NOVEL TRANSMEMBRANE TOPOLOGY OF THE HEPATITIS-B VIRUS ENVELOPE PROTEINS

被引:167
|
作者
PRANGE, R
STREECK, RE
机构
[1] Institute for Medical Microbiology, Johannes Gutenberg-Univ. Mainz, D-55101 Mainz, Augustusplatz
来源
EMBO JOURNAL | 1995年 / 14卷 / 02期
关键词
HBSAG; MEMBRANE PROTEINS; PRES DOMAIN; POST TRANSLATIONAL; PROTEIN TRANSLOCATION;
D O I
10.1002/j.1460-2075.1995.tb06998.x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The small (S), middle (M) and large (L) envelope proteins of the hepatitis B virus (HBV) are initially synthesized as multispanning membrane proteins of the endoplasmic reticulum membrane. We now demonstrate that all envelope proteins synthesized in transfected cells or in a cell-free system adopt more than one transmembrane orientation. The L protein disposes its N-terminal preS domain both to the cytoplasmic and the luminal side of the membrane. This unusual topology does not depend on interaction with the viral nucleocapsid, but is preserved in secreted empty envelope particles. Pulse-chase analysis suggests a novel process of post-translational translocation leading to the non-uniform topology, Analysis of L deletion mutants indicates that the block to co-translational translocation can be attributed to a specific sequence within preS, suggesting that translocation of L may be regulated. Additional topological heterogeneity is displayed in the S region of the envelope proteins and in the S protein itself, as assayed in a cell-free system, S proteins integrated into microsomal membranes exhibit both a luminal and a cytoplasmic orientation of the internal hydrophilic region carrying the major antigenic determinants. This may explain the unusual partial glycosylation of the HBV envelope proteins.
引用
收藏
页码:247 / 256
页数:10
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