Amphipathic helix-dependent localization of NS5A mediates hepatitis C virus RNA replication

  • J Virol. 2003 May;77(10):6055-61. doi: 10.1128/jvi.77.10.6055-6061.2003.
Menashe Elazar  1 ,  Kwang Ho Cheong ,  Ping Liu ,  Harry B Greenberg ,  Charles M Rice ,  Jeffrey S Glenn
Affiliations
  • 1. Division of Gastroenterology and Hepatology, Stanford University School of Medicine, Palo Alto, California 94305, USA.
PMID: 12719597 DOI: 10.1128/jvi.77.10.6055-6061.2003
Abstract

We identified an N-terminal amphipathic helix (AH) in one of hepatitis C virus (HCV)'s nonstructural proteins, NS5A. This AH is necessary and sufficient for membrane localization and is conserved across isolates. Genetically disrupting the AH impairs HCV replication. Moreover, an AH peptide-mimic inhibits the membrane association of NS5A in a dose-dependent manner. These results have exciting implications for the HCV life cycle and novel Antiviral strategies.

Products
  • Cat. No.
    Product Name
    Description
    Target
    Research Area
  • HY-P5366
    PEP1
    99.88%, α-helical peptide
    target: Liposome
    Research Areas: Others