Cross-reactivity of Peanut Allergens

Overview

Journal Curr Allergy Asthma Rep

Specialties Allergy & Immunology
Pulmonary Medicine

Date 2014 Feb 21

PMID 24554241

Citations 26

Authors

Merima Bublin

Heimo Breiteneder

Affiliations

Soon will be listed here.

Abstract

Peanut seeds are currently widely used as source of human food ingredients in the United States of America and in European countries due to their high quality protein and oil content. This article describes the classification and molecular biology of peanut seed allergens with particular reference to their cross-reactivities. Currently, the IUIS allergen nomenclature subcommittee accepts 12 peanut allergens. Two allergens belong to the cupin and four to the prolamin superfamily, and six are distributed among profilins, Bet v 1-like proteins, oleosins, and defensins. Clinical observations frequently report an association of peanut allergy with allergies to legumes, tree nuts, seeds, fruits and pollen. Molecular cross-reactivity has been described between members of the Bet v 1-like proteins, the non-specific lipid transfer proteins, and the profilins. This review also addresses the less well-studied cross-reactivity between cupin and prolamin allergens of peanuts and of other plant food sources and the recently discovered cross-reactivity between peanut allergens of unrelated protein families.

Citing Articles

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References

Kulis M, Chen X, Lew J, Wang Q, Patel O, Zhuang Y . 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(2):326-36. PMC: 3270336. DOI: 10.1111/j.1365-2222.2011.03934.x. View

Sako Y, Nomura N, Uchida A, Ishida Y, Morii H, Koga Y . Aeropyrum pernix gen. nov., sp. nov., a novel aerobic hyperthermophilic archaeon growing at temperatures up to 100 degrees C. Int J Syst Bacteriol. 1996; 46(4):1070-7. DOI: 10.1099/00207713-46-4-1070. View

Shreffler W, Beyer K, Chu T, Burks A, Sampson H . Microarray immunoassay: association of clinical history, in vitro IgE function, and heterogeneity of allergenic peanut epitopes. J Allergy Clin Immunol. 2004; 113(4):776-82. DOI: 10.1016/j.jaci.2003.12.588. View

Schmidt H, Krause S, Gelhaus C, Petersen A, Janssen O, Becker W . Detection and structural characterization of natural Ara h 7, the third peanut allergen of the 2S albumin family. J Proteome Res. 2010; 9(7):3701-9. DOI: 10.1021/pr1002406. View

Crameri R, Scheurer S, Vieths S, Becker W . Patient-tailored cloning of allergens by phage display: peanut (Arachis hypogaea) profilin, a food allergen derived from a rare mRNA. J Chromatogr B Biomed Sci Appl. 2001; 756(1-2):295-305. DOI: 10.1016/s0378-4347(01)00088-3. View

Kulis M, Pons L, Burks A . In vivo and T cell cross-reactivity between walnut, cashew and peanut. Int Arch Allergy Immunol. 2008; 148(2):109-17. PMC: 7065401. DOI: 10.1159/000155741. View

Stotz H, Thomson J, Wang Y . Plant defensins: defense, development and application. Plant Signal Behav. 2009; 4(11):1010-2. PMC: 2819505. DOI: 10.4161/psb.4.11.9755. View

Asarnoj A, Moverare R, Ostblom E, Poorafshar M, Lilja G, Hedlin G . IgE to peanut allergen components: relation to peanut symptoms and pollen sensitization in 8-year-olds. Allergy. 2010; 65(9):1189-95. DOI: 10.1111/j.1398-9995.2010.02334.x. View

Dunwell J, Khuri S, Gane P . Microbial relatives of the seed storage proteins of higher plants: conservation of structure and diversification of function during evolution of the cupin superfamily. Microbiol Mol Biol Rev. 2000; 64(1):153-79. PMC: 98990. DOI: 10.1128/MMBR.64.1.153-179.2000. View

10.

Mittag D, Akkerdaas J, Ballmer-Weber B, Vogel L, Wensing M, Becker W . 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(6):1410-7. DOI: 10.1016/j.jaci.2004.09.014. View

11.

Barre A, Sordet C, Culerrier R, Rance F, Didier A, Rouge P . Vicilin allergens of peanut and tree nuts (walnut, hazelnut and cashew nut) share structurally related IgE-binding epitopes. Mol Immunol. 2007; 45(5):1231-40. DOI: 10.1016/j.molimm.2007.09.014. View

12.

Akkerdaas J, Schocker F, Vieths S, Versteeg S, Zuidmeer L, Hefle S . Cloning of oleosin, a putative new hazelnut allergen, using a hazelnut cDNA library. Mol Nutr Food Res. 2005; 50(1):18-23. DOI: 10.1002/mnfr.200500147. View

13.

Petersen A, Rennert S, Kull S, Becker W, Notbohm H, Goldmann T . Roasting and lipid binding provide allergenic and proteolytic stability to the peanut allergen Ara h 8. Biol Chem. 2013; 395(2):239-50. DOI: 10.1515/hsz-2013-0206. View

14.

Sicherer S, Munoz-Furlong A, Sampson H . Prevalence of peanut and tree nut allergy in the United States determined by means of a random digit dial telephone survey: a 5-year follow-up study. J Allergy Clin Immunol. 2003; 112(6):1203-7. DOI: 10.1016/s0091-6749(03)02026-8. View

15.

Flinterman A, Knol E, Lencer D, Bardina L, den Hartog Jager C, Lin J . Peanut epitopes for IgE and IgG4 in peanut-sensitized children in relation to severity of peanut allergy. J Allergy Clin Immunol. 2008; 121(3):737-743.e10. DOI: 10.1016/j.jaci.2007.11.039. View

16.

Kroghsbo S, Bogh K, Rigby N, Mills E, Rogers A, Madsen C . Sensitization with 7S globulins from peanut, hazelnut, soy or pea induces IgE with different biological activities which are modified by soy tolerance. Int Arch Allergy Immunol. 2011; 155(3):212-24. DOI: 10.1159/000321200. View

17.

Adachi M, Takenaka Y, Gidamis A, Mikami B, Utsumi S . Crystal structure of soybean proglycinin A1aB1b homotrimer. J Mol Biol. 2000; 305(2):291-305. DOI: 10.1006/jmbi.2000.4310. View

18.

Jensen L, Pedersen M, Skov P, Poulsen L, Bindslev-Jensen C, Andersen S . Peanut cross-reacting allergens in seeds and sprouts of a range of legumes. Clin Exp Allergy. 2008; 38(12):1969-77. DOI: 10.1111/j.1365-2222.2008.03129.x. View

19.

Barre A, Jacquet G, Sordet C, Culerrier R, Rouge P . Homology modelling and conformational analysis of IgE-binding epitopes of Ara h 3 and other legumin allergens with a cupin fold from tree nuts. Mol Immunol. 2007; 44(12):3243-55. DOI: 10.1016/j.molimm.2007.01.023. View

20.

Glaspole I, de Leon M, Prickett S, OHehir R, Rolland J . Clinical allergy to hazelnut and peanut: identification of T cell cross-reactive allergens. Int Arch Allergy Immunol. 2011; 155(4):345-54. DOI: 10.1159/000321268. View