CD4-Induced Conformational Changes in the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein: Consequences for Virus Entry and Neutralization

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J Virol, June 1998, p. 4694-4703, Vol. 72, No. 6
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

CD4-Induced Conformational Changes in the Human Immunodeficiency Virus Type 1 gp120 Glycoprotein: Consequences for Virus Entry and Neutralization

Nancy Sullivan,¹^,² Ying Sun,¹ Quentin Sattentau,³ Markus Thali,¹ Dona Wu,¹ Galina Denisova,⁴ Jonathan Gershoni,⁴ James Robinson,⁵ John Moore,⁶ and Joseph Sodroski¹^,²^,^*

Division of Human Retrovirology, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School,¹ and Department of Cancer Biology, Harvard School of Public Health,² Boston, Massachusetts 02115; Centre d'Immunologie de Marseille-Luminy, 13288 Marseille Cedex 9, France³; Department of Cell Research and Immunology, George S. Wise Faculty of Life Sciences, Tel Aviv University, Tel Aviv, Israel 69978⁴; Department of Pediatrics, Tulane University Medical Center, New Orleans, Louisiana 70112⁵; and Aaron Diamond AIDS Research Center, Rockefeller University, New York, New York 10016⁶

Received 11 December 1997/Accepted 3 March 1998

Human immunodeficiency virus type 1 (HIV-1) entry into target cells involves sequential binding of the gp120 exterior envelopeglycoprotein to CD4 and to specific chemokine receptors. SolubleCD4 (sCD4) is thought to mimic membrane-anchored CD4, and itsbinding alters the conformation of the HIV-1 envelope glycoproteins.Two cross-competing monoclonal antibodies, 17b and CG10, thatrecognize CD4-inducible gp120 epitopes and that block gp120-chemokinereceptor binding were used to investigate the nature and functionalsignificance of gp120 conformational changes initiated by CD4binding. Envelope glycoproteins derived from both T-cell line-adaptedand primary HIV-1 isolates exhibited increased binding of the17b antibody in the presence of sCD4. CD4-induced exposure ofthe 17b epitope on the oligomeric envelope glycoprotein complexoccurred over a wide range of temperatures and involved movementof the gp120 V1/V2 variable loops. Amino acid changes that reducedthe efficiency of 17b epitope exposure following CD4 binding invariablycompromised the ability of the HIV-1 envelope glycoproteins toform syncytia or to support virus entry. Comparison of the CD4dependence and neutralization efficiencies of the 17b and CG10antibodies suggested that the epitopes for these antibodies areminimally accessible following attachment of gp120 to cell surfaceCD4. These results underscore the functional importance of theseCD4-induced changes in gp120 conformation and illustrate viralstrategies for sequestering chemokine receptor-binding regionsfrom the humoral immune response.

^* Corresponding author. Mailing address: Dana-Farber Cancer Institute, JFB824, 44 Binney St., Boston, MA 02115. Phone: (617)632-3371. Fax: (617) 632-4338. E-mail: Joseph_Sodroski{at}dfci.harvard.edu.

J Virol, June 1998, p. 4694-4703, Vol. 72, No. 6
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

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