Glycoform analysis of Japanese cypress pollen allergen, Cha o 1: a comparison of the glycoforms of cedar and cypress pollen allergens.
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 GlcNAc2Man3Xyl1Fuc1GlcNAc2 (89%), and that high-mannose type structures (Man9GlcNAc2, Man7GlcNAc2) occur as minor components (11%).
Kimura
Yoshinobu
Y
Department of Biofunctional Chemistry, Graduate School of Natural Science and Technology, Okayama University, Japan. yosh8mar@cc.okayama-u.ac.jp
Kuroki
Misao
M
Maeda
Megumi
M
Okano
Mitsuhiro
M
Yokoyama
Minehiko
M
Kino
Kosuke
K
D002236:Carbohydrate Conformation; D002240:Carbohydrate Sequence; D002851:Chromatography, High Pressure Liquid; D002852:Chromatography, Ion Exchange; D029781:Cupressus / Q000276:immunology*; D004591:Electrophoresis, Polyacrylamide Gel; D006031:Glycosylation; D007536:Isomerism; D008969:Molecular Sequence Data; D010940:Plant Proteins / Q000737:chemistry* / Q000302:isolation & purification; D021241:Spectrometry, Mass, Electrospray Ionization
C408445:Cha o 1 protein, Chamaecyparis obtusa; D010940:Plant Proteins