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  • Title: Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues.
    Author: Meek TD, Lambert DM, Dreyer GB, Carr TJ, Tomaszek TA, Moore ML, Strickler JE, Debouck C, Hyland LJ, Matthews TJ.
    Journal: Nature; 1990 Jan 04; 343(6253):90-2. PubMed ID: 1688646.
    Abstract:
    The gag and pol genes of the human immunodeficiency virus type 1 (HIV-1) (ref. 1) are translated as two polyproteins, Pr55gag and Pr160gag-pol (refs 2-6), which are subsequently cleaved by the action of a virus-encoded protease into the four structural gag proteins of the virion core (p17, p24, p7 and p6) and the pol-encoded enzymes essential for retrovirus replication (protease, reverse transcriptase, ribonuclease H, and endonuclease). Mutational inactivation of the proteases of HIV-1 and other retroviruses results in immature, non-infectious virions, indicating that exogenous inhibition of the protease may represent an attractive approach to anti-AIDS therapy. Here we demonstrate that synthetic peptide analogues, which are potent inhibitors of purified HIV-1 protease, inhibit the processing of the viral polyproteins in cultures of HIV-1-infected T lymphocytes and attenuate viral infectivity.
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