%0 Journal Article
%A Jimenez-Lopez, Jose C
%A Foley, Rhonda C
%A Brear, Ella
%A Clarke, Victoria C
%A Lima-Cabello, Elena
%A Florido, Jose F
%A Singh, Karam B
%A Alché, Juan D
%A Smith, Penelope M C
%T 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.
%D 2017
%U http://hdl.handle.net/10668/11783
%X 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.
%K Conglutins
%K Cross-allergenicity
%K Diagnosis
%K Food allergy
%K IgE-binding activity
%K Immunotherapy
%K Recombinant allergen
%K Seed storage proteins
%K Sweet lupin
%K Vicilin
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