U.S. Department of Agriculture: Agricultural Research Service, Lincoln, Nebraska

 

Date of this Version

2015

Citation

Columbia International Publishing, Journal of Contemporary Immunology (2015) Vol. 2 No. 1 pp. 1-26

Comments

U.S. Government Work

Abstract

Peanuts are a cause of one of the most common food allergies. Allergy to peanuts not only affects a significant fraction of the population, but it is relatively often associated with strong reactions in sensitized individuals. Peanut and tree nut allergies, which start in childhood are often persistent and continue through life, as opposed to other food allergies that resolve with age. Cherefore, peanut allergens are one of the most intensively studied food allergens. In this review we focus on the structural studies of peanut allergens. Despite the fact that these allergens are attracting a lot of interest and several of them have had their structures experimentally determined, still some molecular properties of peanut allergens are not well understood. Peanut allergens like other allergens belong to just a few protein families. Allergens from the cupin superfamily (Ara h 1 and Ara h 3), 2S albumins (Arah 2 and Ara h 6), Ara h 8 (pathogenesis related class-10 protein) and Ara h 5 (profilin) are relatively well characterized in terms of their 3D structures. However some peanut allergens like Ara h 7 (2S albumin), Ara h 9 (nonspecific lipid-transfer protein), and especially oleosins (Ara h 10 and Ara h 11) and defensins (Ara h 12 and Ara h 13), still are waiting for such characterization.

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