HIV-1 protease specificity of peptide cleavage is sufficient for processing of gag and pol polyproteins.
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.
D000595:Amino Acid Sequence; D000956:Antigens, Viral; D015683:Gene Products, gag; D015497:HIV-1 / Q000201:enzymology* / Q000235:genetics; D006868:Hydrolysis; D007700:Kinetics; D010447:Peptide Hydrolases / Q000138:chemical synthesis / Q000235:genetics / Q000378:metabolism*; D012191:Retroviridae Proteins / Q000378:metabolism*; D013379:Substrate Specificity
D000956:Antigens, Viral; D015683:Gene Products, gag; D012191:Retroviridae Proteins; D010447:Peptide Hydrolases