Hepatitis C virus RNA replication requires a conserved structural motif within the transmembrane domain of the NS5B RNA-dependent RNA polymerase.

Details

Serval ID
serval:BIB_E63622E29BB3
Type
Article: article from journal or magazin.
Collection
Publications
Title
Hepatitis C virus RNA replication requires a conserved structural motif within the transmembrane domain of the NS5B RNA-dependent RNA polymerase.
Journal
Journal of Virology
Author(s)
Brass V., Gouttenoire J., Wahl A., Pal Z., Blum H.E., Penin F., Moradpour D.
ISSN
1098-5514[electronic], 0022-538X[linking]
Publication state
Published
Issued date
2010
Volume
84
Number
21
Pages
11580-11584
Language
english
Abstract
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.
Keywords
membrane association, insertion, protein, determinants, sequences, anchor, model
Pubmed
Web of science
Create date
27/10/2010 13:47
Last modification date
20/08/2019 17:09
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