ArticleEMBO molecular medicine2022
Protective antigenic sites identified in respiratory syncytial virus fusion protein reveals importance of p27 domain.
Article in EMBO molecular medicine, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 18 citations in OpenAlex.
- Phylodynamics and molecular epidemiology of the respiratory syncytial virus fusion protein in China.Microbiology spectrum · 2026Article
- Vaccine Development for Human Pneumoviruses.Vaccines · 2025Review
- Examination of respiratory syncytial virus fusion protein proteolytic processing and roles of the P27 domain.Journal of virology · 2024Article
- Evaluating the Impact of N-Glycan Sequon Removal in the p27 Peptide on RSV F Protein Immunogenicity and Functionality.Viruses · 2024Article
- A multi-center study on genetic variations in the fusion protein of respiratory syncytial virus from children with Acute Lower Respiratory Tract Infections in China during 2017-2021.Virologica Sinica · 2024Article
- Article
- Monoclonal antibodies targeting sites in respiratory syncytial virus attachment G protein provide protection against RSV-A and RSV-B in mice.Nature communications · 2024Article
- Design of hepadnavirus core protein-based chimeric virus-like particles carrying epitopes from respiratory syncytial virus.NPJ vaccines · 2024Article
- Immunogenicity of a recombinant plant-produced respiratory syncytial virus F subunit vaccine in mice.Biotechnology reports (Amsterdam, Netherlands) · 2024Article
- Review
- The Efficiency of p27 Cleavage duringJournal of virology · 2023Article
- The RSV F p27 peptide: current knowledge, important questions.Frontiers in microbiology · 2023Review
- Antibody responses of healthy adults to the p27 peptide of respiratory syncytial virus fusion protein.Vaccine · 2022Article
- Protective antigenic sites identified in respiratory syncytial virus fusion protein reveals importance of p27 domain.EMBO molecular medicine · 2022Article
Corrections and comments
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Respiratory syncytial virus (RSV) vaccines primarily focused on surface fusion (F) protein are under development. Therefore, to identify RSV-F protective epitopes, we evaluated 14 antigenic sites recognized following primary human RSV infection. BALB/c mice were vaccinated with F peptides, F proteins, or RSV-A2, followed by rA2-Line19F challenge. F peptides generated binding antibodies with minimal in vitro neutralization titers. However, several F peptides (including Site II) reduced lung viral loads and lung pathology scores in animals, suggesting partial protection from RSV disease. Interestingly, animals vaccinated with peptides (aa 101-121 and 110-136) spanning the F-p27 sequence, which is only present in unprocessed F0 protein, showed control of viral loads with significantly reduced pathology compared with mock-vaccinated controls. Furthermore, we observed F-p27 expression on the surface of RSV-infected cells as well as lungs from RSV-infected mice. The anti-p27 antibodies demonstrated antibody-dependent cellular cytotoxicity (ADCC) of RSV-infected A549 cells. These findings suggest that p27-mediated immune response may play a role in control of RSV disease in vivo, and F-p27 should be considered for inclusion in an effective RSV vaccine.
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