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In vitro assembly of feline immunodeficiency virus capsid protein: Biological role of conserved cysteines

  1. Author:
    Nath, M. D.
    Peterson, D. L.

  2. Author Address

    NCI, Frederick Canc Res & Dev Ctr, NIH, Bldg 567, Room 261, Frederick, MD 21702 USA. NCI, Frederick Canc Res & Dev Ctr, NIH, Frederick, MD 21702 USA. Virginia Commonwealth Univ, Dept Biochem & Mol Biophys, Richmond, VA 23298 USA. Nath MD NCI, Frederick Canc Res & Dev Ctr, NIH, Bldg 567, Room 261, Frederick, MD 21702 USA.
    1. Year: 2001
  2. Journal: Archives of Biochemistry and Biophysics
    1. 392
    2. 2
    3. Pages: 287-294
  4. Type of Article: Article
  1. Abstract:

    Core assembly, a key step in the retroviral life cycle, is poorly understood. Previous studies have shown that the entire gag region is needed to form the assembled particles. In this report, we have shown that the assembly process is driven by recombinant capsid protein (p26) of feline immunodeficiency virus itself. Proteins are expressed in a bacterial system and soluble forms of wild-type and modified proteins are purified from bacterial extracts and are examined on gel-filtration chromatography fitted to an HPLC system. It has also been shown that changing residue Cys190 (one of the two conserved cysteines of feline immunodeficiency virus which are also conserved for all the immunodeficiency viruses including HM to serine by site-directed mutagenesis disrupts the assembly process. In addition, this modification causes considerable thermal instability of the protein while substitutions at nonconserved cysteines do not significantly affect the thermal stability and assembly of the protein. These findings indicate that conserved cysteine residues play a vital role in the capsid protein assembly and, therefore, are critical for virus infectivity. (C) 2001 Academic Press.

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