Document Detail


Crystal structure of peanut (Arachis hypogaea) allergen Ara h 5.
MedLine Citation:
PMID:  23350842     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
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 angstrom. 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 IgE epitopes needs to be interpreted with caution.
Authors:
Yang Wang; Tong-Jen Fu; Andrew Howard; Mahendra H Kothary; Tara H McHugh; Yu-Zhu Zhang
Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-1-25
Journal Detail:
Title:  Journal of agricultural and food chemistry     Volume:  -     ISSN:  1520-5118     ISO Abbreviation:  J. Agric. Food Chem.     Publication Date:  2013 Jan 
Date Detail:
Created Date:  2013-1-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  0374755     Medline TA:  J Agric Food Chem     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
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