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Originally published In Press as doi:10.1074/jbc.M103020200 on July 16, 2001

J. Biol. Chem., Vol. 276, Issue 38, 35435-35443, September 21, 2001
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The Hepatitis B Virus X Protein Induces HIV-1 Replication and Transcription in Synergy with T-cell Activation Signals
FUNCTIONAL ROLES OF NF-kappa B/NF-AT AND SP1-BINDING SITES IN THE HIV-1 LONG TERMINAL REPEAT PROMOTER*

Marta Gómez-Gonzaloabc, Marta Carreteroabd, Joaquín Rullasef, Enrique Lara-Pezziag, José Aramburuh, Benjamin Berkhouti, José Alcamíe, and Manuel López-Cabreraaj

From the a Unidad de Biología Molecular, Hospital Universitario de la Princesa, 28006 Madrid, Spain, the e Centro Nacional de Microbiología, Instituto de Salud Carlos III, 28029 Majadahonda-Madrid, Spain, the h Departament de Ciències Experimentals i de la Salut, Universitat Pompeu Fabra, 08003 Barcelona, Spain, and the i Department of Human Retrovirology, Academic Medical Center, University of Amsterdam, 1105 AZ Amsterdam, The Netherlands

Co-infection with hepatitis B virus (HBV) and human immunodeficiency virus type-1 (HIV-1) is relatively common. However, the impact of this co-infection on the clinical outcome of HIV infection has not been elucidated. We herein demonstrate that the HBV X protein (HBx) superinduces ongoing HIV-1 replication and HIV-1 long terminal repeat (LTR) transcription by synergizing with Tat protein and with T-cell activation signals. Although HBx cooperated with mitogenic stimuli in the induction of reporter plasmids harboring the HIV-1 kappa B enhancer, in both a NF-kappa B-dependent manner and a NF-AT-dependent manner, deletion of this element from the LTR did not affect the HBx-mediated up-regulation in the presence of Tat and/or mitogens. In contrast, mutation of the proximal LTR Sp1-binding sites abolished the HBx-mediated synergistic activation, but only when it was accompanied by deletion of the kappa B enhancer. When HBx was targeted to the nucleus, its ability to synergize with cellular activation stimuli was maintained. Furthermore, mutations of HBx affecting its interaction with the basal transcription machinery abrogated the synergistic activation by HBx, suggesting that this protein exerts its function by acting as a nuclear co-activator. These results indicate that HBx could contribute to a faster progression to AIDS in HBV-HIV co-infected individuals.

* This work was supported by Grant FIS 00/0602 from Ministerio de Sanidad y Consumo (to M. L. C.) and Grant SAF 00/0028 from Ministerio de Ciencia y Tecnología and Fundación Caja de Madrid (to J. A.).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.

b These authors contribute equally to this work.

c Supported by a fellowship from Ministerio de Educación y Cultura of Spain.

d Supported by FIS 00/0602.

f Supported by a fellowship from Fundación Para la Investigación y la Prevención del Sida en España.

g Supported by a fellowship from Comunidad Autónoma de Madrid.

j To whom correspondence should be addressed: Unidad de Biología Molecular, Hospital Universitario de la Princesa, C/Diego de León, 62, 28006 Madrid, Spain. Tel.: 34-91-5202334; Fax: 34-91-5202374; E-mail: mlopez@hlpr.insalud.es.

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