ArticleProceedings of the National Academy of Sciences of the United States of America2013
Architecture of respiratory syncytial virus revealed by electron cryotomography.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 140 papers.
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140 citing papers in PubMed.
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- Filamentous morphology of influenza A virus confers enhanced stability in aerosols.Nature communications · 2026Article
- Inhibition of host N-myristoylation compromises the infectivity of SARS-CoV-2 due to Golgi-bypassing egress.Nature communications · 2026Article
- Human telomerase reverse transcriptase supports respiratory syncytial virus replication.Communications biology · 2026Article
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- ZNRD2 Mediated Nucleoprotein Aggregation Impairs Respiratory Syncytial Virus Replication.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Article
- RSV vaccine development: advances and fusion protein-focused strategies.Frontiers in immunology · 2026Review
- Beyond Processing: Furin as a Central Hub in Viral Pathogenesis and Genetic Susceptibility.Biomolecules · 2025Review
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- Implications of morphological variation in influenza viruses.Microbiology and molecular biology reviews : MMBR · 2025Review
- RSV F evolution escapes some monoclonal antibodies but does not strongly erode neutralization by human polyclonal sera.Journal of virology · 2025Article
- Host RhoA Signaling Controls Filamentous vs. Spherical Morphogenesis and Cell-to-Cell Spread of RSV via Lipid Raft Localization: Host-Directed Antiviral Target.Microorganisms · 2025Article
- Advances in development of antiviral strategies against respiratory syncytial virus.Acta pharmaceutica Sinica. B · 2025Review
- RSV F evolution escapes some monoclonal antibodies but does not strongly erode neutralization by human polyclonal sera.bioRxiv : the preprint server for biology · 2025Article
- Influenza A virus rapidly adapts particle shape to environmental pressures.Nature microbiology · 2025Article
- Single-Particle Electron Microscopy Analysis of Respiratory Syncytial Virus Protein Complexes.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Introduction to Respiratory Syncytial Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
80 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
Human respiratory syncytial virus is a human pathogen that causes severe infection of the respiratory tract. Current information about the structure of the virus and its interaction with host cells is limited. We carried out an electron cryotomographic characterization of cell culture-grown human respiratory syncytial virus to determine the architecture of the virion. The particles ranged from 100 nm to 1,000 nm in diameter and were spherical, filamentous, or a combination of the two. The filamentous morphology correlated with the presence of a cylindrical matrix protein layer linked to the inner leaflet of the viral envelope and with local ordering of the glycoprotein spikes. Recombinant viruses with only the fusion protein in their envelope showed that these glycoproteins were predominantly in the postfusion conformation, but some were also in the prefusion form. The ribonucleocapsids were left-handed, randomly oriented, and curved inside the virions. In filamentous particles, they were often adjacent to an intermediate layer of protein assigned to M2-1 (an envelope-associated protein known to mediate association of ribonucleocapsids with the matrix protein). Our results indicate important differences in structure between the Paramyxovirinae and Pneumovirinae subfamilies within the Paramyxoviridae, and provide fresh insights into host cell exit of a serious pathogen.
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