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Originally published In Press as doi:10.1074/jbc.M009076200 on February 27, 2001

J. Biol. Chem., Vol. 276, Issue 20, 16885-16893, May 18, 2001
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The Tyrosine Kinase Hck Is an Inhibitor of HIV-1 Replication Counteracted by the Viral Vif Protein*

Ghérici Hassaïne§, Marianne Courcoul, Gilles Bessou, Yves Barthalay, Christophe Picard**, Daniel Olive, Yves Collette, Robert VigneDagger Dagger , and Etienne Decroly§§¶¶

§ INSERM Unit 372, Université de la Méditerranée, 163 Avenue de Luminy, 13276 Marseilles Cedex 09, France,  INSERM Unit 119, Institut Paoli-Calmettes, Université de la Méditerranée, 27 Boulevard Lei Roure, 13009 Marseilles, France, and §§ LCPMI, Free University of Brussels, Boulevard du Triomphe, 1050 Brussels, Belgium

The virus infectivity factor (Vif) protein facilitates the replication of human immunodeficiency virus type 1 (HIV-1) in primary lymphocytes and macrophages. Its action is strongly dependent on the cellular environment, and it has been proposed that the Vif protein counteracts cellular activities that would otherwise limit HIV-1 replication. Using a glutathione S-transferase pull-down assay, we identified that Vif binds specifically to the Src homology 3 domain of Hck, a tyrosine kinase from the Src family. The interaction between Vif and the full-length Hck was further assessed by co-precipitation assays in vitro and in human cells. The Vif protein repressed the kinase activity of Hck and was not itself a substrate for Hck phosphorylation. Within one single replication cycle of HIV-1, Hck was able to inhibit the production and the infectivity of vif-deleted virus but not that of wild-type virus. Accordingly, HIV-1 vif - replication was delayed in Jurkat T cell clones stably expressing Hck. Our data demonstrate that Hck controls negatively HIV-1 replication and that this inhibition is suppressed by the expression of Vif. Hck, which is present in monocyte-macrophage cells, represents the first identified cellular inhibitor of HIV-1 replication overcome by Vif.

* This work was supported in part by the following French institutes: INSERM (Dotation Globale INSERM), Agence Nationale de Recherche sur le SIDA (ANRS), and Ensemble contre le Sida (Sidaction).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by Sidaction.

These two authors contributed equally to this work.

** Supported by ANRS.

Dagger Dagger To whom correspondence may be addressed. Tel.: 33-4-91-82-75-83; Fax: 33-4-91-82-60-61; E-mail: rvigne@inserm-u372.univ-mrs.fr.

¶¶ Supported by the Fondation Nationale de la Recherche Scientifique (Belgium). To whom correspondence may be addressed. Tel.: 33-4-91-82-75-83; Fax: 33-4-91-82-60-61; E-mail: edecroly@ulb.ac.be.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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