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Structure of an hiv gp120 envelope glycoprotein in complex with the cd4 receptor and a neutralizing human antibody

Academic Article
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Overview

authors

  • Kwong, P. D.
  • Wyatt, Richard
  • Robinson, J.
  • Sweet, R. W.
  • Sodroski, J.
  • Hendrickson, W. A.

publication date

  • June 1998

journal

  • Nature  Journal

abstract

  • The entry of human immunodeficiency virus (HIV) into cells requires the sequential interaction of the viral exterior envelope glycoprotein, gp120, with the CD4 glycoprotein and a chemokine receptor on the cell surface. These interactions initiate a fusion of the viral and cellular membranes. Although gp120 can elicit virus-neutralizing antibodies, HIV eludes the immune system. We have solved the X-ray crystal structure at 2.5 A resolution of an HIV-1 gp120 core complexed with a two-domain fragment of human CD4 and an antigen-binding fragment of a neutralizing antibody that blocks chemokine-receptor binding. The structure reveals a cavity-laden CD4-gp120 interface, a conserved binding site for the chemokine receptor, evidence for a conformational change upon CD4 binding, the nature of a CD4-induced antibody epitope, and specific mechanisms for immune evasion. Our results provide a framework for understanding the complex biology of HIV entry into cells and should guide efforts to intervene.

subject areas

  • Amino Acid Sequence
  • Animals
  • Antigens, CD4
  • CHO Cells
  • Cricetinae
  • Cricetulus
  • Crystallography, X-Ray
  • Glycosylation
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV Envelope Protein gp41
  • Humans
  • Immunoglobulin Fragments
  • Membrane Fusion
  • Models, Molecular
  • Molecular Sequence Data
  • Neutralization Tests
  • Protein Conformation
  • Receptors, CCR5
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Identity

International Standard Serial Number (ISSN)

  • 0028-0836

PubMed ID

  • 9641677
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Additional Document Info

start page

  • 648

end page

  • 659

volume

  • 393

issue

  • 6686

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