Characterization of narrow-leaf lupin (Lupinus angustifolius L.) recombinant major allergen IgE-binding proteins and the natural β-conglutin counterparts in sweet lupin seed species
Date
2018-04-01
Authors
Jimenez-Lopez, Jose C.
Foley, Rhonda C.
Brear, Ella
Clarke, Victoria C.
Lima-Cabello, Elena
Florido, Jose F.
Singh, Karam B.
Alché, Juan D.
Smith, Penelope M. C.
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Elsevier
Abstract
β-conglutin has been identified as a major allergen for Lupinus angustifolius seeds. The aim of this study was to evaluate the binding of IgE to five recombinant β-conglutin isoforms (rβ) that we overexpressed and purified and to their natural counterparts in different lupin species and cultivars. Western blotting suggested β-conglutins were the main proteins responsible for the IgE reactivity of the lupin species and cultivars. Newly identified polypeptides from "sweet lupin" may constitute a potential new source of primary or cross-reactive sensitization to lupin, particularly to L. albus and L. angustifolius seed proteins. Several of them exhibited qualitative and quantitative differences in IgE-binding among these species and cultivars, mainly in sera from atopic patients that react to lupin rather than peanut. IgE-binding was more consistent to recombinant β2 than to any of the other isoforms, making this protein a potential candidate for diagnosis and immunotherapy.
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Keywords
conglutins, cross-allergenicity, diagnosis, food allergy, ige-binding activity, immunotherapy, recombinant allergen, seed storage proteins, sweet lupin, vicilin
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Food chemistry
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Journal article
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Open Access
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