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- W2533150511 abstract "Significance Respiratory syncytial virus is a highly contagious human pathogen, infecting the majority of infants before age 2 y, and is the leading cause of viral bronchiolitis and viral pneumonia in infants and children. An approved prophylactic humanized mouse monoclonal antibody, palivizumab, is currently the standard-of-care treatment for immunocompromised individuals, and competition with palivizumab has been proposed as the basis for measuring effective immune responses for vaccine trials. Using a combination of X-ray crystallography, hydrogen-deuterium exchange, and saturation alanine mutagenesis scanning, we show the structural basis for neutralization by a human antibody at the palivizumab antigenic site. Furthermore, we describe nonneutralizing antibodies that directly compete with palivizumab and another human antibody 14N4. Taken together, the data presented provide unique concepts in structure-based vaccine design." @default.
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- W2533150511 date "2016-10-17" @default.
- W2533150511 modified "2023-09-27" @default.
- W2533150511 title "Structural basis for nonneutralizing antibody competition at antigenic site II of the respiratory syncytial virus fusion protein" @default.
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- W2533150511 doi "https://doi.org/10.1073/pnas.1609449113" @default.
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