Hepatitis C Virus RNA Replication Requires a Conserved Structural Motif within the Transmembrane Domain of the NS5B RNA-Dependent RNA Polymerase

被引：16

作者：

Brass, Volker ^{[1
]}

Gouttenoire, Jerome ^{[2
]}

Wahl, Anja ^{[1
]}

Pal, Zsuzsanna ^{[1
]}

Blum, Hubert E. ^{[1
]}

Penin, Francois ^{[3
]}

Moradpour, Darius ^{[2
]}

机构：

[1] Univ Freiburg, Dept Med 2, D-79106 Freiburg, Germany

[2] Univ Lausanne, CHU Vaudois, Div Gastroenterol & Hepatol, CH-1011 Lausanne, Switzerland

[3] Univ Lyon, Inst Biol & Chim Prot, IFR BioSci Gerland Lyon Sud 128, CNRS,UMR 5086, F-69397 Lyon, France

来源：

JOURNAL OF VIROLOGY | 2010年 / 84卷 / 21期

基金：

瑞士国家科学基金会;

关键词：

MEMBRANE ASSOCIATION; INSERTION; PROTEIN; DETERMINANTS; SEQUENCES; ANCHOR; MODEL;

D O I：

10.1128/JVI.01519-10

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

Hepatitis C virus (HCV) nonstructural protein 5B (NS5B), the viral RNA-dependent RNA polymerase (RdRp), is a tail-anchored protein with a highly conserved C-terminal transmembrane domain (TMD) that is required for the assembly of a functional replication complex. Here, we report that the TMD of the HCV RdRp can be functionally replaced by a newly identified analogous membrane anchor of the GB virus B (GBV-B) NS5B RdRp. Replicons with a chimeric RdRp consisting of the HCV catalytic domain and the GBV-B membrane anchor replicated with reduced efficiency. Compensatory amino acid changes at defined positions within the TMD improved the replication efficiency of these chimeras. These observations highlight a conserved structural motif within the TMD of the HCV NS5B RdRp that is required for RNA replication.

引用

页码：11580 / 11584

页数：5

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