ArticlePloS one2016
Stability Characterization of a Vaccine Antigen Based on the Respiratory Syncytial Virus Fusion Glycoprotein.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
What it found
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Who cites it
24 citing papers in PubMed.
- A cavity-reduced prefusion RSV F bivalent vaccine elicits durable and protective immunity.EMBO molecular medicine · 2026Article
- Distinct mechanisms of neutralization by antibodies targeting a conserved pneumovirus F epitope.bioRxiv : the preprint server for biology · 2026Article
- Potency Evaluation and Predictive Quality Control System Construction Strategy for Respiratory Syncytial Virus mRNA Vaccines.Vaccines · 2026Review
- Intranasal delivery of a polymeric nanoparticle subunit vaccine for the induction of protective immunity against respiratory syncytial virus.Frontiers in immunology · 2026Article
- Prediction of pre- and postfusion conformations of class I fusion proteins with AlphaFold2.PloS one · 2026Article
- Nanoparticle vaccine based on the pre-fusion F glycoprotein of respiratory syncytial virus elicits robust protective immune responses.Journal of virology · 2025Article
- Highly scalable prefusion-stabilized RSV F vaccine with enhanced immunogenicity and robust protection.Nature communications · 2025Article
- A truncated pre-F protein mRNA vaccine elicits an enhanced immune response and protection against respiratory syncytial virus.Nature communications · 2025Article
- DS2 designer pre-fusion F vaccine induces strong and protective antibody response against RSV infection.NPJ vaccines · 2024Article
- Lethal model for respiratory syncytial virus infection using C57BL/6 mice.Journal of virology · 2024Article
- Article
- Review
- Respiratory Syncytial Virus Vaccines: A Review of the Candidates and the Approved Vaccines.Pathogens (Basel, Switzerland) · 2023Review
- Gamma Irradiation-Inactivated Respiratory Syncytial Virus Vaccine Provides Protection but Exacerbates Pulmonary Inflammation by Switching from Prefusion to Postfusion F Protein.Microbiology spectrum · 2023Article
- Transplacental Antibody Transfer of Respiratory Syncytial Virus Specific IgG in Non-Human Primate Mother-Infant Pairs.Pathogens (Basel, Switzerland) · 2021Article
- The respiratory syncytial virus (RSV) prefusion F-protein functional antibody repertoire in adult healthy donors.EMBO molecular medicine · 2021Article
- Micro-fusion inhibition tests: quantifying antibody neutralization of virus-mediated cell-cell fusion.The Journal of general virology · 2021Article
- Modified mRNA/lipid nanoparticle-based vaccines expressing respiratory syncytial virus F protein variants are immunogenic and protective in rodent models of RSV infection.NPJ vaccines · 2020Article
- Challenges of Developing Novel Vaccines With Particular Global Health Importance.Frontiers in immunology · 2020Review
- Alternative Virus-Like Particle-Associated Prefusion F Proteins as Maternal Vaccines for Respiratory Syncytial Virus.Journal of virology · 2019Article
Corrections and comments
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Infection with Respiratory Syncytial Virus (RSV) causes both upper and lower respiratory tract disease in humans, leading to significant morbidity and mortality in both young children and older adults. Currently, there is no licensed vaccine available, and therapeutic options are limited. During the infection process, the type I viral fusion (F) glycoprotein on the surface of the RSV particle rearranges from a metastable prefusion conformation to a highly stable postfusion form. In people naturally infected with RSV, most potent neutralizing antibodies are directed to the prefusion form of the F protein. Therefore, an engineered RSV F protein stabilized in the prefusion conformation (DS-Cav1) is an attractive vaccine candidate. Long-term stability at 4°C or higher is a desirable attribute for a commercial subunit vaccine antigen. To assess the stability of DS-Cav1, we developed assays using D25, an antibody which recognizes the prefusion F-specific antigenic site Ø, and a novel antibody 4D7, which was found to bind antigenic site I on the postfusion form of RSV F. Biophysical analysis indicated that, upon long-term storage at 4°C, DS-Cav1 undergoes a conformational change, adopting alternate structures that concomitantly lose the site Ø epitope and gain the ability to bind 4D7.
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