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Inhibition of the maturation of HIV structural proteins by a renin peptide inhibitor.

Marchetto S, Nisato D, Chermann JC; International Conference on AIDS.

Int Conf AIDS. 1989 Jun 4-9; 5: 627 (abstract no. Th.C.P.66).

Unite de Recherches INSERM sur les Retrovirus et Maladies Associees (U.322) - Campus de Luminy - BP 33 - 13273 Marseille Cedex 9 - France

The protease encoded by the Human Immunodeficiency Virus (HIV) pol gene cleaves the gag-pol protein precursors and plays an important role in the viral replication cycle of HIV. The HIV protease belongs to the family of aspartyl-proteases, as pepsin or renin, and can be inhibited by specific inhibitors. Fourteen synthetic peptides known to be inhibitors of renin were tested; one of them showed an inhibition of the cytopathic effect of HIV on MT4 cells. This peptide also inhibited viral production by the CEM cell line, since no reverse transcriptase activity was detected and no viral antigen was revealed by immunofluorescence during several weeks after infection by HIV. Nevertheless, when the inhibitor peptide was removed from the culture, infectious virus particles were produced after a few days. These results demonstrate that specific inhibitors of proteases can block "in vitro" infections by HIV and provide possible strategies against AIDS.

Publication Types:
  • Meeting Abstracts
Keywords:
  • AIDS Vaccines
  • Aspartic Endopeptidases
  • Cell Line
  • Chymosin
  • Endopeptidases
  • Genes, gag
  • Genes, pol
  • HIV Protease
  • HIV Protease Inhibitors
  • Humans
  • In Vitro
  • Peptides
  • RNA-Directed DNA Polymerase
  • Renin
  • genetics
Other ID:
  • 00331889
UI: 102179221

From Meeting Abstracts




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