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Epitope mapping of the major allergen 2S albumin from pine nut.
Crespo, Jesus F; Bueno, Cristina; Villalba, Mayte; Monaci, Linda; Cuadrado, Carmen; Novak, Natalija; Cabanillas, Beatriz.
Afiliação
  • Crespo JF; Department of Allergy, Research Institute Hospital 12 de Octubre, Avenida de Córdoba s/n, 28041 Madrid, Spain.
  • Bueno C; Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain.
  • Villalba M; Departamento de Bioquímica y Biología Molecular, Facultad de Ciencias Químicas, Universidad Complutense de Madrid, Madrid, Spain.
  • Monaci L; Institute of Sciences of Food Production, CNR-ISPA, 70126 Bari, Italy.
  • Cuadrado C; Department of Food Technology, National Institute of Agricultural, Food Research, and Technology (INIA), Ctra. La Coruña Km. 7.5, 28040 Madrid, Spain.
  • Novak N; Department of Dermatology and Allergy, University Hospital Bonn, Venusberg Campus 1, 53127 Bonn, Germany.
  • Cabanillas B; Department of Allergy, Research Institute Hospital 12 de Octubre, Avenida de Córdoba s/n, 28041 Madrid, Spain. Electronic address: bcabanillas.imas12@h12o.es.
Food Chem ; 339: 127895, 2021 Mar 01.
Article em En | MEDLINE | ID: mdl-32866706
ABSTRACT
The epitopes of the major allergen of pine nut, Pin p 1, were analyzed using a peptide library and sera from patients with clinical allergy to pine nut in order to deepen into the allergenic characteristics of Pin p 1. Analyses of epitope similarities and epitopes location in a 3D-model were also performed. Results showed that three main regions of Pin p 1 containing 5 epitopes were recognized by patient sera IgE. The epitopes of Pin p 1 had important similarities with epitopes of allergenic 2S albumins from peanut (Ara h 2 and 6) and Brazil nut (Ber e 1). The epitopes of Pin p 1 were found in α-helices and coils in the 3D protein structure. Interestingly, all epitopes were found to be well-exposed in the protein surface, which suggests facile access for IgE-binding to the structure of Pin p 1 which is known to be highly resistant.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Alérgenos / Mapeamento de Epitopos / Pinus / Albuminas 2S de Plantas / Epitopos Idioma: En Ano de publicação: 2021 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Alérgenos / Mapeamento de Epitopos / Pinus / Albuminas 2S de Plantas / Epitopos Idioma: En Ano de publicação: 2021 Tipo de documento: Article