Structural basis of respiratory syncytial virus neutralization by motavizumab
JS McLellan, M Chen, A Kim, Y Yang… - Nature structural & …, 2010 - nature.com
JS McLellan, M Chen, A Kim, Y Yang, BS Graham, PD Kwong
Nature structural & molecular biology, 2010•nature.comMotavizumab is∼ 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.
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.
Abstract
Motavizumab is ∼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.
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