ArticleJournal of virology2010
Neutralization of human respiratory syncytial virus infectivity by antibodies and low-molecular-weight compounds targeted against the fusion glycoprotein.
Article in Journal of virology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 59 citations in OpenAlex.
- Convalescent plasma treatment reduced mortality in patients with severe pandemic influenza A (H1N1) 2009 virus infection.Clinical infectious diseases : an official publication of the Infectious Diseases Society of America · 2011Trial
- Genomic Surveillance and Antigenic Characterization of Respiratory Syncytial Virus (RSV) in Spain During the 2023-2024 Season of Nirsevimab Administration.The Journal of infectious diseases · 2026Article
- Structure-Guided Design of Peptide Inhibitors Targeting Class I Viral Fusion Proteins.Pathogens (Basel, Switzerland) · 2025Review
- Article
- Structural basis for respiratory syncytial virus and human metapneumovirus neutralization.Current opinion in virology · 2023Review
- A vulnerable, membrane-proximal site in human respiratory syncytial virus F revealed by a prefusion-specific single-domain antibody.Journal of virology · 2021Article
- Convergent structural features of respiratory syncytial virus neutralizing antibodies and plasticity of the site V epitope on prefusion F.PLoS pathogens · 2020Article
- Antibody development for preventing the human respiratory syncytial virus pathology.Molecular medicine (Cambridge, Mass.) · 2020Review
- Crystal Structure and Immunogenicity of the DS-Cav1-Stabilized Fusion Glycoprotein From Respiratory Syncytial Virus Subtype B.Pathogens & immunity · 2019Article
- Development of a Virosomal RSV Vaccine Containing 3D-PHAD® Adjuvant: Formulation, Composition, and Long-Term Stability.Pharmaceutical research · 2018Article
- Induction and Subversion of Human Protective Immunity: Contrasting Influenza and Respiratory Syncytial Virus.Frontiers in immunology · 2018Review
- Neutralizing epitopes of RSV and palivizumab resistance in Japan.Fukushima journal of medical science · 2017Review
- Characterization of Pre-F-GCN4t, a Modified Human Respiratory Syncytial Virus Fusion Protein Stabilized in a Noncleaved Prefusion Conformation.Journal of virology · 2017Article
- RSV N-nanorings fused to palivizumab-targeted neutralizing epitope as a nanoparticle RSV vaccine.Nanomedicine : nanotechnology, biology, and medicine · 2017Article
- Structural, antigenic and immunogenic features of respiratory syncytial virus glycoproteins relevant for vaccine development.Vaccine · 2017Review
- The Complexity of Antibody Responses Elicited against the Respiratory Syncytial Virus Glycoproteins in Hospitalized Children Younger than 2 Years.Frontiers in microbiology · 2017Article
- Rapid profiling of RSV antibody repertoires from the memory B cells of naturally infected adult donors.Science immunology · 2016Article
- Trivalency of a Nanobody Specific for the Human Respiratory Syncytial Virus Fusion Glycoprotein Drastically Enhances Virus Neutralization and Impacts Escape Mutant Selection.Antimicrobial agents and chemotherapy · 2016Article
- Influence of Respiratory Syncytial Virus F Glycoprotein Conformation on Induction of Protective Immune Responses.Journal of virology · 2016Article
- Stability Characterization of a Vaccine Antigen Based on the Respiratory Syncytial Virus Fusion Glycoprotein.PloS one · 2016Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human respiratory syncytial virus (HRSV) fusion (F) protein is an essential component of the virus envelope that mediates fusion of the viral and cell membranes, and, therefore, it is an attractive target for drug and vaccine development. Our aim was to analyze the neutralizing mechanism of anti-F antibodies in comparison with other low-molecular-weight compounds targeted against the F molecule. It was found that neutralization by anti-F antibodies is related to epitope specificity. Thus, neutralizing and nonneutralizing antibodies could bind equally well to virions and remained bound after ultracentrifugation of the virus, but only the former inhibited virus infectivity. Neutralization by antibodies correlated with inhibition of cell-cell fusion in a syncytium formation assay, but not with inhibition of virus binding to cells. In contrast, a peptide (residues 478 to 516 of F protein [F478-516]) derived from the F protein heptad repeat B (HRB) or the organic compound BMS-433771 did not interfere with virus infectivity if incubated with virus before ultracentrifugation or during adsorption of virus to cells at 4 degrees C. These inhibitors must be present during virus entry to effect HRSV neutralization. These results are best interpreted by asserting that neutralizing antibodies bind to the F protein in virions interfering with its activation for fusion. Binding of nonneutralizing antibodies is not enough to block this step. In contrast, the peptide F478-516 or BMS-433771 must bind to F protein intermediates generated during virus-cell membrane fusion, blocking further development of this process.
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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.