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Human immunodeficiency virus type 1 Vif binds the viral protease by interaction with its N-terminal region

Experimental Pathology, The Hebrew University-Hadassah Medical School, Jerusalem 91120, Israel¹
Department of Organic Chemistry, The Hebrew University, Givat Ram, Jerusalem 91904, Israel²

Author for correspondence: Moshe Kotler. Fax +972 2 6758190. e-mail mkotler{at}cc.huji.ac.il

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.