C-Terminal 23 kDa polypeptide of soybean Gly m Bd 28 K is a potential allergen

Planta
Ping XiangGautam Sarath

Abstract

Gly m Bd 28 K is a major soybean (Glycine max Merr.) glycoprotein allergen. It was originally identified as a 28 kDa polypeptide in soybean seed flour. However, the full-length protein is encoded by an open reading frame (ORF) of 473 amino acids, and contains a 23 kDa C-terminal polypeptide of as yet unknown allergenic and structural characteristics. IgE-binding (allergenic potential) of the Gly m Bd 28 K protein including the 23 kDa C-terminal portion as well as shorter fragments derived from the full-length ORF were evaluated using sera from soy-sensitive adults. All of these sera contained IgE that efficiently recognized the C-terminal region. Epitope mapping demonstrated that a dominant linear C-terminal IgE binding epitope resides between residues S256 and A270. Alanine scanning of this dominant epitope indicated that five amino acids, Y260, D261, D262, K264 and D266, contribute most towards IgE-binding. A model based on the structure of the beta subunit of soybean beta-conglycinin revealed that Gly m Bd 28 K contains two cupin domains. The dominant epitope is on the edge of the first beta-sheet of the C-terminal cupin domain and is present on a potentially solvent-accessible loop connecting the two cupin domains. Thus, th...Continue Reading

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Jan 16, 2013·Journal of Agricultural and Food Chemistry·Bin LiuJianhua Wang
May 24, 2012·Journal of Clinical Bioinformatics·Elena LópezJesús F Crespo
Feb 10, 2016·Journal of Agricultural and Food Chemistry·Ángela María CandrevaSilvana Petruccelli
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