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Originally published In Press as doi:10.1074/jbc.M207439200 on September 12, 2002

J. Biol. Chem., Vol. 277, Issue 47, 45091-45098, November 22, 2002
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Docking of HIV-1 Vpr to the Nuclear Envelope Is Mediated by the Interaction with the Nucleoporin hCG1*

Erwann Le RouzicDagger §, Aurélie Mousnier, Cecilia Rustum||**, Françoise StutzDagger Dagger , Einar Hallberg**, Catherine Dargemont, and Serge BenichouDagger §§

From the Dagger  Institut Cochin, Department of Infectious Diseases, CNRS UMR8104, INSERM U567, Université Paris 5, Paris, France, the  Institut Jacques Monod, CNRS UMR7592, Université Paris VI and Université Paris VII, Paris, France, || Södertörns Högskola, 141 89 Huddinge, Sweden, the Dagger Dagger  Institut de Microbiologie, Lausanne, Switzerland, and the ** Department of Neurochemistry and Neurotoxicology, Stockholm University, 106 91 Stockholm, Sweden

The HIV-1 genome contains several genes coding for auxiliary proteins, including the small Vpr protein. Vpr affects the integrity of the nuclear envelope and participates in the nuclear translocation of the preintegration complex containing the viral DNA. Here, we show by photobleaching experiments performed on living cells expressing a Vpr-green fluorescent protein fusion that the protein shuttles between the nucleus and the cytoplasm, but a significant fraction is concentrated at the nuclear envelope, supporting the hypothesis that Vpr interacts with components of the nuclear pore complex. An interaction between HIV-1 Vpr and the human nucleoporin CG1 (hCG1) was revealed in the yeast two-hybrid system, and then confirmed both in vitro and in transfected cells. This interaction does not involve the FG repeat domain of hCG1 but rather the N-terminal region of the protein. Using a nuclear import assay based on digitonin-permeabilized cells, we demonstrate that hCG1 participates in the docking of Vpr at the nuclear envelope. This association of Vpr with a component of the nuclear pore complex may contribute to the disruption of the nuclear envelope and to the nuclear import of the viral DNA.

* This work was supported in part by INSERM, CNRS, Université Paris 5, and the French Agency against AIDS.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 a fellowship from SIDACTION.

§§ To whom correspondence may be addressed: Serge Benichou, Dept. of Infectious Diseases, Institut Cochin, INSERM U567, Bâtiment Gustave Roussy, 27 rue du Faubourg Saint Jacques, 75014 Paris, France. Tel.: 33-1-40-51-65-78; Fax: 33-1-40-51-65-70; E-mail: benichou@cochin.inserm.fr.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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