TY - JOUR
T1 - Glycoform of a newly identified pollen allergen, Cha o 3, from Chamaecyparis obtusa (Japanese cypress, Hinoki)
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
N1 - Funding Information:
This work was supported in part by grants from the Ministry of Education, Culture, Sports, Science, and Technology of Japan Basic Research C (no. 15K07841 to M.M.) and Fostering Joint International Research (no. 15KK0282) to M.M, and the Japan Science and Technology Agency (Adaptable and Seamless Technology Transfer Program through Target-driven R&D (A-step). no. AS262Z00115Q to YK). We are grateful to the Department of Instrumental Analysis, Advanced Science Research Center, Okayama University, for ESI-MS analysis.
Publisher Copyright:
© 2017 Elsevier Ltd
PY - 2017
Y1 - 2017
N2 - 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.
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.
KW - Antigenic N-glycan
KW - Cha o 3
KW - Chamaecyparis obtuse
KW - Japanese cypress
KW - Pollen allergen
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U2 - 10.1016/j.carres.2017.05.005
DO - 10.1016/j.carres.2017.05.005
M3 - Article
C2 - 28575723
AN - SCOPUS:85019741880
SN - 0008-6215
VL - 448
SP - 18
EP - 23
JO - Carbohydrate Research
JF - Carbohydrate Research
ER -