TY - JOUR
T1 - Vicilin and the basic subunit of legumin are putative chickpea allergens
AU - Bar-El Dadon, Shimrit
AU - Pascual, Cristina Yolanda
AU - Eshel, Dani
AU - Teper-Bamnolker, Paula
AU - Paloma Ibáñez, María Dolores
AU - Reifen, Ram
PY - 2013/5/1
Y1 - 2013/5/1
N2 - 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.
AB - 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.
KW - Chickpea
KW - Cross reactivity
KW - Food allergy
KW - IgE
KW - Legumes
UR - http://www.scopus.com/inward/record.url?scp=84869204001&partnerID=8YFLogxK
U2 - 10.1016/j.foodchem.2012.10.031
DO - 10.1016/j.foodchem.2012.10.031
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C2 - 23265449
AN - SCOPUS:84869204001
SN - 0308-8146
VL - 138
SP - 13
EP - 18
JO - Food Chemistry
JF - Food Chemistry
IS - 1
ER -