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Identification of a Brazil-Nut Allergen in Transgenic Soybeans

Nordlee, Julie A., Taylor, Steve L., Townsend, Jeffrey A., Thomas, Laurie A., Bush, Robert K.·1996·New England Journal of Medicine

Abstract

BACKGROUND: The nutritional quality of soybeans (Glycine max) is compromised by a relative deficiency of methionine in the protein fraction of the seeds. To improve the nutritional quality, methionine-rich 2S albumin from the Brazil nut (Betholletia excelsa) has been introduced into transgenic soybeans. Since the Brazil nut is a known allergenic food, we assessed the allergenicity of the 2S albumin. METHODS: The ability of proteins in transgenic and non-transgenic soybeans, Brazil nuts, and purified 2S albumin to bind to IgE in serum from subjects allergic to Brazil nuts was determined by radioallergosorbent tests (4 subjects) and sodium dodecyl sulfate-polyacrylamide-gel electrophoresis (9 subjects) with immunoblotting and autoradiography. Three subjects also underwent skin-prick testing with extracts of soybean, transgenic soybean, and Brazil nut. RESULTS: On radioallergosorbent testing of pooled serum from four subjects allergic to Brazil nuts, protein extracts of transgenic soybean inhibited binding of IgE to Brazil-nut proteins. On immunoblotting, serum IgE from eight of nine subjects bound to purified 2S albumin from the Brazil nut and the transgenic soybean. On skin-prick testing, three subjects had positive reactions to extracts of Brazil nut and transgenic soybean and negative reactions to soybean extract. CONCLUSIONS: The 2S albumin is probably a major Brazil-nut allergen, and the transgenic soybeans analyzed in this study contain this protein. Our study show that an allergen from a food known to be allergenic can be transferred into another food by genetic engineering.

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Authors
Nordlee, J. A., Taylor, S. L., Townsend, J. A., Thomas, L. A., & Bush, R. K.
Venue
New England Journal of Medicine
Published
1996-03-14
Volume
334
Issue
11
Pages
688-692
ISSN
  • 0028-4793 (ISSN-L)
  • 1533-4406
OpenAlex
W2314231266
Cited by
670
References
0
FWCI
9.87
Type
journal article
Language
en
Open access
closed

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