1. Purification of soybean cupins and comparison of IgE binding with peanut allergens in a population of allergic subjects.
- Author
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Ramadan S, Marsh J, El-Sherbeny GA, El-Halawany EF, Luan F, Baumert JL, Johnson P, Osman Y, and Goodman RE
- Subjects
- Amino Acid Sequence, Antigens, Plant chemistry, Chromatography, Liquid, Cross Reactions, Humans, Peanut Hypersensitivity, Protein Binding, Tandem Mass Spectrometry, Antigens, Plant immunology, Arachis chemistry, Globulins chemistry, Immunoglobulin E, Seed Storage Proteins chemistry, Soybean Proteins chemistry, Glycine max chemistry
- Abstract
Identification, purification and characterization of allergens is crucial to the understanding of IgE-mediated disease. Immunologic and structural studies with purified allergens is essential for understanding relative immunogenicity and cross-reactivity. In this work, the complex soybean 7S vicilins (Gly m 5) with three subunits and 11S legumins (Gly m 6) with five subunits were purified and characterized along with purified peanut allergens (Ara h 1, 2, 3, and 6) by label-free liquid chromatography-tandem mass spectrometry (LC-MS/MS). Individual subjects plasma IgE binding was tested from subjects allergic to soybeans and or peanuts by immunoblotting, ImmunoCAP™ and ISAC™ ImmunoCAP chip, comparing these soybean proteins with those of purified peanut allergens; vicilin (Ara h 1), 2S albumin (Ara h 2 and Ara h 6) and 11S globulin (Ara h 3). Results show differences between methods and subjects demonstrating the complexity of finding answers to questions of cross-reactivity., (Copyright © 2020 Elsevier Ltd. All rights reserved.)
- Published
- 2021
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