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 Blood, 1 April 2005, Vol. 105, No. 7, pp. 2802-2811.
Prepublished online as a Blood First Edition Paper on December 9, 2004; DOI 10.1182/blood-2004-06-2212.

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IMMUNOBIOLOGY

Cell surface–associated Tat modulates HIV-1 infection and spreading through a specific interaction with gp120 viral envelope protein

Serena Marchiò, Massimo Alfano, Luca Primo, Daniela Gramaglia, Luca Butini, Luisa Gennero, Enrico De Vivo, Wadih Arap, Mauro Giacca, Renata Pasqualini, and Federico Bussolino

From the Division of Molecular Angiogenesis and Division of Molecular Oncology, Department of Oncological Sciences, University of Turin Medical School, Institute for Cancer Research and Treatment, Candiolo, Italy; Creabilis Therapeutics, Colleretto Giacosa, Italy; AIDS Immunopathogenesis Unit, Department of Immunology and Infectious Diseases, San Raffaele Scientific Institute, Milan, Italy; Service of Clinical Immunology, Department of Internal Medicine, Marche Polytechnic University School of Medicine and Ancona General Hospital, Torrette di Ancona, Italy; Division of Infectious Diseases, Amedeo di Savoia Hospital, Turin, Italy; Service for Drug Addictions, Turin, Italy; The University of Texas MD Anderson Cancer Center, Houston, TX; and Molecular Medicine Laboratory, International Center for Genetic Engineering and Biotechnology, Trieste, Italy.

Human immunodeficiency virus-1 (HIV-1) Tat, a nuclear transactivator of viral gene expression, has the unusual property of being released by infected cells. Recent studies suggest that extracellular Tat is partially sequestered by heparan sulfate proteoglycans. As a consequence, Tat is concentrated on the cell surface and protected from proteolytic degradation, thus remaining in a biologically active form. We show that Tat binds the surfaces of both HIV-1–infected and surrounding uninfected cells. We provide evidence for a specific interaction between Tat and the HIV-1 glycoprotein 120 (gp120) envelope protein, which enhances virus attachment and entry into cells. We map the interacting sites of both Tat and gp120 and show that synthetic peptides mimicking the gp120 site inhibit HIV-1 infection. Our data demonstrate that membrane-associated Tat is a novel modulator of virus entry and suggest that the Tat-gp120 interaction represents a critical step in HIV-1 spreading during the course of infection.


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