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 journalArticle

1 Citation (Scopus)

Abstract

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
Volume448
DOIs
Publication statusPublished - Aug 7 2017

Fingerprint

Chamaecyparis
Pollen
Cupressus
Allergens
Polysaccharides
Bearings (structural)
Glycosylation
Cellulase
Cupressaceae
Epitopes
Amino Acids
Amino Acid Sequence

Keywords

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

ASJC Scopus subject areas

  • Analytical Chemistry
  • Biochemistry
  • Organic Chemistry

Cite this

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.

In: Carbohydrate Research, Vol. 448, 07.08.2017, p. 18-23.

Research output: Contribution to journalArticle

Osada, Toshihiro ; Maeda, Megumi ; Tanabe, Chinatsu ; Furuta, Kaori ; Vavricka, Christopher J. ; Sasaki, Eiji ; Okano, Mitsuhiro ; Kimura, Yoshinobu. / Glycoform of a newly identified pollen allergen, Cha o 3, from Chamaecyparis obtusa (Japanese cypress, Hinoki). In: Carbohydrate Research. 2017 ; Vol. 448. pp. 18-23.
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abstract = "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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AU - Osada, Toshihiro

AU - Maeda, Megumi

AU - Tanabe, Chinatsu

AU - Furuta, Kaori

AU - Vavricka, Christopher J.

AU - Sasaki, Eiji

AU - Okano, Mitsuhiro

AU - Kimura, Yoshinobu

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AB - 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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