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Antibody vs. HIV in a clash of evolutionary titans

Academic Article
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Overview

authors

  • Burton, Dennis
  • Stanfield, Robyn
  • Wilson, Ian

publication date

  • 2005

journal

  • Proceedings of the National Academy of Sciences of the United States of America  Journal

abstract

  • HIV has evolved many strategies to avoid neutralizing antibody responses, particularly to conserved regions on the external glycoprotein spikes of the virus. Nevertheless, a small number of antibodies have been evolved by the human immune system to recognize conserved parts of the glycoproteins, and therefore, have broadly neutralizing cross-strain activities. These antibodies constitute important tools in the quest to design immunogens that can elicit broadly neutralizing antibodies in humans and hence contribute to an effective HIV vaccine. Crystallographic analyses of the antibodies, in many cases in an antigen-complexed form, have revealed novel and, in some instances, remarkable structural adaptations to attain virus recognition. Antibodies, like HIV, can evolve relatively rapidly through mutation and selection. It seems that the structures of these broadly neutralizing antibodies bear witness to a heroic struggle between two titans of rapid evolution.

subject areas

  • AIDS Vaccines
  • Antigens, Viral
  • Binding Sites
  • Evolution, Molecular
  • Glycoproteins
  • HIV
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • Humans
  • Neutralization Tests
  • Protein Conformation
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Identity

PubMed Central ID

  • PMC1257708

International Standard Serial Number (ISSN)

  • 0027-8424

Digital Object Identifier (DOI)

  • 10.1073/pnas.0505126102

PubMed ID

  • 16219699
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Additional Document Info

start page

  • 14943

end page

  • 14948

volume

  • 102

issue

  • 42

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