Vicilin and the basic subunit of legumin are putative chickpea allergens

Shimrit Bar-El Dadon, Cristina Yolanda Pascual, Dani Eshel, Paula Teper-Bamnolker, María Dolores Paloma Ibáñez, Ram Reifen*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

32 Scopus citations


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.

Original languageAmerican English
Pages (from-to)13-18
Number of pages6
JournalFood Chemistry
Issue number1
StatePublished - 1 May 2013


  • Chickpea
  • Cross reactivity
  • Food allergy
  • IgE
  • Legumes


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