ArticlePLoS pathogens2020
Convergent structural features of respiratory syncytial virus neutralizing antibodies and plasticity of the site V epitope on prefusion F.
Article in PLoS pathogens, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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Who cites it
10 citing papers in PubMed.
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein.Cell reports. Medicine · 2026Article
- DS2 designer pre-fusion F vaccine induces strong and protective antibody response against RSV infection.NPJ vaccines · 2024Article
- A potent broad-spectrum neutralizing antibody targeting a conserved region of the prefusion RSV F protein.Nature communications · 2024Article
- A potently neutralizing and protective human antibody targeting antigenic site V on RSV and hMPV fusion glycoprotein.bioRxiv : the preprint server for biology · 2024Article
- Structural characterization of M8C10, a neutralizing antibody targeting a highly conserved prefusion-specific epitope on the metapneumovirus fusion trimerization interface.Journal of virology · 2023Article
- Discovery and multimerization of cross-reactive single-domain antibodies against SARS-like viruses to enhance potency and address emerging SARS-CoV-2 variants.Scientific reports · 2023Article
- Cross-protective antibodies against common endemic respiratory viruses.Nature communications · 2023Article
- Profiling of hMPV F-specific antibodies isolated from human memory B cells.Nature communications · 2022Article
- Article
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Authors and funding
18 authors.
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Abstract
Respiratory syncytial virus (RSV) is a global public health burden for which no licensed vaccine exists. To aid vaccine development via increased understanding of the protective antibody response to RSV prefusion glycoprotein F (PreF), we performed structural and functional studies using the human neutralizing antibody (nAb) RSB1. The crystal structure of PreF complexed with RSB1 reveals a conformational, pre-fusion specific site V epitope with a unique cross-protomer binding mechanism. We identify shared structural features between nAbs RSB1 and CR9501, elucidating for the first time how diverse germlines obtained from different subjects can develop convergent molecular mechanisms for recognition of the same PreF site of vulnerability. Importantly, RSB1-like nAbs were induced upon immunization with PreF in naturally-primed cattle. Together, this work reveals new details underlying the immunogenicity of site V and further supports PreF-based vaccine development efforts.
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Registered trials
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