Article

All three subunits of soybean beta-conglycinin are potential food allergens.

U.S. Department of Agriculture, Division of Plant Sciences, Plant Genetics Research Unit, Agricultural Research Service, University of Missouri, Columbia, Missouri 65211, USA.
Journal of Agricultural and Food Chemistry (impact factor: 2.82). 02/2009; 57(3):938-43. DOI:10.1021/jf802451g pp.938-43
Source: PubMed

ABSTRACT 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 alpha-subunit of beta-conglycinin, but not the highly homologous alpha'- and beta-subunits, has been shown to be a major allergenic protein. The objective of this study was to examine if the alpha'- and beta-subunits of beta-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 alpha'-, alpha-, and beta-subunits of beta-conglycinin, respectively. Additionally, purified alpha'-, alpha-, and beta-subunits of beta-conglycinin were recognized by IgE antibodies present in the soybean-allergic patients. The IgE reactivity to the beta-subunit of beta-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 alpha-subunit of beta-conglycinin, the alpha'- and beta-subunits of beta-conglycinin also are potential food allergens.

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Data provided are for informational purposes only. Although carefully collected, accuracy cannot be guaranteed. The impact factor represents a rough estimation of the journal's impact factor and does not reflect the actual current impact factor. Publisher conditions are provided by RoMEO. Differing provisions from the publisher's actual policy or licence agreement may be applicable.

Keywords

15 soybean proteins
 
21 kDa proteins
 
52 kDa proteins
 
big 8
 
Escherichia coli
 
homologous alpha'-
 
IgE antibodies
 
IgE antibodies present
 
IgE reactivity
 
Immunoblot analysis
 
major allergenic protein
 
Matrix-assisted laser desorption ionization time-of-flight mass spectrometry
 
potential allergens
 
purified alpha'-
 
recombinant protein
 
soy proteins
 
soybean-allergic patients
 
soybean-sensitive patients
 
Soybeans
 
trypsin-digested 72