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Glycoform of a newly identified pollen allergen, Cha o 3, from Chamaecyparis obtusa (Japanese cypress, Hinoki).
Osada, Toshihiro; Maeda, Megumi; Tanabe, Chinatsu; Furuta, Kaori; Vavricka, Christopher J; Sasaki, Eiji; Okano, Mitsuhiro; Kimura, Yoshinobu.
Afiliação
  • Osada T; Discovery and Preclinical Research Division, Taiho Pharmaceutical Co., Ltd, Tsukuba, Ibaraki 300-2611, Japan.
  • Maeda M; Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama 700-8530, Japan.
  • Tanabe C; Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama 700-8530, Japan.
  • Furuta K; Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama 700-8530, Japan.
  • Vavricka CJ; Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama 700-8530, Japan; Graduate School of Science Technology and Innovation, Kobe University, Kobe 657-8501, Japan.
  • Sasaki E; Discovery and Preclinical Research Division, Taiho Pharmaceutical Co., Ltd, Tsukuba, Ibaraki 300-2611, Japan.
  • Okano M; Department of Otolaryngology - Head and Neck Surgery, Okayama University, Graduate School of Medicine and Dentistry, Okayama 700-8558, Japan.
  • Kimura Y; Department of Biofunctional Chemistry, Graduate School of Environmental and Life Science, Okayama University, 1-1-1 Tsushima-Naka, Okayama 700-8530, Japan. Electronic address: yosh8mar@okayama-u.ac.jp.
Carbohydr Res ; 448: 18-23, 2017 Aug 07.
Article em En | MEDLINE | ID: mdl-28575723
Cha o 3 is a newly found glycosylated allergen from Chamaecyparis obtusa (Japanese cypress) pollen. The deduced amino acid sequence of Cha o 3 indicates that this glycoallergen contains a cellulase domain and a number of putative N-glycosylation sites. However, the structures of N -glycans linked to Cha o 3 remain to be determined. In this study, therefore, we analyzed the glycoform of Cha o 3 and found that this glycoallergen carries exclusively plant complex-type N-glycans; major structures were GlcNAc2Man3Xyl1Fuc1GlcNAc2 (39%), Gal1Fuc1GlcNAc2Man3Xyl1Fuc1GlcNAc2 (14%), and Gal2Fuc2GlcNAc2Man3Xyl1Fuc1GlcNAc2 (25%). The glycoform of Cha o 3 bearing the Lea epitope is similar to those of Cry j1, Jun a 1, or Cup a 1, major glycoallergens in cedar or cypress pollens, and the predominant occurrence of GlcNAc2Man3Xyl1Fuc1GlcNAc2 is a common structural feature of glycoallergens from Cupressaceae pollens.
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Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Pólen / Polissacarídeos / Alérgenos / Chamaecyparis Idioma: En Revista: Carbohydr Res Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Japão País de publicação: Holanda

Texto completo: 1 Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Pólen / Polissacarídeos / Alérgenos / Chamaecyparis Idioma: En Revista: Carbohydr Res Ano de publicação: 2017 Tipo de documento: Article País de afiliação: Japão País de publicação: Holanda