Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles

被引:60
作者
Werr, M [1 ]
Prange, R [1 ]
机构
[1] UNIV MAINZ,INST MED MICROBIOL & HYG,D-55101 MAINZ,GERMANY
关键词
D O I
10.1128/JVI.72.1.778-782.1998
中图分类号
Q93 [微生物学];
学科分类号
071005 ; 100705 ;
摘要
Unlike those of the S and the L envelope proteins, the functional role of the related M protein in the life cycle of the hepatitis B virus (HBV) is less understood. We now demonstrate that a single N glycan, specific for M, is required for efficient secretion of M empty envelope particles. Moreover, this glycan mediates specific association of M with the chaperone calnexin. Conversely, the N glycan, common to all three envelope proteins, is involved neither in calnexin binding nor in subviral particle release. As proper folding and trafficking of M need the assistance of the chaperone, the glycan-dependent association of M with calnexin may thus play a crucial role in the assembly of HBV. Beyond being modified by N glycosylation, M is modified by O glycosylation occurring within its amino acid sequence at positions 27 to 47. The O glycans, however, were found to be dispensable for secretion of M but may rather support viral infectivity. Surprisingly, nonglycosylated M localizes exclusively to the cytosol, either for degradation or for a yet-unknown function.
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页码:778 / 782
页数:5
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