ArticlePLoS pathogens2019
Alternative conformations of a major antigenic site on RSV F.
Article in PLoS pathogens, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed.
- Structural and functional characterization of a conserved cryptic epitope on SARS-CoV-2 spike S2 subunit.PLoS pathogens · 2026Article
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- Structural vaccinology expedites rational design of next-generation vaccines for influenza and respiratory syncytial virus.Virologica Sinica · 2026Review
- Venenum bufonis and its active constituents alleviate RSV-induced pneumonia in mice by suppressing macrophage infiltration and NLRP3 inflammasome activation.Virus research · 2026Article
- A novel bispecific nanobody protects mice against RSV infection via intranasal administration.Journal of virology · 2025Article
- Highly scalable prefusion-stabilized RSV F vaccine with enhanced immunogenicity and robust protection.Nature communications · 2025Article
- Hydrophobic residue substitutions enhance the stability andJournal of virology · 2025Article
- A single amino acid mutation alters multiple neutralization epitopes in the respiratory syncytial virus fusion glycoprotein.Npj viruses · 2025Article
- Respiratory syncytial virus vaccines for toddlers and school-aged children: a pressing necessity for global health.Frontiers in pediatrics · 2025Article
- DS2 designer pre-fusion F vaccine induces strong and protective antibody response against RSV infection.NPJ vaccines · 2024Article
- A foldon-free prefusion F trimer vaccine for respiratory syncytial virus to reduce off-target immune responses.Nature microbiology · 2024Article
- Rational design of uncleaved prefusion-closed trimer vaccines for human respiratory syncytial virus and metapneumovirus.Nature communications · 2024Article
- Interactions Between Bovine Respiratory Syncytial Virus and Cattle: Aspects of Pathogenesis and Immunity.Viruses · 2024Review
- The Cumulative Variations of Respiratory Syncytial Virus Fusion Protein (F) in Ten Consecutive Years in China.Infectious disease reports · 2024Article
- Differences Between RSV A and RSV B Subgroups and Implications for Pharmaceutical Preventive Measures.Infectious diseases and therapy · 2024Review
- A tale of two fusion proteins: understanding the metastability of human respiratory syncytial virus and metapneumovirus and implications for rational design of uncleaved prefusion-closed trimers.bioRxiv : the preprint server for biology · 2024Article
- A general computational design strategy for stabilizing viral class I fusion proteins.Nature communications · 2024Article
- Assessing the protection elicited by virus-like particles expressing the RSV pre-fusion F and tandem repeated G proteins against RSV rA2 line19F infection in mice.Respiratory research · 2024Article
- Article
- The Efficiency of p27 Cleavage duringJournal of virology · 2023Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
The respiratory syncytial virus (RSV) fusion (F) glycoprotein is a major target of neutralizing antibodies arising from natural infection, and antibodies that specifically bind to the prefusion conformation of RSV F generally demonstrate the greatest neutralization potency. Prefusion-stabilized RSV F variants have been engineered as vaccine antigens, but crystal structures of these variants have revealed conformational differences in a key antigenic site located at the apex of the trimer, referred to as antigenic site Ø. Currently, it is unclear if flexibility in this region is an inherent property of prefusion RSV F or if it is related to inadequate stabilization of site Ø in the engineered variants. Therefore, we set out to investigate the conformational flexibility of antigenic site Ø, as well as the ability of the human immune system to recognize alternative conformations of this site, by determining crystal structures of prefusion RSV F bound to neutralizing human-derived antibodies AM22 and RSD5. Both antibodies bound with high affinity and were specific for the prefusion conformation of RSV F. Crystal structures of the complexes revealed that the antibodies recognized distinct conformations of antigenic site Ø, each diverging at a conserved proline residue located in the middle of an α-helix. These data suggest that antigenic site Ø exists as an ensemble of conformations, with individual antibodies recognizing discrete states. Collectively, these results have implications for the refolding of pneumovirus and paramyxovirus fusion proteins and should inform development of prefusion-stabilized RSV F vaccine candidates.
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