Glycoform of a newly identified pollen allergen, Cha o 3, from Chamaecyparis obtusa (Japanese cypress, Hinoki)

Toshihiro Osada, Megumi Maeda, Chinatsu Tanabe, Kaori Furuta, Christopher J. Vavricka, Eiji Sasaki, Mitsuhiro Okano, Yoshinobu Kimura

Research output: Contribution to journalArticlepeer-review

8 Citations (Scopus)


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.

Original languageEnglish
Pages (from-to)18-23
Number of pages6
JournalCarbohydrate Research
Publication statusPublished - 2017


  • Antigenic N-glycan
  • Cha o 3
  • Chamaecyparis obtuse
  • Japanese cypress
  • Pollen allergen

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry


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