Abstract |
The vif gene, one of the six auxiliary genes of human immunodeficiency virus (HIV), is essential for virus propagation in peripheral blood lymphocytes and macrophages and in certain T-cell lines. Previously, it was demonstrated that Vif inhibits the autoprocessing of truncated HIV type 1 (HIV-1) Gag- Pol polyproteins expressed in bacterial cells, as well as the protease-mediated cleavage of synthetic peptides in vitro. Peptides derived from the aa 78-98 region in the Vif molecule specifically inhibit and bind the HIV-1 protease in vitro and arrest the production of infectious viruses in HIV-1-infected cells. This study demonstrates that (i) purified recombinant Vif protein and HIV-1 but not avian sarcoma leukaemia virus protease specifically bind each other and (ii) the interaction between these two proteins takes place at the N terminus of the protease (aa 1-9) and the central part of Vif (aa 78-98). The data presented in this report suggest a model in which Vif interacts with the dimerization sites of the viral protease.
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Authors | Lea Baraz, Marina Hutoran, Immanuel Blumenzweig, Mark Katzenellenbogen, Assaf Friedler, Chaim Gilon, Michael Steinitz, Moshe Kotler |
Journal | The Journal of general virology
(J Gen Virol)
Vol. 83
Issue Pt 9
Pg. 2225-2230
(Sep 2002)
ISSN: 0022-1317 [Print] England |
PMID | 12185277
(Publication Type: Journal Article, Research Support, Non-U.S. Gov't)
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Chemical References |
- Gene Products, vif
- HIV Protease Inhibitors
- Peptide Fragments
- Recombinant Proteins
- vif Gene Products, Human Immunodeficiency Virus
- HIV Protease
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Topics |
- Binding Sites
- Dimerization
- Dose-Response Relationship, Drug
- Gene Products, vif
(biosynthesis, genetics, metabolism)
- HIV Protease
(chemistry, genetics, metabolism)
- HIV Protease Inhibitors
(chemical synthesis, pharmacology)
- HIV-1
(metabolism)
- Peptide Fragments
(chemical synthesis, pharmacology)
- Protein Binding
- Recombinant Proteins
(metabolism)
- Virus Replication
- vif Gene Products, Human Immunodeficiency Virus
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