ArticleJournal of virology2011
Recombinant Sendai viruses expressing fusion proteins with two furin cleavage sites mimic the syncytial and receptor-independent infection properties of respiratory syncytial virus.
Article in Journal of virology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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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
20 citing papers in PubMed, 35 citations in OpenAlex.
- Novel requirements for HAP2/GCS1-mediated gamete fusion iniScience · 2024Article
- Cleavage of the syncytial protein of J paramyxovirus is required for its ability to promote cell-cell fusion.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Entry of Enveloped Viruses into Host Cells: Membrane Fusion.Sub-cellular biochemistry · 2024Review
- The RSV F p27 peptide: current knowledge, important questions.Frontiers in microbiology · 2023Review
- Article
- Cell-Cell Fusion Mediated by Viruses and HERV-Derived Fusogens in Cancer Initiation and Progression.Cancers · 2021Review
- Cell Fusion-Mediated Tissue Regeneration as an Inducer of Polyploidy and Aneuploidy.International journal of molecular sciences · 2020Review
- The Proteolytic Regulation of Virus Cell Entry by Furin and Other Proprotein Convertases.Viruses · 2019Review
- Structural, antigenic and immunogenic features of respiratory syncytial virus glycoproteins relevant for vaccine development.Vaccine · 2017Review
- Use of single chain antibody derivatives for targeted drug delivery.Molecular medicine (Cambridge, Mass.) · 2016Article
- Engineering, Structure and Immunogenicity of the Human Metapneumovirus F Protein in the Postfusion Conformation.PLoS pathogens · 2016Article
- Review
- Evidence for ubiquitin-regulated nuclear and subnuclear trafficking among Paramyxovirinae matrix proteins.PLoS pathogens · 2015Article
- Entry of enveloped viruses into host cells: membrane fusion.Sub-cellular biochemistry · 2013Review
- Respiratory syncytial virus: virology, reverse genetics, and pathogenesis of disease.Current topics in microbiology and immunology · 2013Article
- Fusion activation by a headless parainfluenza virus 5 hemagglutinin-neuraminidase stalk suggests a modular mechanism for triggering.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Progress in understanding and controlling respiratory syncytial virus: still crazy after all these years.Virus research · 2011Review
- Residues of the human metapneumovirus fusion (F) protein critical for its strain-related fusion phenotype: implications for the virus replication cycle.Journal of virology · 2011Article
- Viruslike particle vaccine induces protection against respiratory syncytial virus infection in mice.The Journal of infectious diseases · 2011Article
- Mechanisms of Oncolysis by Paramyxovirus Sendai.Acta naturaeArticle
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cell entry by paramyxoviruses requires fusion between viral and cellular membranes. Paramyxovirus infection also gives rise to the formation of multinuclear, fused cells (syncytia). Both types of fusion are mediated by the viral fusion (F) protein, which requires proteolytic processing at a basic cleavage site in order to be active for fusion. In common with most paramyxoviruses, fusion mediated by Sendai virus F protein (F(SeV)) requires coexpression of the homologous attachment (hemagglutinin-neuraminidase [HN]) protein, which binds to cell surface sialic acid receptors. In contrast, respiratory syncytial virus fusion protein (F(RSV)) is capable of fusing membranes in the absence of the viral attachment (G) protein. Moreover, F(RSV) is unique among paramyxovirus fusion proteins since F(RSV) possesses two multibasic cleavage sites, which are separated by an intervening region of 27 amino acids. We have previously shown that insertion of both F(RSV) cleavage sites in F(SeV) decreases dependency on the HN attachment protein for syncytium formation in transfected cells. We now describe recombinant Sendai viruses (rSeV) that express mutant F proteins containing one or both F(RSV) cleavage sites. All cleavage-site mutant viruses displayed reduced thermostability, with double-cleavage-site mutants exhibiting a hyperfusogenic phenotype in infected cells. Furthermore, insertion of both F(RSV) cleavage sites in F(SeV) reduced dependency on the interaction of HN with sialic acid for infection, thus mimicking the unique ability of RSV to fuse and infect cells in the absence of a separate attachment protein.
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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.