Identification of an IgE epitope of soybean allergen Gly m Bd 60K

被引:15
|
作者
He, MengXue [1 ]
Xi, Jun [1 ]
机构
[1] Henan Univ Technol, Sch Food Sci & Technol, Zhengzhou 450001, Henan, Peoples R China
基金
中国国家自然科学基金;
关键词
Gly m Bd 60K; Overlapping peptide; IgE epitope; Critical amino acids; BETA-CONGLYCININ; ALPHA-SUBUNIT; PROTEINS;
D O I
10.1016/j.lwt.2020.110131
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
Soybeans (Glycine max L.) are one of the most important sources of food allergens, along with cow's milk and eggs; they are recognized as the "three major allergens" of children, which seriously affect children's health. ss-conglycinin is the major soybean allergen, and the alpha subunit of beta-conglycinin, Gly m Bd 60K, is an important allergen in susceptible populations; it was the earliest recognized major allergenic protein. Before this work, we confirmed that the processing treatment reduced the antigenicity of beta-conglycinin, and we located the destroyed antigenic sites of Gly m Bd 60K after three processing technologies. In this paper, we used overlapping peptide technology to further study the destroyed antigenic sites of Gly m Bd 60 K. Finally, one epitope that contained both conformational and a linear IgE epitope was found with an amino acid sequence of (380)EGQQQGEQRLQ(390). Alanine scanning of this fragment documented that Q382, Q383, G385, and Q387 were the critical amino acids of this epitope.
引用
收藏
页数:6
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