Abstract
Background and aim: Hepatitis C virus (HCV) nonstructural proteins form a membrane-associated replication complex. 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. The aim of this study was to further validate the function of the NS5B TMD in the process of replication complex formation.
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