Proline-138 is essential for the assembly of hepatitis B virus core protein

J Gen Virol. 1998 Mar:79 ( Pt 3):587-90. doi: 10.1099/0022-1317-79-3-587.

Abstract

In small RNA viruses, arm-like segments located at the N or C termini have been suggested as mediators in the assembly of the capsid proteins. In many cases the arms of several subunits converge at a common point (the symmetry axis). Recent advances in studies of the hepatitis B virus (HBV) core protein attest the convergence of the segments preceding the protamine region, around the symmetry axis, where five or six HBc protein subunits converge. We report a mutation study of the region that we have suggested forms an arm-like structure, which reveals that a single mutation, Pro-138 --> Gly, prevents the full-length HBV core protein self-assembling into particles.

MeSH terms

  • Amino Acid Sequence
  • Hepatitis B Core Antigens / chemistry*
  • Hepatitis B Core Antigens / genetics
  • Hepatitis B Core Antigens / metabolism
  • Hepatitis B virus / chemistry*
  • Hepatitis B virus / genetics
  • Hepatitis B virus / metabolism
  • Humans
  • Molecular Sequence Data
  • Mutagenesis
  • Proline / physiology*
  • Protein Folding
  • Protein Structure, Secondary
  • Tumor Cells, Cultured
  • Viral Core Proteins / chemistry*
  • Viral Core Proteins / genetics
  • Viral Core Proteins / metabolism

Substances

  • Hepatitis B Core Antigens
  • Viral Core Proteins
  • Proline