|OFFERMAN, LESA - University Of South Carolina|
|PERDUE, MAKENZIE - University Of South Carolina|
|HE, JOHN - University Of South Carolina|
|CHRUSZCZ, MAKSYMILIAN - University Of South Carolina|
Submitted to: Journal of Contemporary Immunology
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/30/2014
Publication Date: 1/3/2015
Citation: Offerman, L., Perdue, M., He, J., Hurlburt, B.K., Maleki, S.J., Chruszcz, M. 2015. Structural biology of peanut allergens. Journal of Contemporary Immunology. 2(1):1-26.
Interpretive Summary: Peanut allergy is on the rise world wide and can cause a range of reactions from mild itching/burning of the mouth to deadly anaphylaxis. Twelve proteins in peanut have been identified as the cause of the allergic reaction. Considerable effort has been expended recently to understand allergen reactivity. Towards that goal, the 3-dimensional structures of the allergens are being determined. This review summarizes the status of the structural biological analysis of peanut allergens.
Technical 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; therefore, 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. While allergens from cupin (Ara h 1 and Ara h 3) and prolamin (Arah 2, Ara h 6, Ara h 7 and Ara h 9) superfamilies are relatively well characterized in terms of their 3D structures, some peanut allergens like oleosins (Ara h 10 and Ara h 11), as well as defensins (Ara h 12 and Ara h 13) still are waiting for such characterization.