Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues. Academic Article uri icon


  • 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.

published proceedings

  • Nature

altmetric score

  • 9

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.

citation count

  • 220

complete list of authors

  • Meek, TD||Lambert, DM||Dreyer, GB||Carr, TJ||Tomaszek, TA||Moore, ML||Strickler, JE||Debouck, C||Hyland, LJ||Matthews, TJ

publication date

  • January 1990

published in