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Structural basis of immune evasion at the site of cd4 attachment on hiv-1 gp120

Academic Article
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Overview

authors

  • Chen, L.
  • Kwon, Y. D.
  • Zhou, T. Q.
  • Wu, X.
  • O'Dell, S.
  • Cavacini, L.
  • Hessell, A. J.
  • Pancera, M.
  • Tang, M.
  • Xu, L.
  • Yang, Z. Y.
  • Zhang, M. Y.
  • Arthos, J.
  • Burton, Dennis
  • Dimitrov, D. S.
  • Nabel, G. J.
  • Posner, M. R.
  • Sodroski, J.
  • Wyatt, Richard
  • Mascola, J. R.
  • Kwong, P. D.

publication date

  • November 2009

journal

  • Science  Journal

abstract

  • The site on HIV-1 gp120 that binds to the CD4 receptor is vulnerable to antibodies. However, most antibodies that interact with this site cannot neutralize HIV-1. To understand the basis of this resistance, we determined co-crystal structures for two poorly neutralizing, CD4-binding site (CD4BS) antibodies, F105 and b13, in complexes with gp120. Both antibodies exhibited approach angles to gp120 similar to those of CD4 and a rare, broadly neutralizing CD4BS antibody, b12. Slight differences in recognition, however, resulted in substantial differences in F105- and b13-bound conformations relative to b12-bound gp120. Modeling and binding experiments revealed these conformations to be poorly compatible with the viral spike. This incompatibility, the consequence of slight differences in CD4BS recognition, renders HIV-1 resistant to all but the most accurately targeted antibodies.

subject areas

  • Amino Acid Sequence
  • Antibodies, Neutralizing
  • Antigens, CD4
  • Binding Sites
  • Binding Sites, Antibody
  • Crystallography, X-Ray
  • Epitopes
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV-1
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Immune Evasion
  • Models, Molecular
  • Molecular Sequence Data
  • Peptide Fragments
  • Protein Conformation
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Identity

PubMed Central ID

  • PMC2862588

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1175868

PubMed ID

  • 19965434
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Additional Document Info

start page

  • 1123

end page

  • 1127

volume

  • 326

issue

  • 5956

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