4esp

Publication Abstract from PubMed

Profilins from numerous species are known to be allergens, including food allergens, such as peanut ( Arachis hypogaea ) allergen Ara h 5, and pollen allergens, such as birch allergen Bet v 2. Patients with pollen allergy can also cross-react to peanut. Structural characterization of allergens will allow a better understanding of the allergenicity of food allergens and their cross-reactivities. The three-dimensional structures of most known food allergens remain to be elucidated. Here, we report the first crystallographic study of a food allergen in the profilin family. The structure of peanut allergen Ara h 5 was determined, and the resolution of the final refined structure was 1.1 A. Structure alignment revealed that Ara h 5 is more similar to Bet v 2 than to Hev b 8, although sequence alignment suggested that Ara h 5 is more closely related to Hev b 8 than to Bet v 2, indicating that homology-model-based prediction of immunoglobulin E epitopes needs to be interpreted with caution.

Crystal Structure of Peanut ( Arachis hypogaea ) Allergen Ara h 5.,Wang Y, Fu TJ, Howard A, Kothary MH, McHugh TH, Zhang Y J Agric Food Chem. 2013 Feb 20;61(7):1573-8. doi: 10.1021/jf303861p. Epub 2013, Feb 11. PMID:23350842^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.