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

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. W...

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Detalles Bibliográficos
Autores: Jiménez-López, José Carlos, Foley, Rhonda C., Brear, Ella, Clarke, Victoria C., Lima Cabello, Elena, Florido, José Fernando, Singh, Karam B., Alché Ramírez, Juan de Dios, Smith, Penelope M. C.
Tipo de recurso: artículo
Fecha de publicación:2018
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/164371
Acceso en línea:http://hdl.handle.net/10261/164371
Access Level:acceso abierto
Palabra clave:Food allergy
Diagnosis
Cross-allergenicity
Conglutins
IgE-binding activity
Immunotherapy
Seed storage proteins
Sweet lupin
Recombinant allergen
Vicilin
Descripción
Sumario: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.