Phosphorylation of hepatitis C virus nonstructural protein 5A modulates its protein interactions and viral RNA replication.

ABSTRACT: The study of the hepatitis C virus (HCV) has been hindered by the lack of in vitro model systems. The recent development of HCV subgenomic RNA replicons has permitted the study of viral RNA replication in cell culture; however, the requirements for efficient replication of replicons in this system are poorly understood. Many viral isolates do not function as replicons and most require conserved changes, termed adaptive mutations, to replicate efficiently. In this report, we focus on the HCV nonstructural protein 5A (NS5A), a frequent locus for adaptive mutation. We found the interaction between NS5A and human vesicle-associated membrane protein-associated protein A (hVAP-A), a cellular target N-ethylmaleimide-sensitive factor attachment protein receptor, to be required for efficient RNA re

SUBMITTER: Evans MJ 

PROVIDER: S-EPMC516513 | biostudies-literature | 2004 Aug

REPOSITORIES: biostudies-literature