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J Virol, March 1998, p. 2500-2504, Vol. 72, No. 3
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Human Immunodeficiency Virus (HIV) Envelope Binds to CXCR4 Independently of CD4, and Binding Can Be Enhanced by Interaction with Soluble CD4 or by HIV Envelope Deglycosylation

Juan C. Bandres,1,2,3,* Qing F. Wang,1 Jeanne O'Leary,1 Françoise Baleaux,4 Ali Amara,4 James A. Hoxie,5 Susan Zolla-Pazner,1,2 and Miroslaw K. Gorny1,2

Research Center for AIDS and HIV Infection, Manhattan VA Medical Center,1 and Departments of Pathology2 and Medicine,3 New York University, New York, New York 10010; Unite d'Immunologie Virale, Institut Pasteur, 75724 Paris Cedex 15, France4; and Hematology-Oncology Division, University of Pennsylvania, Philadelphia, Pennsylvania 191045

Received 23 July 1997/Accepted 20 November 1997

Chemokine receptor CXCR4 (also known as LESTR and fusin) has been shown to function as a coreceptor for T-cell-tropic strains of human immunodeficiency virus type 1 (HIV-1). We have developed a binding assay to show that HIV envelope (Env) can interact with CXCR4 independently of CD4 but that this binding is markedly enhanced by the previous interaction of Env with soluble CD4. We also show that nonglycosylated HIV-1SF-2 gp120 or sodium metaperiodate-treated oligomeric gp160 from HIV-1451 bound much more readily to CXCR4 than their counterparts with intact carbohydrate residues did.

* Corresponding author. Mailing address: Manhattan VA Medical Center, 423 23 St., Room 18125N, New York, NY 10010. Phone: (212) 263-6769. Fax: (212) 951-6321. E-mail: bandrj01{at}mcrcr.med.nyu.edu.




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