N‐linked oligosaccharide chains of Sendai virus fusion protein determine the interaction with endoplasmic reticulum molecular chaperones

FEBS Letters

Taira, Hideharu¹  Segawa, Hiroaki¹  Yamashita, Tetsuro¹  Tamura, Taku¹ 

[1] Faculty of Agriculture, Iwate University, Ueda, Morioka, Iwate 020-8550, Japan

关键词: Sendai virus fusion protein;    Calnexin;    BiP;    ERp57;    N-linked oligosaccharide chain;    F protein;    Sendai virus fusion protein;    CNX;    calnexin;    CRT;    calreticulin;    ER;    endoplasmic reticulum;    CHAPS;    3-[(3-cholamidopropyl)-dimethylammonio]-1-propane-sulfonate;    CST;    castanospermine;    PBS;    phosphate-buffered saline;    TBS;    Tris-buffered saline;   

DOI  :  10.1016/S0014-5793(02)02229-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The selectivity and individual roles of the N-linked oligosaccharide chains of Sendai virus fusion protein (F protein) in the interaction with endoplasmic reticulum molecular chaperones were investigated by analyses of transient expression of single N-glycosylation mutants and sequential immunoprecipitation. We demonstrated differential interactions depending on the location of the N-linked oligosaccharide chain, and showed that these interactions were correlated with the folding and transport of F proteins. Moreover, mutant F proteins that lacked the specific N-linked oligosaccharide chains required for disulfide bond formation showed increased association with ERp57.

【 授权许可】

Unknown