HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteins

Biochem Biophys Res Commun. 1988 Oct 14;156(1):297-303. doi: 10.1016/s0006-291x(88)80839-8.


The mature proteins of retroviruses originate as a result of proteolytic cleavages of polyprotein precursors. Retroviruses encode proteases responsible for several of these processing events, making them potential antiviral drug targets. A 99-amino acid HIV-1 protease, produced by chemical synthesis or by expression in bacteria, is shown here to hydrolyze peptides corresponding to all of the known cleavage sites in the HIV-1 gag and pol polyproteins. It does not hydrolyze peptides corresponding to an env cleavage site or a distantly related retroviral gag cleavage site.

MeSH terms

  • Amino Acid Sequence
  • Antigens, Viral
  • Gene Products, gag
  • HIV-1 / enzymology*
  • HIV-1 / genetics
  • Hydrolysis
  • Kinetics
  • Peptide Hydrolases / chemical synthesis
  • Peptide Hydrolases / genetics
  • Peptide Hydrolases / metabolism*
  • Retroviridae Proteins / metabolism*
  • Substrate Specificity


  • Antigens, Viral
  • Gene Products, gag
  • Retroviridae Proteins
  • Peptide Hydrolases