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

Jose C. Jimenez-Lopez, Rhonda C. Foley, Ella Brear, Victoria C. Clarke, Elena Lima-Cabello, Jose F. Florido, Karam B. Singh, Juan D. Alché, Penelope M.C. Smith

Research output: Contribution to journalArticle

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.

LanguageEnglish
Pages60-70
Number of pages11
JournalFood Chemistry
Volume244
DOIs
StatePublished - 1 Apr 2018

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Lupinus
Galectin 3
Lupinus angustifolius
allergens
Allergens
Immunoglobulin E
Seed
binding proteins
Seeds
seeds
leaves
Protein Isoforms
cultivars
Immunotherapy
proteins
immunotherapy
Proteins
Western Blotting
peanuts
polypeptides

Cite this

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./ 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. In: Food Chemistry. 2018 ; Vol. 244. pp. 60-70
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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. / 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.

In: Food Chemistry, Vol. 244, 01.04.2018, p. 60-70.

Research output: Contribution to journalArticle

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