Human immunodeficiency virus has an aspartic-type protease that can be inhibited by pepstatin A.
The protease encoded by the human immunodeficiency virus (HIV) processes the viral gag and gag-pol protein precursor by posttranslational cleavage. In this study we have demonstrated by site-specific mutagenesis (Asp----Thr) and by pepstatin A inhibition that the recombinant HIV protease is an aspartic-type protease. Furthermore, incubation of HIV-infected H9 cells with pepstatin A inhibited part of the intracellular processing of the HIV gag protein yet had no apparent toxicity on HIV-infected cells during 48 hr of incubation.
D000818:Animals; D016282:Aspartic Acid Endopeptidases; D002460:Cell Line; D002729:Chloromercuribenzoates / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases; D006678:HIV / Q000201:enzymology*; D009842:Oligopeptides / Q000494:pharmacology*; D010436:Pepstatins / Q000494:pharmacology*; D011480:Protease Inhibitors; D020245:p-Chloromercuribenzoic Acid
D002729:Chloromercuribenzoates; D009842:Oligopeptides; D010436:Pepstatins; D011480:Protease Inhibitors; C014195:Streptomyces pepsin inhibitor; D020245:p-Chloromercuribenzoic Acid; D010450:Endopeptidases; D016282:Aspartic Acid Endopeptidases; C031375:pepstatin