ArticleJournal of virology2020
Conformational Flexibility in Respiratory Syncytial Virus G Neutralizing Epitopes.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- A Self-Assembling Cross-Protective Antigen Against Multiple Gram-Positive Nosocomial Pathogens.ACS omega · 2025Article
- Layer-by-Layer Microparticle Vaccines Containing a S177Q Point Mutation in the Central Conserved Domain of the RSV G Protein Improves Immunogenicity.Viral immunology · 2025Article
- Structures of respiratory syncytial virus G bound to broadly reactive antibodies provide insights into vaccine design.Scientific reports · 2025Article
- Article
- Bovine Respiratory Syncytial Virus Nanovaccine Induces Long-Lasting Humoral Immunity in Mice.ACS pharmacology & translational science · 2024Article
- A rationally designed antigen elicits protective antibodies against multiple nosocomial Gram-positive pathogens.NPJ vaccines · 2024Article
- Review
- Structural basis for respiratory syncytial virus and human metapneumovirus neutralization.Current opinion in virology · 2023Review
- A conformational epitope in placental malaria vaccine antigen VAR2CSA: What does it teach us?PLoS pathogens · 2023Article
- Immunogenicity and protective efficacy of an RSV G S177Q central conserved domain nanoparticle vaccine.Frontiers in immunology · 2023Article
- Non-glycosylated G protein with CpG ODN provides robust protection against respiratory syncytial virus without inducing eosinophilia.Frontiers in immunology · 2023Article
- Immunization with a mucosal, post-fusion F/G protein-based polyanhydride nanovaccine protects neonatal calves against BRSV infection.Frontiers in immunology · 2023Article
- Review
- Structure-Based Design and Antigenic Validation of Respiratory Syncytial Virus G Immunogens.Journal of virology · 2022Article
- Review
- Sendai Virus-Vectored Vaccines That Express Envelope Glycoproteins of Respiratory Viruses.Viruses · 2021Review
- Learning from the past: development of safe and effective COVID-19 vaccines.Nature reviews. Microbiology · 2021Article
- Article
- Immunogenicity and inflammatory properties of respiratory syncytial virus attachment G protein in cotton rats.PloS one · 2021Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Respiratory syncytial virus (RSV) is a top cause of severe lower respiratory tract disease and mortality in infants and the elderly. Currently, no vaccine or effective treatment exists for RSV. The RSV G glycoprotein mediates viral attachment to cells and contributes to pathogenesis by modulating host immunity through interactions with the human chemokine receptor CX3CR1. Antibodies targeting the RSV G central conserved domain are protective in both prophylactic and postinfection animal models. Here, we describe the crystal structure of the broadly neutralizing human monoclonal antibody 3G12 bound to the RSV G central conserved domain. Antibody 3G12 binds to a conformational epitope composed of highly conserved residues, explaining its broad neutralization activity. Surprisingly, RSV G complexed with 3G12 adopts a distinct conformation not observed in previously described RSV G-antibody structures. Comparison to other structures reveals that the RSV G central conserved domain is flexible and can adopt multiple conformations in the regions flanking the cysteine noose. We also show that restriction of RSV G flexibility with a proline mutation abolishes binding to antibody 3G12 but not antibody 3D3, which recognizes a different conformation of RSV G. Our studies provide new insights for rational vaccine design, indicating the importance of preserving both the global structural integrity of antigens and local conformational flexibility at antigenic sites, which may elicit a more diverse antibody response and broader protection against infection and disease.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.