Structure of Respiratory Syncytial Virus Fusion Glycoprotein in the Postfusion Conformation Reveals Preservation of Neutralizing Epitopes
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Implication
Structural study identifies preserved neutralizing epitopes in RSV fusion protein, suggesting vaccine potential.
Key Points
- This research aims to uncover the structure of the respiratory syncytial virus fusion glycoprotein in its postfusion state and its implications for antibody neutralization.
- Conducted structural and biophysical studies on stable ectodomain constructs of RSV F glycoprotein.
- Determined the 2.8-Å crystal structure of the trimeric RSV F ectodomain in postfusion conformation.
- Utilized surface plasmon resonance to assess antibody binding affinity to the postfusion glycoprotein.
- The 2.8-Å crystal structure of the trimeric F glycoprotein shows preserved neutralizing epitopes.
- Both antibodies, 101F and motavizumab, bound to the postfusion F glycoprotein indicating high affinity.
- Modeling suggests a quaternary epitope for motavizumab and a larger single protomer epitope for 101F.
Cite This Study
McLellan et al. (2011) studied this question.