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

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

P L Darke  1 , R F Nutt, S F Brady, V M Garsky, T M Ciccarone, C T Leu, P K Lumma, R M Freidinger, D F Veber, I S Sigal
Affiliations

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

P L Darke et al. Biochem Biophys Res Commun. .

Abstract

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.

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