Glycoform analysis of Japanese cypress pollen allergen, Cha o 1: A comparison of the glycoforms of cedar and Cypress pollen allergens

Yoshinobu Kimura, Misao Kuroki, Megumi Maeda, Mitsuhiro Okano, Minehiko Yokoyama, Kosuke Kino

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A Japanese cypress (Chamaecyparis obtusa) pollen allergen, Cha o 1, is one of the major allergens that cause allergic pollinosis in Japan. Although it has been found that Cha o 1 is glycosylated and that the amino acid sequence is highly homologous with that of Japanese cedar pollen allergen (Cry j 1), the structure of N-glycans linked to Cha o 1 remains to be determined. In this study, therefore, we analyzed the structures of the N-glycans of Cha o1. The N-glycans were liberated by hydrazinolysis from purified Cha o 1, and the resulting sugar chains were N-acetylated and pyridylaminated. The structures of pyridylaminated N-glycans were analyzed by a combination of exoglycosidase digestion, two dimensional (2D-) sugar chain mapping, and electrospray ionization mass spectrometry analysis. Structural analysis indicated that the major N-glycan structure of Cha o1 is GlcNAc2Man3Xyl1-Fuc1GlcNAc2 (89%), and that high-mannose type structures (Man9GlcNAc2, Man7GlcNAc2) occur as minor components (11%).

Original languageEnglish
Pages (from-to)485-491
Number of pages7
JournalBioscience, Biotechnology and Biochemistry
Issue number2
Publication statusPublished - 2008



  • Antigenic oligosaccharide
  • Cha o 1
  • Chamaecyparis obtusa
  • Japanese cypress pollen allergen
  • N-glycan structure

ASJC Scopus subject areas

  • Bioengineering
  • Biotechnology
  • Biochemistry
  • Biochemistry, Genetics and Molecular Biology(all)
  • Chemistry (miscellaneous)
  • Applied Microbiology and Biotechnology
  • Food Science

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