title: The N-terminal half of the core protein of hepatitis C virus is sufficient for nucleocapsid formation.
abstract: The core (C) protein of hepatitis C virus (HCV) appears to be a multifunctional protein that is involved in many viral and cellular processes. Although its effects on host cells have been extensively discussed in the literature, little is known about its main function, the assembly and packaging of the viral genome. We have studied the in vitro assembly of several deleted versions of recombinant HCV C protein expressed in E. coli. We demonstrated that the 75 N-terminal residues of the C protein were sufficient to assemble and generate nucleocapsid-like particles (NLPs) in vitro. However, homogeneous particles of regular size and shape were observed only when NLPs were produced from at least the first 79 N-terminal amino acids of the C protein. This small protein unit fused to the endoplasmic reticulum-anchoring domain also generated NLPs in yeast cells. These data suggest that the N-terminal half of the C protein is important for formation of NLPs. Similarities between the HCV C protein and C proteins of other members of the Flaviviridae are discussed.
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Nathalie
authors.initials: N
authors.lastname: Majeau
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Valérie
authors.initials: V
authors.lastname: Gagné
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Annie
authors.initials: A
authors.lastname: Boivin
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Marilène
authors.initials: M
authors.lastname: Bolduc
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Josée-Anne
authors.initials: JA
authors.lastname: Majeau
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Dominique
authors.initials: D
authors.lastname: Ouellet
authors.affiliation: Centre de Recherche en Infectiologie, Pav. CHUL, U. Laval, 2705 boul. Laurier, Québec (Québec), Canada G1V 4G2.
authors.forename: Denis
authors.initials: D
authors.lastname: Leclerc
mesh_terms: D000595:Amino Acid Sequence; D001483:Base Sequence; D004279:DNA, Viral / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics; D016174:Hepacivirus / Q000235:genetics / Q000502:physiology*; D066298:In Vitro Techniques; D008854:Microscopy, Electron; D008954:Models, Biological; D008969:Molecular Sequence Data; D019251:Nucleocapsid / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D010446:Peptide Fragments / Q000737:chemistry / Q000235:genetics / Q000502:physiology; D010843:Pichia / Q000235:genetics; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014758:Viral Core Proteins / Q000737:chemistry / Q000235:genetics / Q000502:physiology*; D019065:Virus Assembly
chemical_list: D004279:DNA, Viral; D010446:Peptide Fragments; D011994:Recombinant Proteins; D014758:Viral Core Proteins