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Brass, Volker; Gouttenoire, Jérôme; Wahl, Anja; Pal, Zsuzsanna; Blum, Hubert E.; Penin, François; Moradpour, Darius

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

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  • Media type: E-Article
  • Title: Hepatitis C Virus RNA Replication Requires a Conserved Structural Motif within the Transmembrane Domain of the NS5B RNA-Dependent RNA Polymerase
  • Contributor: Brass, Volker; Gouttenoire, Jérôme; Wahl, Anja; Pal, Zsuzsanna; Blum, Hubert E.; Penin, François; Moradpour, Darius
  • Published: American Society for Microbiology, 2010
  • Published in: Journal of Virology, 84 (2010) 21, Seite 11580-11584
  • Language: English
  • DOI: 10.1128/jvi.01519-10
  • ISSN: 0022-538X; 1098-5514
  • Keywords: Virology ; Insect Science ; Immunology ; Microbiology
  • Origination:
  • Footnote:
  • Description: <jats:title>ABSTRACT</jats:title> <jats:p>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.</jats:p>
  • Access State: Open Access