between the major peanut allergens ara h 1, 2,3 and 6 in a mouse model for peanut allergy

Clinical and Translational Allergy

Volumn 5, Issue 1, 2015, Pages

  Smit, Joost J ^a,b   Pennings, Maarten T ^b,c,e   Willemsen, Karina ^a   Van Roest, Manon ^a   Van Hoffen, Els ^c,d   Pieters, Raymond H ^a  

^a UTRECHT UNIVERSITY   (Netherlands)

^b Utrecht Centre for Food Allergy   (Netherlands)

^c UNIVERSITY MEDICAL CENTER UTRECHT   (Netherlands)

^d NIZO FOOD RESEARCH   (Netherlands)

^e UNIVERSITY OF APPLIED SCIENCES UTRECHT   (Netherlands)

Author keywords

Anaphylaxis; Cross reactivity; IgE; Mouse model; Peanut allergy; Peanut proteins; Sensitization; T cell

Indexed keywords

ARA H 1 PROTEIN; ARA H 2 PROTEIN; ARA H 3 PROTEIN; ARA H 6 PROTEIN; FOOD ALLERGEN; HISTAMINE; IMMUNOGLOBULIN E ANTIBODY; INTERLEUKIN 13; INTERLEUKIN 5; MONOCYTE CHEMOTACTIC PROTEIN 1; PEANUT EXTRACT; UNCLASSIFIED DRUG;

ALLERGIC REACTION; ANAPHYLAXIS; ANIMAL CELL; ANIMAL EXPERIMENT; ANIMAL MODEL; ANTIBODY RESPONSE; ARTICLE; CONTROLLED STUDY; CROSS REACTION; CYTOKINE PRODUCTION; CYTOKINE RESPONSE; DENDRITIC CELL; FEMALE; MAST CELL DEGRANULATION; MOUSE; MOUSE MODEL; NONHUMAN; PEANUT ALLERGY; PRIORITY JOURNAL; T LYMPHOCYTE;

EID: 84978023489     PISSN: None     EISSN: 20457022     Source Type: Journal    
DOI: 10.1186/s13601-015-0056-9     Document Type: Article

References (28)

1. Radauer C, Nandy A, Ferreira F, Goodman RE, Larsen JN, Lidholm J, et al. Update of the WHO/IUIS Allergen Nomenclature Database based on analysis of allergen sequences. Allergy. 2014;69:413-9.
2. Zhuang Y, Dreskin SC. Redefining the major peanut allergens. Immunol Res. 2013;55:125-34.
3. 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.
4. 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;34:583-90.
5. 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.
6. Radauer C, Bublin M, Wagner S, Mari A, Breiteneder H. Allergens are distributed into few protein families and possess a restricted number of biochemical functions. J Allergy Clin Immunol. 2008;121:847-52.e7.
7. Bublin M, Breiteneder H. Cross-reactivity of peanut allergens. Curr Allergy Asthma Rep. 2014;14:426.
8. Kulis M, Pons L, Burks AW. In vivo and T cell cross-reactivity between walnut, cashew and peanut. Int Arch Allergy Immunol. 2009;148:109-17.
9. Bublin M, Kostadinova M, Radauer C, Hafner C, Szépfalusi Z, Varga E-M, 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;132:118-24.
10. Li XM, Serebrisky D, Lee SY, Huang CK, Bardina L, Schofield BH, et al. A murine model of peanut anaphylaxis: T- And B-cell responses to a major peanut allergen mimic human responses. J Allergy Clin Immunol. 2000;106(1 Pt 1):150-8.
11. Smit JJ, Willemsen K, Hassing I, Fiechter D, Storm G, van Bloois L, et al. Contribution of classic and alternative effector pathways in peanut-induced anaphylactic responses. PLoS One. 2011;6:e28917.
12. Arias K, Chu DK, Flader K, Botelho F, Walker T, Arias N, et al. Distinct immune effector pathways contribute to the full expression of peanut-induced anaphylactic reactions in mice. J Allergy Clin Immunol. 2011;127:1552-61.e1.
13. Pochard P, Vickery B, Berin MC, Grishin A, Sampson HA, Caplan M, et al. Targeting Toll-like receptors on dendritic cells modifies the T(H)2 response to peanut allergens in vitro. J Allergy Clin Immunol. 2010;126:92-7.e5.
14. Van-Wijk F, Hartgring S, Koppelman SJ, Pieters R, Knippels LMJ. Mixed antibody and T cell responses to peanut and the peanut allergens Ara h 1, Ara h 2, Ara h 3 and Ara h 6 in an oral sensitization model. Clin Exp Allergy. 2004;34:1422-8.
15. Koppelman SJ, Knol EF, Vlooswijk RAA, Wensing M, Knulst AC, Hefle SL, et al. Peanut allergen Ara h 3: isolation from peanuts and biochemical characterization. Allergy. 2003;58:1144-51.
16. Mittag D, Akkerdaas J, Ballmer-Weber BK, Vogel L, Wensing M, Becker W-M, 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;114:1410-7.
17. Sun J, Arias K, Alvarez D, Fattouh R, Walker T, Goncharova S, et al. Impact of CD40 ligand, B cells, and mast cells in peanut-induced anaphylactic responses. J Immunol. 2007;179:6696-703.
18. Smit JJ, Bol-Schoenmakers M, Hassing I, Fiechter D, Boon L, Bleumink R, et al. The role of intestinal dendritic cells subsets in the establishment of food allergy. Clin Exp Allergy. 2011;41:890-8.
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 anaphylaxis and can effectively desensitize peanut-allergic mice. Clin Exp Allergy. 2012;42:326-36.
20. Flinterman AE, Pasmans SGMA, den-Hartog Jager CF, Hoekstra MO, Bruijnzeel-Koomen CAFM, Knol EF, et al. T cell responses to major peanut allergens in children with and without peanut allergy. Clin Exp Allergy. 2010;40:590-7.
21. Prickett SR, Voskamp AL, Dacumos-Hill A, Symons K, Rolland JM, O'Hehir RE. Ara h 2 peptides containing dominant CD4+ T-cell epitopes: candidates for a peanut allergy therapeutic. J Allergy Clin Immunol. 2011;127:608-15.e1-5.
22. Starkl P, Felix F, Krishnamurthy D, Stremnitzer C, Roth-Walter F, Prickett SR, et al. An unfolded variant of the major peanut allergen Ara h 2 with decreased anaphylactic potential. Clin Exp Allergy. 2012;42:1801-12.
23. Vissers YM, Blanc F, Skov PS, Johnson PE, Rigby NM, Przybylski-Nicaise L, et al. Effect of heating and glycation on the allergenicity of 2S albumins (Ara h 2/6) from peanut. PLoS One. 2011;6:e23998.
24. Koppelman SJ, Hefle SL, Taylor SL, de-Jong GAH. Digestion of peanut allergens Ara h 1, Ara h 2, Ara h 3, and Ara h 6: A comparative in vitro study and partial characterization of digestion-resistant peptides. Mol Nutr Food Res. 2010;54:1711-21.
25. 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.
26. 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.
27. Shreffler WG, Beyer K, Chu T-HT, Burks AW, Sampson HA. Microarray immunoassay: Association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. J Allergy Clin Immunol. 2004;113:776-82.
28. Lewis SA, Grimshaw KEC, Warner JO, Hourihane JO. The promiscuity of immunoglobulin E binding to peanut allergens, as determined by Western blotting, correlates with the severity of clinical symptoms. Clin Exp Allergy. 2005;35:767-73.