A disulfide-bonded dimer of the core protein of hepatitis C virus is important for virus-like particle production.

ABSTRACT: Hepatitis C virus (HCV) core protein forms the nucleocapsid of the HCV particle. Although many functions of core protein have been reported, how the HCV particle is assembled is not well understood. Here we show that the nucleocapsid-like particle of HCV is composed of a disulfide-bonded core protein complex (dbc-complex). We also found that the disulfide-bonded dimer of the core protein (dbd-core) is formed at the endoplasmic reticulum (ER), where the core protein is initially produced and processed. Mutational analysis revealed that the cysteine residue at amino acid position 128 (Cys128) of the core protein, a highly conserved residue among almost all reported isolates, is responsible for dbd-core formation and virus-like particle production but has no effect on the replication of the H

SUBMITTER: Kushima Y 

PROVIDER: S-EPMC2937620 | biostudies-literature | 2010 Sep

REPOSITORIES: biostudies-literature