ArticlePloS one2019
Structure basis of neutralization by a novel site II/IV antibody against respiratory syncytial virus fusion protein.
Article in PloS one, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 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.
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Who cites it
9 citing papers in PubMed.
- Structural Advances in Respiratory Syncytial Virus: Implications for Vaccine and Antiviral Development.Microorganisms · 2026Review
- DS2 designer pre-fusion F vaccine induces strong and protective antibody response against RSV infection.NPJ vaccines · 2024Article
- Age-Stratified Seroprevalence of Respiratory Syncytial Virus: Analysis Using Prefusion F and G Protein Antibodies.Vaccines · 2024Article
- Characterization of a Panel of Monoclonal Antibodies Targeting the F-Protein of the Respiratory Syncytial Virus (RSV) for the Typing of Contemporary Circulating Strains.Tropical medicine and infectious disease · 2023Article
- New Anti-RSV Nucleoprotein Monoclonal Antibody Pairs Discovered Using Rabbit Phage Display Technology.Antibodies (Basel, Switzerland) · 2023Article
- The Efficiency of p27 Cleavage duringJournal of virology · 2023Article
- Article
- Antibody Epitopes of Pneumovirus Fusion Proteins.Frontiers in immunology · 2019Review
- Article
Corrections and comments
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Authors and funding
15 authors.
Funding
Abstract
Globally, human respiratory syncytial virus (RSV) is a leading cause of lower respiratory tract infections in newborns, young children, and the elderly for which there is no vaccine. The RSV fusion (F) glycoprotein is a major target for vaccine development. Here, we describe a novel monoclonal antibody (designated as R4.C6) that recognizes both pre-fusion and post-fusion RSV F, and binds with nanomole affinity to a unique neutralizing site comprised of antigenic sites II and IV on the globular head. A 3.9 Å-resolution structure of RSV F-R4.C6 Fab complex was obtained by single particle cryo-electron microscopy and 3D reconstruction. The structure unraveled detailed interactions of R4.C6 with antigenic site II on one protomer and site IV on a neighboring protomer of post-fusion RSV F protein. These findings significantly further our understanding of the antigenic complexity of the F protein and provide new insights into RSV vaccine design.
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Registered trials
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