Structural basis of respiratory syncytial virus neutralization by motavizumab

Nat Struct Mol Biol. 2010 Feb;17(2):248-50. doi: 10.1038/nsmb.1723. Epub 2010 Jan 24.

Abstract

Motavizumab is approximately tenfold more potent than its predecessor, palivizumab (Synagis), the FDA-approved monoclonal antibody used to prevent respiratory syncytial virus (RSV) infection. The structure of motavizumab in complex with a 24-residue peptide corresponding to its epitope on the RSV fusion (F) glycoprotein reveals the structural basis for this greater potency. Modeling suggests that motavizumab recognizes a different quaternary configuration of the F glycoprotein than that observed in a homologous structure.

Publication types

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

MeSH terms

  • Antibodies, Monoclonal / chemistry*
  • Antibodies, Monoclonal / immunology
  • Antibodies, Monoclonal, Humanized
  • Antibodies, Neutralizing / chemistry*
  • Antibodies, Neutralizing / immunology
  • Antibodies, Viral / chemistry*
  • Antibodies, Viral / immunology
  • Antiviral Agents / chemistry*
  • Antiviral Agents / immunology
  • Crystallography, X-Ray
  • Epitopes / chemistry*
  • Epitopes / immunology
  • Humans
  • Models, Molecular
  • Neutralization Tests
  • Protein Structure, Quaternary
  • Respiratory Syncytial Viruses / immunology*
  • Viral Fusion Proteins / chemistry*
  • Viral Fusion Proteins / immunology

Substances

  • Antibodies, Monoclonal
  • Antibodies, Monoclonal, Humanized
  • Antibodies, Neutralizing
  • Antibodies, Viral
  • Antiviral Agents
  • Epitopes
  • F protein, human respiratory syncytial virus
  • Viral Fusion Proteins
  • motavizumab

Associated data

  • PDB/3IXT