An amphipathic alpha-helix at the C terminus of hepatitis C virus nonstructural protein 4B mediates membrane association

J Virol. 2009 Nov;83(21):11378-84. doi: 10.1128/JVI.01122-09. Epub 2009 Aug 19.

Abstract

Nonstructural protein 4B (NS4B) plays an essential role in the formation of the hepatitis C virus (HCV) replication complex. It is an integral membrane protein that has been only poorly characterized to date. It is believed to comprise a cytosolic N-terminal part, a central part harboring four transmembrane passages, and a cytosolic C-terminal part. Here, we describe an amphipathic alpha-helix at the C terminus of NS4B (amino acid residues 229 to 253) that mediates membrane association and is involved in the formation of a functional HCV replication complex.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Cell Line
  • Hepacivirus / metabolism*
  • Humans
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Structure, Secondary*
  • Protein Structure, Tertiary
  • Recombinant Fusion Proteins / chemistry
  • Recombinant Fusion Proteins / genetics
  • Recombinant Fusion Proteins / metabolism
  • Sequence Alignment
  • Viral Nonstructural Proteins / chemistry*
  • Viral Nonstructural Proteins / genetics
  • Viral Nonstructural Proteins / metabolism
  • Virus Internalization*
  • Virus Replication

Substances

  • Recombinant Fusion Proteins
  • Viral Nonstructural Proteins