RT Journal Article
T1 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.
A1 Jimenez-Lopez, Jose C
A1 Foley, Rhonda C
A1 Brear, Ella
A1 Clarke, Victoria C
A1 Lima-Cabello, Elena
A1 Florido, Jose F
A1 Singh, Karam B
A1 Alché, Juan D
A1 Smith, Penelope M C
K1 Conglutins
K1 Cross-allergenicity
K1 Diagnosis
K1 Food allergy
K1 IgE-binding activity
K1 Immunotherapy
K1 Recombinant allergen
K1 Seed storage proteins
K1 Sweet lupin
K1 Vicilin
AB 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.
YR 2017
FD 2017-10-06
LK http://hdl.handle.net/10668/11783
UL http://hdl.handle.net/10668/11783
LA en
DS RISalud
RD Apr 6, 2025