%0 Journal Article %A Baraz, Lea %A Hutoran, Marina %A Blumenzweig, Immanuel %A Katzenellenbogen, Mark %A Friedler, Assaf %A Gilon, Chaim %A Steinitz, Michael %A Kotler, Moshe %T Human immunodeficiency virus type 1 Vif binds the viral protease by interaction with its N-terminal region %D 2002 %J Journal of General Virology, %V 83 %N 9 %P 2225-2230 %@ 1465-2099 %R https://doi.org/10.1099/0022-1317-83-9-2225 %I Microbiology Society, %X 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. %U https://www.microbiologyresearch.org/content/journal/jgv/10.1099/0022-1317-83-9-2225