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Structural basis of respiratory syncytial virus neutralization by motavizumab.

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.

SUBMITTER: McLellan JS

PROVIDER: S-EPMC3050594 | biostudies-literature | 2010 Feb

REPOSITORIES: biostudies-literature

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Structural basis of respiratory syncytial virus neutralization by motavizumab.

McLellan Jason S JS Chen Man M Kim Albert A Yang Yongping Y Graham Barney S BS Kwong Peter D PD

Nature structural & molecular biology 20100124 2

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 ...[more]

PMID: 20098425

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