Conserved determinants for membrane association of nonstructural protein 5A from hepatitis C virus and related viruses.

ABSTRACT: Nonstructural protein 5A (NS5A) is a membrane-associated essential component of the hepatitis C virus (HCV) replication complex. An N-terminal amphipathic alpha helix mediates in-plane membrane association of HCV NS5A and at the same time is likely involved in specific protein-protein interactions required for the assembly of a functional replication complex. The aim of this study was to identify the determinants for membrane association of NS5A from the related GB viruses and pestiviruses. Although primary amino acid sequences differed considerably, putative membrane anchor domains with amphipathic features were predicted in the N-terminal domains of NS5A proteins from these viruses. Confocal laser scanning microscopy, as well as membrane flotation analyses, demonstrated that NS5As from G

SUBMITTER: Brass V 

PROVIDER: S-EPMC1866014 | biostudies-literature | 2007 Mar

REPOSITORIES: biostudies-literature