title: Interaction with membranes of the full C-terminal domain of protein NS4B from hepatitis C virus.
abstract: Hepatitis C virus (HCV) NS4B protein is a transmembrane highly hydrophobic protein responsible for many key aspects of the viral replication process. The C-terminal part of NS4B is essential for replication and is a potential target for HCV replication inhibitors. In this work we have carried out a study of the binding to and interaction with model biomembranes of a peptide corresponding to the C-terminal domain of NS4B, NS4B(Cter). We show that NS4B(Cter) partitions into phospholipid membranes, is capable of rupturing membranes even at very low peptide-to-lipid ratios and its membrane-activity is modulated by lipid composition. NS4B(Cter) is located in a shallow position in the membrane but it is able to affect the lipid environment from the membrane surface down to the hydrophobic core. Our results identify the C-terminal region of the HCV NS4B protein as a membrane interacting domain, and therefore directly implicated in the HCV life cycle and possibly in the formation of the membranous web.
authors: Universidad Miguel Hernandez, Eliche-Alicante, Spain.
authors: M Francisca
authors: MF
authors: Palomares-Jerez
authors: Henrique
authors: H
authors: Nemesio
authors: José
authors: J
authors: Villalaín
mesh_terms: D000595:Amino Acid Sequence; D002152:Calorimetry, Differential Scanning; D002462:Cell Membrane / Q000378:metabolism; D016174:Hepacivirus / Q000378:metabolism*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D013055:Spectrophotometry, Infrared; D017361:Viral Nonstructural Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: C080107:NS4B protein, flavivirus; D017361:Viral Nonstructural Proteins