Peptide Paratope Mimics of the Broadly Neutralizing HIV-1 Antibody b12

Chembiochem. 2017 Apr 4;18(7):647-653. doi: 10.1002/cbic.201600621. Epub 2017 Mar 6.

Abstract

The broadly neutralizing HIV-1 antibody b12 recognizes the CD4 binding site of the HIV-1 envelope glycoprotein gp120 and efficiently neutralizes HIV-1 infections in vitro and in vivo. Based on the 3D structure of a b12⋅gp120 complex, we have designed an assembled peptide (b12-M) that presents the parts of the three heavy-chain complementarity-determining regions (CDRs) of b12, which contain the contact sites of the antibody for gp120. This b12-mimetic peptide, as well as a truncated peptide presenting only two of the three heavy-chain CDRs of b12, were shown to recognize gp120 in a similar manner to b12, as well as to inhibit HIV-1 infection, demonstrating functional mimicry of b12 by the paratope mimetic peptides.

Keywords: HIV-1; MAb b12; antibody mimics; gp120; immunochemistry; peptides.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-HIV Agents / chemical synthesis
  • Anti-HIV Agents / immunology*
  • Antibodies, Monoclonal / immunology*
  • Antibodies, Neutralizing / immunology*
  • Binding Sites
  • Cell Line
  • HIV Envelope Protein gp120 / immunology*
  • HIV-1 / immunology*
  • Humans
  • Immunoglobulin Heavy Chains / immunology
  • Peptides / chemical synthesis
  • Peptides / immunology*
  • Protein Engineering

Substances

  • Anti-HIV Agents
  • Antibodies, Monoclonal
  • Antibodies, Neutralizing
  • HIV Envelope Protein gp120
  • Immunoglobulin Heavy Chains
  • Peptides