Your browser doesn't support javascript.
loading
1H, 13C and 15N resonance assignments and second structure information of Fag s 1: Fagales allergen from Fagus sylvatica.
Moraes, A H; Asam, C; Batista, A; Almeida, F C L; Wallner, M; Ferreira, F; Valente, A P.
Afiliação
  • Moraes AH; Centro Nacional de Ressonância Magnética, Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
  • Asam C; Christian Doppler Laboratory for Allergy Diagnosis and Therapy, University of Salzburg, Salzburg, Austria.
  • Batista A; Centro Nacional de Ressonância Magnética, Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
  • Almeida FC; Centro Nacional de Ressonância Magnética, Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil.
  • Wallner M; Christian Doppler Laboratory for Allergy Diagnosis and Therapy, University of Salzburg, Salzburg, Austria.
  • Ferreira F; Christian Doppler Laboratory for Allergy Diagnosis and Therapy, University of Salzburg, Salzburg, Austria.
  • Valente AP; Centro Nacional de Ressonância Magnética, Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil. valente@cnrmn.bioqmed.ufrj.br.
Biomol NMR Assign ; 10(1): 45-8, 2016 Apr.
Article em En | MEDLINE | ID: mdl-26289775
Fagales allergens belonging to the Bet v 1 family account responsible for the majority of spring pollinosis in the temperate climate zones in the Northern hemisphere. Among them, Fag s 1 from beech pollen is an important trigger of Fagales pollen associated allergic reactions. The protein shares high similarity with birch pollen Bet v 1, the best-characterized member of this allergen family. Of note, recent work on Bet v 1 and its homologues found in Fagales pollen demonstrated that not all allergenic members of this family have the capacity to induce allergic sensitization. Fag s 1 was shown to bind pre-existing IgE antibodies most likely primarily directed against other members of this multi-allergen family. Therefore, it is especially interesting to compare the structures of Bet v 1-like pollen allergens, which have the potential to induce allergic sensitization with allergens that are mainly cross-reactive. This in the end will help to identify allergy eliciting molecular pattern on Bet v 1-like allergens. In this work, we report the (1)H, (15)N and (13)C NMR assignment of beech pollen Fag s 1 as well as the secondary structure information based on backbone chemical shifts.
Assuntos
Palavras-chave
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Alérgenos / Ressonância Magnética Nuclear Biomolecular / Fagus Idioma: En Revista: Biomol NMR Assign Assunto da revista: BIOLOGIA MOLECULAR / MEDICINA NUCLEAR Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda
Texto completo
Adicionar na Minha BVS
Imprimir
XML
PubMed Links
Buscar no Google

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Proteínas de Plantas / Alérgenos / Ressonância Magnética Nuclear Biomolecular / Fagus Idioma: En Revista: Biomol NMR Assign Assunto da revista: BIOLOGIA MOLECULAR / MEDICINA NUCLEAR Ano de publicação: 2016 Tipo de documento: Article País de afiliação: Brasil País de publicação: Holanda