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Journal of Virology, November 2002, p. 11091-11103, Vol. 76, No. 21
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.21.11091-11103.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Synergistic Activation of Human Immunodeficiency Virus Type 1 Promoter Activity by NF-{kappa}B and Inhibitors of Deacetylases: Potential Perspectives for the Development of Therapeutic Strategies

Vincent Quivy,1 Emmanuelle Adam,1 Yves Collette,2 Dominique Demonte,1 Alain Chariot,3 Caroline Vanhulle,1 Ben Berkhout,4 Rémy Castellano,2 Yvan de Launoit,5,6 Arsène Burny,1 Jacques Piette,3 Vincent Bours,3 and Carine Van Lint1*

Laboratoire de Virologie Moléculaire, Service de Chimie Biologique, Institut de Biologie et de Médecine Moléculaires, Université Libre de Bruxelles, 6041 Gosselies,1 Center for Molecular and Cellular Therapy, Université de Liège, Sart-Tilman, 4000 Liège,3 Laboratoire de Microbiologie, Faculté de Médecine, Université Libre de Bruxelles, 1070 Brussels, Belgium,5 Department of Human Retrovirology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands,4 INSERM U119, 13009 Marseille,2 Institut de Biologie de Lille, Institut Pasteur de Lille, UMR 8526 CNRS, 59021 Lille Cedex, France6

Received 18 March 2002/ Accepted 17 July 2002

The transcription factor NF-{kappa}B plays a central role in the human immunodeficiency virus type 1 (HIV-1) activation pathway. HIV-1 transcription is also regulated by protein acetylation, since treatment with deacetylase inhibitors such as trichostatin A (TSA) or sodium butyrate (NaBut) markedly induces HIV-1 transcriptional activity of the long terminal repeat (LTR) promoter. Here, we demonstrate that TSA (NaBut) synergized with both ectopically expressed p50/p65 and tumor necrosis factor alpha/SF2 (TNF)-induced NF-{kappa}B to activate the LTR. This was confirmed for LTRs from subtypes A through G of the HIV-1 major group, with a positive correlation between the number of {kappa}B sites present in the LTRs and the amplitude of the TNF-TSA synergism. Mechanistically, TSA (NaBut) delayed the cytoplasmic recovery of the inhibitory protein I{kappa}B{alpha}. This coincided with a prolonged intranuclear presence and DNA binding activity of NF-{kappa}B. The physiological relevance of the TNF-TSA (NaBut) synergism was shown on HIV-1 replication in both acutely and latently HIV-infected cell lines. Therefore, our results open new therapeutic strategies aimed at decreasing or eliminating the pool of latently HIV-infected reservoirs by forcing viral expression.

* Corresponding author. Mailing address: Université Libre de Bruxelles, Institut de Biologie et de Médecine Moléculaires, Service de Chimie Biologique, Laboratoire de Virologie Moléculaire, Rue des Profs Jeener et Brachet, 12, 6041 Gosselies, Belgium. Phone: 32-2-650 9807. Fax: 32-2-650 9800. E-mail: cvlint{at}ulb.ac.be.

Journal of Virology, November 2002, p. 11091-11103, Vol. 76, No. 21
0022-538X/02/$04.00+0     DOI: 10.1128/JVI.76.21.11091-11103.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.



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