Inhibition of HIV-1 protease in infected T-lymphocytes by synthetic peptide analogues View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-01

AUTHORS

Thomas D. Meek, Dennis M. Lambert, Geoffrey B. Dreyer, Thomas J. Carr, Thaddeus A. Tomaszek, Michael L. Moore, James E. Strickler, Christine Debouck, Lawrence J. Hyland, Thomas J. Matthews, Brian W. Metcalf, Stephen R. Petteway

ABSTRACT

THE gag and pol genes of the human immunodeficiency virus type 1 (HIV-1) (ref. 1) are translated as two polyproteins, Pr55gag and Prl60gag-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 (pi7, p24, p7 and p6)7–9and the pol-encoded enzymes essential for retrovirus replication (protease, reverse transcriptase, ribonuclease H, and endonuclease). Mutational inactivation of the proteases of HIV-110–13 and other retro viruses14,15results 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. More... »

PAGES

90-92

Journal

TITLE

Nature

ISSUE

6253

VOLUME

343

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/343090a0

    DOI

    http://dx.doi.org/10.1038/343090a0

    DIMENSIONS

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    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/1688646


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    29 schema:description THE gag and pol genes of the human immunodeficiency virus type 1 (HIV-1) (ref. 1) are translated as two polyproteins, Pr55gag and Prl60gag-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 (pi7, p24, p7 and p6)7–9and the pol-encoded enzymes essential for retrovirus replication (protease, reverse transcriptase, ribonuclease H, and endonuclease). Mutational inactivation of the proteases of HIV-110–13 and other retro viruses14,15results 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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