Ana o 1, a cashew (Anacardium occidental) allergen of the vicilin seed storage protein family

JOURNAL OF ALLERGY AND CLINICAL IMMUNOLOGY

卷:110

Article

Wang, F ; Robotham, JM ; Teuber, SS ; Tawde, P ; Sathe, SK ; Roux, KH

关键词: Ana o 1;    Anacardium occidental;    food allergy;    cashew allergy;    tree nut allergy;    vicilin;    7S globulin;    sucrose-binding protein;    seed storage proteins;    linear epitope;    epitope map;   

DOI  :  10.1067/mai.2002.125208

来源: Elsevier

【 摘 要 】

Background: The allergens responsible for cashew food allergy have not been well characterized. Objectives: We initiated a study to clone cDNAs encoding cashew food allergens. Methods: A cashew cDNA library was screened with human serum for IgE-reactive clones and rabbit IgG anti-cashew extract antisera. Reactive clones were sequenced and Expressed, and linear epitopes were identified by means of solid-phase overlapping peptide analysis. Immunoblot inhibition was used to identify the native peptide in cashew extract. Results: Four closely related clones reactive with both human and rabbit antisera were sequenced. Sequence analysis showed that these encode members of the vicilin/sucrose-binding protein family of plant seed storage proteins. Screening of the recombinant protein with sera from 20 patients with cashew allergy and 8 cashew-tolerant patients with allergies to other tree nuts showed that 50% and 25% of sera from patients with cashew allergy and cashew-tolerant subjects, respectively, bound the recombinant protein. The corresponding native allergen protein, designated Ana o 1, was located at approximately 50 kd. Epitope mapping revealed 11 linear IgE-binding epitopes, of which 3 appear to be immunodominant. None of the epitopes were shared in common with those of the peanut vicilin allergen Ara h 1. Conclusion: Ana o 1, a vicilin-like protein, is a major food allergen in cashews. Cashew and peanut vicilins do not share linear epitopes.

【 授权许可】

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