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J Virol, May 1998, p. 3512-3519, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Neutralization of Human Immunodeficiency Virus Type 1 by Antibody to gp120 Is Determined Primarily by Occupancy of Sites on the Virion Irrespective of Epitope Specificity

Paul W. H. I. Parren,1 Isabelle Mondor,2 Denise Naniche,3 Henrik J. Ditzel,1 P. J. Klasse,4 Dennis R. Burton,1,* and Quentin J. Sattentau2,*

Departments of Immunology and Molecular Biology1 and Division of Virology,3 The Scripps Research Institute, La Jolla, California 92037; Centre d'Immunologie de Marseille-Luminy, 13288 Marseille, France2; and The MRC Laboratory for Molecular Cell Biology, University College London, London WC1E 6BT, United Kingdom4

Received 2 September 1997/Accepted 12 January 1998

We investigated the relative importance of binding site occupancy and epitope specificity in antibody neutralization of human immunodeficiency virus (HIV) type 1 (HIV-1). The neutralization of a T-cell-line-adapted HIV-1 isolate (MN) was analyzed with a number of monovalent recombinant Fab fragments (Fabs) and monoclonal antibodies with a range of specificities covering all confirmed gp120-specific neutralization epitopes. Binding of Fabs to recombinant monomeric gp120 was determined by surface plasmon resonance, and binding of Fabs and whole antibodies to functional oligomeric gp120 was determined by indirect immunofluorescence and flow cytometry on HIV-infected cells. An excellent correlation between neutralization and oligomeric gp120 binding was observed, and a lack of correlation with monomeric gp120 binding was confirmed. A similar degree of correlation was observed between oligomeric gp120 binding and neutralization with a T-cell-line-adapted HIV-1 molecular clone (Hx10). The ratios of oligomer binding/neutralization titer fell, in general, within a relatively narrow range for antibodies to different neutralization epitopes. These results suggest that the occupancy of binding sites on HIV-1 virions is the major factor in determining neutralization, irrespective of epitope specificity. Models to account for these observations are proposed.

* Corresponding author. Mailing address for Dennis R. Burton: Department of Immunology, IMM2, The Scripps Research Institute, 10550 N. Torrey Pines Rd., La Jolla, CA 92037. Phone: (619) 784-9298. Fax: (619) 784-8360. E-mail: burton{at}scripps.edu. Mailing address for Quentin J. Sattentau: Centre d'Immunologie de Marseille-Luminy, Case 906, 13288 Marseille Cedex 9, France. Phone: (33) 4 491 26 94 94. Fax: (33) 4 491 26 94 30. E-mail: sattenta{at}ciml.univ-mrs.fr.

J Virol, May 1998, p. 3512-3519, Vol. 72, No. 5
0022-538X/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


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