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

Research output: Research - peer-reviewArticle

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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: Research - peer-reviewArticle

Harvard

Jimenez-Lopez, JC, Foley, RC, Brear, E, Clarke, VC, Lima-Cabello, E, Florido, JF, Singh, KB, Alché, JD & Smith, PMC 2018, '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' Food Chemistry, vol 244, pp. 60-70. DOI: 10.1016/j.foodchem.2017.10.015

APA

Jimenez-Lopez, J. C., Foley, R. C., Brear, E., Clarke, V. C., Lima-Cabello, E., Florido, J. F., ... Smith, P. M. C. (2018). 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. Food Chemistry, 244, 60-70. DOI: 10.1016/j.foodchem.2017.10.015

Vancouver

Jimenez-Lopez JC, Foley RC, Brear E, Clarke VC, Lima-Cabello E, Florido JF et al. 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. Food Chemistry. 2018 Apr 1;244:60-70. Available from, DOI: 10.1016/j.foodchem.2017.10.015

Author

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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@article{c2832770158048cca3e5dc156ffd352d,
title = "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",
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.",
keywords = "Conglutins, Cross-allergenicity, Diagnosis, Food allergy, IgE-binding activity, Immunotherapy, Recombinant allergen, Seed storage proteins, Sweet lupin, Vicilin",
author = "Jimenez-Lopez, {Jose C.} and Foley, {Rhonda C.} and Ella Brear and Clarke, {Victoria C.} and Elena Lima-Cabello and Florido, {Jose F.} and Singh, {Karam B.} and Alché, {Juan D.} and Smith, {Penelope M.C.}",
year = "2018",
month = "4",
doi = "10.1016/j.foodchem.2017.10.015",
volume = "244",
pages = "60--70",
journal = "Food chemistry",
issn = "0308-8146",
publisher = "Elsevier",

}

RIS

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TY - JOUR

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

AU - Jimenez-Lopez,Jose C.

AU - Foley,Rhonda C.

AU - Brear,Ella

AU - Clarke,Victoria C.

AU - Lima-Cabello,Elena

AU - Florido,Jose F.

AU - Singh,Karam B.

AU - Alché,Juan D.

AU - Smith,Penelope M.C.

PY - 2018/4/1

Y1 - 2018/4/1

N2 - 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.

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.

KW - Conglutins

KW - Cross-allergenicity

KW - Diagnosis

KW - Food allergy

KW - IgE-binding activity

KW - Immunotherapy

KW - Recombinant allergen

KW - Seed storage proteins

KW - Sweet lupin

KW - Vicilin

UR - http://www.scopus.com/inward/record.url?scp=85031013737&partnerID=8YFLogxK

U2 - 10.1016/j.foodchem.2017.10.015

DO - 10.1016/j.foodchem.2017.10.015

M3 - Article

VL - 244

SP - 60

EP - 70

JO - Food chemistry

T2 - Food chemistry

JF - Food chemistry

SN - 0308-8146

ER -

ID: 21599511