An Amphipathic α-Helix at the C Terminus of Hepatitis C Virus Nonstructural Protein 4B Mediates Membrane Association

Jérôme Gouttenoire(University Hospital of Lausanne), Roland Montserret(Université Claude Bernard Lyon 1), Audrey Kennel(University Hospital of Lausanne), François Pénin(Université Claude Bernard Lyon 1), Darius Moradpour(University Hospital of Lausanne)
Journal of Virology
August 20, 2009
Cited by 71Open Access
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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.


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