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Epitopes from two soybean glycinin subunits are antigenic in pigs
Author(s) -
Taliercio Earl,
Kim Sung Woo
Publication year - 2013
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.6113
Subject(s) - epitope , antigen , biology , biochemistry , genetics
BACKGROUND Glycinin is a seed storage protein in soybean ( Glycine max ) that is allergenic in pigs. Glycinin is a hexamer composed of subunits consisting of basic and acidic portions joined by disulfide bridges. There are five glycinin subunit isoforms designated Gy1–Gy5. The purpose of this study is to identify epitopes from selected glycinin subunits that are antigenic in pigs . RESULTS Twenty‐seven out of 30 pigs had antibodies against glycinin in their sera. Ten of these sera had immunoglobulin G ( IgG ) against the Gy4 ( A5A4B3 ) or Gy1 ( A1aBx ) subunit. Three sera recognised overlapping regions between the two subunits tested, though no serum stained both A5A4B3 and A1aBx . Two sera stained a highly conserved region between A5A4B3 and A1aBx , though again neither serum stained both peptides. The basic part of the A1aBx subunit was not recognised by any of the sera tested even though immunoblot data indicated that the basic and acidic subunits of glycinin are nearly equally antigenic . CONCLUSION Two antigenic regions of A5A4B3 and A1aBx were identified that bound antibodies in half of the sera that reacted with these two proteins. Half of the sera reacted with unique regions of A5A4B3 and A1aBx . The failure of the basic portion of A1aBx to bind pig antibodies may indicate that it is less antigenic than the basic portion of A5A4B3 and other glycinin subunits. Published 2013. This article is a U.S. Government work and is in the public domain in the USA.