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
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Research Support, N.I.H., Intramural
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Antibodies, Monoclonal / chemistry*
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Antibodies, Monoclonal / immunology
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Antibodies, Monoclonal, Humanized
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Antibodies, Neutralizing / chemistry*
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Antibodies, Neutralizing / immunology
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Antibodies, Viral / chemistry*
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Antibodies, Viral / immunology
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Antiviral Agents / chemistry*
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Antiviral Agents / immunology
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Crystallography, X-Ray
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Epitopes / chemistry*
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Epitopes / immunology
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Humans
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Models, Molecular
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Neutralization Tests
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Protein Structure, Quaternary
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Respiratory Syncytial Viruses / immunology*
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Viral Fusion Proteins / chemistry*
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Viral Fusion Proteins / immunology
Substances
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Antibodies, Monoclonal
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Antibodies, Monoclonal, Humanized
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Antibodies, Neutralizing
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Antibodies, Viral
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Antiviral Agents
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Epitopes
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F protein, human respiratory syncytial virus
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Viral Fusion Proteins
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motavizumab