Antibody binding in proximity to the receptor/glycoprotein complex leads to a basal level of virus neutralization

J Virol. 2007 Aug;81(16):8809-13. doi: 10.1128/JVI.00394-07. Epub 2007 May 30.

Abstract

Hypothetically, antibodies may neutralize enveloped viruses by diverse mechanisms, such as disruption of receptor binding, interference with conformational changes required for virus entry, steric hindrance, or virus aggregation. Here, we demonstrate that retroviral infection mediated by the avian sarcoma-leukosis virus (ASLV-A) envelope glycoproteins can be neutralized by an antibody directed against a functionally unimportant component of a chimeric receptor protein. Thus, the binding of an antibody in proximity to the retroviral envelope glycoprotein-receptor complex, without binding to the entry machinery itself, results in neutralization. This finding provides additional support for the hypothesis that steric hindrance is sufficient for antibody-mediated neutralization of retroviruses.

Publication types

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

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology
  • Antibodies, Monoclonal / pharmacology
  • Antibodies, Viral / immunology
  • Antibodies, Viral / pharmacology*
  • Antigen-Antibody Reactions
  • Avian Sarcoma Viruses / drug effects*
  • Avian Sarcoma Viruses / immunology
  • CCR5 Receptor Antagonists*
  • Cells, Cultured
  • Glycoproteins / immunology*
  • Humans
  • Ligands
  • Receptors, Virus / antagonists & inhibitors*
  • Receptors, Virus / immunology
  • Viral Envelope Proteins / immunology*
  • Virus Internalization / drug effects*

Substances

  • Antibodies, Monoclonal
  • Antibodies, Viral
  • CCR5 Receptor Antagonists
  • Glycoproteins
  • Ligands
  • Receptors, Virus
  • Viral Envelope Proteins