The Structural Biology of Hepatitis B Virus: Form and Function

Annu Rev Virol. 2016 Sep 29;3(1):429-451. doi: 10.1146/annurev-virology-110615-042238. Epub 2016 Aug 1.

Abstract

Hepatitis B virus is one of the smallest human pathogens, encoded by a 3,200-bp genome with only four open reading frames. Yet the virus shows a remarkable diversity in structural features, often with the same proteins adopting several conformations. In part, this is the parsimony of viruses, where a minimal number of proteins perform a wide variety of functions. However, a more important theme is that weak interactions between components as well as components with multiple conformations that have similar stabilities lead to a highly dynamic system. In hepatitis B virus, this is manifested as a virion where the envelope proteins have multiple structures, the envelope-capsid interaction is irregular, and the capsid is a dynamic compartment that actively participates in metabolism of the encapsidated genome and carries regulated signals for intracellular trafficking.

Keywords: antiviral; capsid; icosahedral; nucleoprotein complex; reverse transcriptase; self-assembly.

Publication types

  • Review

MeSH terms

  • Capsid / metabolism
  • Capsid / ultrastructure*
  • Capsid Proteins / metabolism*
  • Genome, Viral / genetics
  • Hepatitis B / virology
  • Hepatitis B Core Antigens / metabolism*
  • Hepatitis B Core Antigens / ultrastructure
  • Hepatitis B e Antigens / metabolism*
  • Hepatitis B e Antigens / ultrastructure
  • Hepatitis B virus / genetics
  • Hepatitis B virus / ultrastructure*
  • Humans
  • Viral Envelope Proteins / metabolism*
  • Virus Assembly / physiology*

Substances

  • Capsid Proteins
  • Hepatitis B Core Antigens
  • Hepatitis B e Antigens
  • Viral Envelope Proteins