Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues.
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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.
author list (cited authors)
Meek, T. D., Lambert, D. M., Dreyer, G. B., Carr, T. J., Tomaszek, T. A., Moore, M. L., ... Matthews, T. J.
complete list of authors
Meek, TD||Lambert, DM||Dreyer, GB||Carr, TJ||Tomaszek, TA||Moore, ML||Strickler, JE||Debouck, C||Hyland, LJ||Matthews, TJ