An unrelated monoclonal antibody neutralizes human immunodeficiency virus type 1 by binding to an artificial epitope engineered in a functionally neutral region of the viral envelope glycoproteins

J Virol. 2005 May;79(9):5616-24. doi: 10.1128/JVI.79.9.5616-5624.2005.

Abstract

Neutralizing antibodies often recognize regions of viral envelope glycoproteins that play a role in receptor binding or other aspects of virus entry. To address whether this is a necessary feature of a neutralizing antibody, we identified the V4 region of the gp120 envelope glycoprotein of human immunodeficiency virus type 1 (HIV-1) as a sequence that is tolerant of drastic change and thus appears to play a negligible role in envelope glycoprotein function. An artificial epitope tag was inserted into the V4 region without a significant effect on virus entry or neutralization by antibodies that recognize HIV-1 envelope glycoprotein sequences. An antibody directed against the artificial epitope tag was able to neutralize the modified, but not the wild-type, HIV-1. Thus, the specific target of a neutralizing antibody need not contribute functionally to the process of virus entry.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Amino Acid Sequence
  • Antibodies, Monoclonal / immunology
  • Epitopes / genetics
  • Epitopes / immunology
  • HIV Antibodies / immunology
  • HIV Envelope Protein gp120 / genetics
  • HIV Envelope Protein gp120 / immunology*
  • HIV-1 / genetics
  • HIV-1 / immunology*
  • HIV-1 / physiology
  • Molecular Sequence Data
  • Neutralization Tests
  • Recombinant Proteins / immunology
  • Virus Replication / immunology

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • HIV Antibodies
  • HIV Envelope Protein gp120
  • Recombinant Proteins