Hepatitis B virus core protein dimer‑dimer interface is critical for viral replication.

ABSTRACT: Hepatitis B virus (HBV) core protein (HBc) serves pivotal roles in the viral life cycle, particularly serving as the basic unit for capsid assembly, and is closely associated with HBV genome replication and progeny virion production. Previous studies have demonstrated that HBc has at least two functional interfaces; two HBc monomers form a homodimer via an intradimer interface, and then 90 or 120 homodimers form an icosahedral capsid via a dimer‑dimer interface. In the present study, the role of the HBc dimer‑dimer interface in HBV replication was investigated. A panel of residues located at the dimer‑dimer interface were identified based on the crystal structure of HBc. Native gel electrophoresis and western blotting revealed that, despite mutations in the dimer‑dimer interface, HBc forme

SUBMITTER: Zheng CL 

PROVIDER: S-EPMC6297743 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature