Epitopes described in "Structural basis of respiratory syncytial virus neutralization by motavizumab."

Article Authors:Jason S McLellan; Man Chen; Albert Kim; Yongping Yang; Barney S Graham; Peter D Kwong
Article Title:Structural basis of respiratory syncytial virus neutralization by motavizumab.
Reference Detail
Reference ID:1018833
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.
Affiliations:Vaccine Research Center, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, Maryland, USA.
Reference Type:Literature
PubMed ID:20098425
Journal:Nat Struct Mol Biol
Journal Volume:17
Article Pages:248-50
Journal ISSN:1545-9993
Article Chemical List:Antibodies, Monoclonal;Antibodies, Monoclonal, Humanized;Antibodies, Neutralizing;Antibodies, Viral;Antiviral Agents;Epitopes;F protein, human respiratory syncytial virus;Viral Fusion Proteins;motavizumab
Article MeSH List:Antibodies, Monoclonal(chemistry; immunology); Antibodies, Monoclonal, Humanized; Antibodies, Neutralizing(chemistry; immunology); Antibodies, Viral(chemistry; immunology); Antiviral Agents(chemistry; immunology); Crystallography, X-Ray; Epitopes(chemistry; immunology); Humans; Models, Molecular; Neutralization Tests; Protein Structure, Quaternary; Respiratory Syncytial Viruses(immunology); Viral Fusion Proteins(chemistry; immunology)
Curation Last Updated:2015-06-05 01:57:40