All Three Subunits of Soybean β-Conglycinin Are Potential Food Allergens

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• 作者：Hari B. Krishnan ; Won-Seok Kim ; Sungchan Jang ; Monty S. Kerley
• 刊名：Journal of Agricultural and Food Chemistry
• 出版年：2009
• 出版时间：February 11, 2009
• 年：2009
• 卷：57
• 期：3
• 页码：938-943
• 全文大小：175K
• 年卷期：v.57,no.3(February 11, 2009)
• ISSN：1520-5118

文摘

Soybeans are recognized as one of the “big 8” food allergens. IgE antibodies from soybean-sensitive patients recognize more than 15 soybean proteins. Among these proteins only the α-subunit of β-conglycinin, but not the highly homologous α′- and β-subunits, has been shown to be a major allergenic protein. The objective of this study was to examine if the α′- and β-subunits of β-conglycinin can also serve as potential allergens. Immunoblot analysis using sera collected from soybean-allergic patients revealed the presence of IgE antibodies that recognized several soy proteins including 72, 70, 52, 34, and 21 kDa proteins. Matrix-assisted laser desorption ionization time-of-flight mass spectrometry (MALDI-TOF) analysis of trypsin-digested 72, 70, and 52 kDa proteins indicated that these proteins were the α′-, α-, and β-subunits of β-conglycinin, respectively. Additionally, purified α′-, α-, and β-subunits of β-conglycinin were recognized by IgE antibodies present in the soybean-allergic patients. The IgE reactivity to the β-subunit of β-conglycinin was not abolished when this glycoprotein was either deglycosylated using glycosidases or expressed as a recombinant protein in Escherichia coli. The results suggest that in addition to the previously recognized α-subunit of β-conglycinin, the α′- and β-subunits of β-conglycinin also are potential food allergens.