Ontology highlight
ABSTRACT:
SUBMITTER: Lange CM
PROVIDER: S-EPMC4093864 | biostudies-literature | 2014 Jun
REPOSITORIES: biostudies-literature
Lange Christian M CM Bellecave Pantxika P Dao Thi Viet Loan VL Tran Huong T L HT Penin François F Moradpour Darius D Gouttenoire Jérôme J
Journal of virology 20140319 11
Hepatitis C virus (HCV) nonstructural protein 2 (NS2) is required for HCV polyprotein processing and particle assembly. It comprises an N-terminal membrane domain and a C-terminal, cytosolically oriented protease domain. Here, we demonstrate that the NS2 protease domain itself associates with cellular membranes. A single charged residue in the second α-helix of the NS2 protease domain is required for proper membrane association, NS2 protein stability, and efficient HCV polyprotein processing. ...[more]