Proline-138 is essential for the assembly of hepatitis B virus core protein.
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.
Metzger
K
K
Department of Virology, University of Ulm, Germany.
Bringas
R
R
D000595:Amino Acid Sequence; D006512:Hepatitis B Core Antigens / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006515:Hepatitis B virus / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011392:Proline / Q000502:physiology*; D017510:Protein Folding; D017433:Protein Structure, Secondary; D014407:Tumor Cells, Cultured; D014758:Viral Core Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D006512:Hepatitis B Core Antigens; D014758:Viral Core Proteins; D011392:Proline