2013 journal article

Epitopes from two soybean glycinin subunits are antigenic in pigs

JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 93(12), 2927–2932.

By: E. Taliercio* & S. Kim n

author keywords: A1aBx; A5A4B3; allergen; antibody; ELISA; seed storage protein
MeSH headings : Amino Acid Sequence; Animals; Antigens, Plant / adverse effects; Antigens, Plant / analysis; Antigens, Plant / chemistry; Conserved Sequence; Cross Reactions; Crosses, Genetic; Dietary Proteins / adverse effects; Dietary Proteins / antagonists & inhibitors; Dietary Proteins / chemistry; Epitope Mapping / veterinary; Epitopes / analysis; Female; Food Hypersensitivity / blood; Food Hypersensitivity / etiology; Food Hypersensitivity / immunology; Food Hypersensitivity / veterinary; Globulins / adverse effects; Globulins / antagonists & inhibitors; Globulins / chemistry; Lactation; Pregnancy; Pregnancy Complications / blood; Pregnancy Complications / etiology; Pregnancy Complications / immunology; Pregnancy Complications / veterinary; Protein Subunits / adverse effects; Protein Subunits / antagonists & inhibitors; Protein Subunits / chemistry; Seed Storage Proteins / adverse effects; Seed Storage Proteins / antagonists & inhibitors; Seed Storage Proteins / chemistry; Soybean Proteins / adverse effects; Soybean Proteins / antagonists & inhibitors; Soybean Proteins / chemistry; Soybeans / adverse effects; Sus scrofa; Swine; Swine Diseases / blood; Swine Diseases / etiology; Swine Diseases / immunology; United States
TL;DR: Two antigenic regions of A5A4B3 and A1aBx were identified that bound antibodies in half of the sera that reacted with these two proteins, and the failure of the basic portion of A1 aBx to bind pig antibodies may indicate that it is less antigenic than the basic portions of A 5A4 B3 and other glycinin subunits. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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.