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

Détails

ID Serval
serval:BIB_E63622E29BB3
Type
Article: article d'un périodique ou d'un magazine.
Collection
Publications
Titre
Hepatitis C virus RNA replication requires a conserved structural motif within the transmembrane domain of the NS5B RNA-dependent RNA polymerase.
Périodique
Journal of Virology
Auteur(s)
Brass V., Gouttenoire J., Wahl A., Pal Z., Blum H.E., Penin F., Moradpour D.
ISSN
1098-5514[electronic], 0022-538X[linking]
Statut éditorial
Publié
Date de publication
2010
Volume
84
Numéro
21
Pages
11580-11584
Langue
anglais
Résumé
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.
Mots-clé
membrane association, insertion, protein, determinants, sequences, anchor, model
Pubmed
Web of science
Création de la notice
27/10/2010 13:47
Dernière modification de la notice
20/08/2019 17:09
Données d'usage