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Structural basis for broad and potent neutralization of HIV-1 by antibody VRC01

Academic Article
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Overview

authors

  • Zhou, T.
  • Georgiev, I.
  • Wu, X.
  • Yang, Z. Y.
  • Dai, K.
  • Finzi, A.
  • Kwon, Y. D.
  • Scheid, J. F.
  • Shi, W.
  • Xu, L.
  • Yang, Y.
  • Zhu, Jiang
  • Nussenzweig, M. C.
  • Sodroski, J.
  • Shapiro, L.
  • Nabel, G. J.
  • Mascola, J. R.
  • Kwong, P. D.

publication date

  • August 2010

journal

  • Science  Journal

abstract

  • During HIV-1 infection, antibodies are generated against the region of the viral gp120 envelope glycoprotein that binds CD4, the primary receptor for HIV-1. Among these antibodies, VRC01 achieves broad neutralization of diverse viral strains. We determined the crystal structure of VRC01 in complex with a human immunodeficiency virus HIV-1 gp120 core. VRC01 partially mimics CD4 interaction with gp120. A shift from the CD4-defined orientation, however, focuses VRC01 onto the vulnerable site of initial CD4 attachment, allowing it to overcome the glycan and conformational masking that diminishes the neutralization potency of most CD4-binding-site antibodies. To achieve this recognition, VRC01 contacts gp120 mainly through immunoglobulin V-gene regions substantially altered from their genomic precursors. Partial receptor mimicry and extensive affinity maturation thus facilitate neutralization of HIV-1 by natural human antibodies.

subject areas

  • AIDS Vaccines
  • Amino Acid Sequence
  • Antibodies, Neutralizing
  • Antibody Affinity
  • Antigenic Variation
  • Antigens, CD4
  • Base Sequence
  • Binding Sites, Antibody
  • Crystallography, X-Ray
  • Epitopes
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • HIV-1
  • Humans
  • Immunoglobulin Fab Fragments
  • Models, Molecular
  • Molecular Mimicry
  • Molecular Sequence Data
  • Neutralization Tests
  • Protein Conformation
  • Protein Structure, Tertiary
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Identity

PubMed Central ID

  • PMC2981354

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1192819

PubMed ID

  • 20616231
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Additional Document Info

start page

  • 811

end page

  • 817

volume

  • 329

issue

  • 5993

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