A Conserved HIV gp120 Glycoprotein Structure Involved in Chemokine Receptor Binding-Reference-Cited by-同舟云学术

A Conserved HIV gp120 Glycoprotein Structure Involved in Chemokine Receptor Binding

Published:1998-06-19 Issue:5371 Volume:280 Page:1949-1953
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Rizzuto Carlo D.¹²³,Wyatt Richard¹²³,Hernández-Ramos Nivia¹²³,Sun Ying¹²³,Kwong Peter D.¹²³,Hendrickson Wayne A.¹²³,Sodroski Joseph¹²³

Affiliation:

1. C. D. Rizzuto, R. Wyatt, N. Hernández-Ramos, Y. Sun, Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, Boston, MA 02115, USA.

2. P. D. Kwong and W. A. Hendrickson, Department of Biochemistry and Molecular Biophysics, Howard Hughes Medical Institute, Columbia University, New York, NY 10032, USA.

3. J. Sodroski, Department of Cancer Immunology and AIDS, Dana-Farber Cancer Institute, Department of Pathology, Harvard Medical School, and Department of Immunology and Infectious Diseases, Harvard School of Public Health, Boston, MA 02115, USA.

Abstract

The entry of primate immunodeficiency viruses into target cells depends on a sequential interaction of the gp120 envelope glycoprotein with the cellular receptors, CD4 and members of the chemokine receptor family. The gp120 third variable (V3) loop has been implicated in chemokine receptor binding, but the use of the CCR5 chemokine receptor by diverse primate immunodeficiency viruses suggests the involvement of an additional, conserved gp120 element. Through the use of gp120 mutants, a highly conserved gp120 structure was shown to be critical for CCR5 binding. This structure is located adjacent to the V3 loop and contains neutralization epitopes induced by CD4 binding. This conserved element may be a useful target for pharmacologic or prophylactic intervention in human immunodeficiency virus (HIV) infections.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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