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Nucleic Acids Research 2005 33(3):977-986; doi:10.1093/nar/gki241
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Published online 17 February 2005

© The Author 2005. Published by Oxford University Press. All rights reserved
The online version of this article has been published under an open access model. Users are entitled to use, reproduce, disseminate, or display the open access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and Oxford University Press are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact journals.permissions{at}oupjournals.org

Article

HIV-1 integrase crosslinked oligomers are active in vitro

Aurélie Faure, Christina Calmels, Cécile Desjobert, Michel Castroviejo, Anne Caumont-Sarcos, Laura Tarrago-Litvak, Simon Litvak and Vincent Parissi*

CNRS UMR 5097, Université Victor Segalen Bordeaux 2, IFR 66 ‘Pathologies Infectieuses et Cancers’ 146 rue Léo Saignat, 33076 Bordeaux cedex, France

*To whom correspondence should be addressed at UMR 5097, CNRS-Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux cedex, France. Tel: +33 0 5 57 57 17 40; Fax: +33 0 5 57 57 17 66; Email: vincent.parissi{at}reger.u-bordeaux2.fr

Received September 14, 2004. Revised December 2, 2004. Accepted January 23, 2005.

The oligomeric state of active human immunodeficiency virus type 1 (HIV-1) integrase (IN) has not been clearly elucidated. We analyzed the activity of the different purified oligomeric forms of recombinant IN obtained after stabilization by platinum crosslinking. The crosslinked tetramer isolated by gel chromatography was able to catalyze the full-site integration of the two viral LTR ends into a target DNA in vitro, whereas the isolated dimeric form of the enzyme was involved in the processing and integration of only one viral end. Accurate concerted integration by IN tetramers was confirmed by cloning and sequencing. Kinetic studies of DNA-integrase complexes led us to propose a model explaining the formation of an active complex. Our data suggest that the tetrameric IN bound to the viral DNA ends is the minimal complex involved in the concerted integration of both LTRs and should be the oligomeric form targeted by future inhibitors.


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