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Originally published In Press as doi:10.1074/jbc.M009029200 on March 16, 2001

J. Biol. Chem., Vol. 276, Issue 21, 18102-18107, May 25, 2001
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Characterization of the Nuclear Import Pathway for HIV-1 Integrase*

Christel DepienneDagger §, Aurélie MousnierDagger , Hervé Leh, Erwann Le Rouzic||, Dominique Dormont§, Serge Benichou||, and Catherine DargemontDagger **

From the Dagger  Institut Jacques Monod, Unité Mixte de Recherche 7592, CNRS, Université Paris VI, Université Paris VII, Paris 75251, France, § Commissariat à l'Energie Atomique (Saclay, France), Service de Neurovirologie, Fontenay aux Roses 92265, France,  Unité Mixte de Recherche 8532, Institut Gustave Roussy, Villejuif 94805, France, and || INSERM U529, Institut Cochin de Génétique Moléculaire, Paris 75014, France

The karyophilic properties of the human immunodeficiency virus, type I (HIV-1) pre-integration complex (PIC) allow the virus to infect non-dividing cells. To better understand the mechanisms responsible for nuclear translocation of the PIC, we investigated nuclear import of HIV-1 integrase (IN), a PIC-associated viral enzyme involved in the integration of the viral genome in the host cell DNA. Accumulation of HIV-1 IN into nuclei of digitonin-permeabilized cells does not result from passive diffusion but rather from an active transport that occurs through the nuclear pore complexes. HIV-1 IN is imported by a saturable mechanism, implying that a limiting cellular factor is responsible for this process. Although IN has been previously proposed to contain classical basic nuclear localization signals, we found that nuclear accumulation of IN does not involve karyopherins alpha , beta 1, and beta 2-mediated pathways. Neither the non-hydrolyzable GTP analog, guanosine 5'-O-(thiotriphosphate), nor the GTP hydrolysis-deficient Ran mutant, RanQ69L, significantly affects nuclear import of IN, which depends instead on ATP hydrolysis. Therefore these results support the idea that IN import is not mediated by members of the karyopherin beta  family. More generally, in vitro nuclear import of IN does not require addition of cytosolic factors, suggesting that cellular factor(s) involved in this active but atypical pathway process probably remain associated with the nuclear compartment or the nuclear pore complexes from permeabilized cells.

* This work was supported by grants from the Agence Nationale de Recherche contre le Syndrome d'ImmunoDeficience Acquise, the Fondation pour la Recherche Médicale, and 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.

** To whom correspondence should be addressed: Equipe de Transport Nucléocytoplasmique-Institut Jacques Monod, UMR 7592-2, Place Jussieu-Tour 43-75251 Paris Cedex 05, France. Tel./Fax: 33 1 44276956; E-mail: dargemont@ijm.jussieu.fr.

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