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N ‐linked oligosaccharide chains of Sendai virus fusion protein determine the interaction with endoplasmic reticulum molecular chaperones
Author(s) -
Tamura Taku,
Yamashita Tetsuro,
Segawa Hiroaki,
Taira Hideharu
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02229-9
Subject(s) - endoplasmic reticulum , sendai virus , oligosaccharide , immunoprecipitation , glycosylation , chemistry , endoplasmic reticulum associated protein degradation , mutant , fusion protein , protein folding , biochemistry , glycoprotein , microbiology and biotechnology , biology , gene , unfolded protein response , recombinant dna
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.