Exploring converse molecular mechanisms of anti-HIV-1 antibodies using a synthetic CXCR4 mimic

Bioorg Med Chem Lett. 2012 Oct 1;22(19):6099-102. doi: 10.1016/j.bmcl.2012.08.035. Epub 2012 Aug 16.

Abstract

Different molecular mechanisms of the two broadly neutralizing anti-HIV-1 antibodies b12 and VRC01, as evidenced by their converse effects on the interaction of HIV-1 envelope glycoprotein gp120 with cellular coreceptors, were demonstrated using a synthetic CXCR4 mimetic peptide (CX4-M1) as coreceptor surrogate. While the interaction of gp120 with CX4-M1 was distinctly enhanced by VRC01, b12 was shown to have the contrary effect, and also to inhibit the VRC01-induced enhancement of gp120 binding to the CXCR4 mimetic peptide.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • HIV / immunology*
  • HIV Antibodies / chemistry
  • HIV Antibodies / immunology*
  • HIV Envelope Protein gp120 / chemistry
  • HIV Envelope Protein gp120 / immunology
  • Models, Molecular
  • Molecular Mimicry / immunology*
  • Peptides / chemical synthesis
  • Peptides / chemistry
  • Peptides / immunology*
  • Receptors, CXCR4 / immunology*

Substances

  • HIV Antibodies
  • HIV Envelope Protein gp120
  • Peptides
  • Receptors, CXCR4