Vicilin and the basic subunit of legumin are putative chickpea allergens

Bar-El Dadon , S. and Pascual , C.Y. and Eshel , D. and et al, . (2013) Vicilin and the basic subunit of legumin are putative chickpea allergens. Food Chemistry, 138 (1). pp. 13-18.

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IgE-mediated reactions to food allergens constitute a major health problem in industrialized countries. Chickpea is consumed in Mediterranean countries, and reportedly associated with IgE-mediated hypersensitivity reactions. However, the nature of allergic reactions to chickpea has not been characterized. A serum pool from paediatric patients allergic to chickpeas was used to detect IgE-binding proteins from chickpea seeds by immunoassay and immunoblot inhibition assay. Protein samples enriched in chickpea legumin and vicilin were obtained by anion exchange chromatography, and were identified by mass spectrometric analysis. IgE-immunoassays of globulin fractions from chickpeas revealed that vicilin (50 kDa) and the basic subunit of legumin (20 kDa) were bound by IgE from patient sera. Pea and lentil protein extracts strongly inhibited the IgE binding to chickpea globulin. We speculate that vicilin and the basic subunit of legumin are major chickpea allergens. Also, the globulin fraction of chickpea likely cross-reacts with the allergenic proteins of pea and lentil.

Item Type: Article
Uncontrolled Keywords: Chickpea, Legumes, Food allergy, Cross reactivity, IgE IgE
Author Affiliation: The School of Nutritional Sciences, The Robert H. Smith Faculty of Agriculture, Food and Environment, The Hebrew University of Jerusalem, Israel.
Subjects: Social Sciences > Agricultural Extension,Technology, ICT
Postharvest Management > Food Technology
Plant Physiology and Biochemistry > Plant Physiology
Divisions: Chickpea
Depositing User: Mr Arbind Seth
Date Deposited: 27 Aug 2013 05:40
Last Modified: 27 Aug 2013 05:40
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