ArticleThe EMBO journal2022
Helical ordering of envelope-associated proteins and glycoproteins in respiratory syncytial virus.
Article in The EMBO journal, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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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
27 citing papers in PubMed, 43 citations in OpenAlex.
- Open and closed forms of assembled henipavirus nucleoprotein suggest structural basis of genome access.Science advances · 2026Article
- Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes.Science advances · 2026Article
- Prophylactic monoclonal antibodies against respiratory syncytial virus in early life: An in-depth review of mechanisms of action, failure factors, and future perspectives.Pediatric allergy and immunology : official publication of the European Society of Pediatric Allergy and Immunology · 2025Review
- The GATE glycoprotein complex enhances human cytomegalovirus entry in endothelial cells.Nature microbiology · 2025Article
- Introduction to Respiratory Syncytial Virus.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Antagonism of BST2/Tetherin, a new restriction factor of respiratory syncytial virus, requires the viral NS1 protein.PLoS pathogens · 2024Article
- Integrating immunoinformatics and computational epitope prediction for a vaccine candidate against respiratory syncytial virus.Infectious Disease Modelling · 2024Article
- Assembly of respiratory syncytial virus matrix protein lattice and its coordination with fusion glycoprotein trimers.Nature communications · 2024Article
- The cryoEM structure of the Hendra henipavirus nucleoprotein reveals insights into paramyxoviral nucleocapsid architectures.Scientific reports · 2024Article
- Review
- Structure of the N-RNA/P interface indicates mode of L/P recruitment to the nucleocapsid of human metapneumovirus.Nature communications · 2023Article
- Respiratory syncytial virus infection and novel interventions.Nature reviews. Microbiology · 2023Review
- Correlative montage parallel array cryo-tomography for in situ structural cell biology.Nature methods · 2023Article
- The road to approved vaccines for respiratory syncytial virus.NPJ vaccines · 2023Review
- Cryo-electron tomography to study viral infection.Biochemical Society transactions · 2023Review
- Cryo-EM structure of the nucleocapsid-like assembly of respiratory syncytial virus.Signal transduction and targeted therapy · 2023Article
- Review
- Optimal Conditions for In Vitro Assembly of Respiratory Syncytial Virus Nucleocapsid-like Particles.Viruses · 2023Article
- Biochemistry of the Respiratory Syncytial Virus L Protein Embedding RNA Polymerase and Capping Activities.Viruses · 2023Review
- In Situ Imaging of Virus-Infected Cells by Cryo-Electron Tomography: An Overview.Sub-cellular biochemistry · 2023Review
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 2 countries.
Funding
Abstract
Human respiratory syncytial virus (RSV) causes severe respiratory illness in children and the elderly. Here, using cryogenic electron microscopy and tomography combined with computational image analysis and three-dimensional reconstruction, we show that there is extensive helical ordering of the envelope-associated proteins and glycoproteins of RSV filamentous virions. We calculated a 16 Å resolution sub-tomogram average of the matrix protein (M) layer that forms an endoskeleton below the viral envelope. These data define a helical lattice of M-dimers, showing how M is oriented relative to the viral envelope. Glycoproteins that stud the viral envelope were also found to be helically ordered, a property that was coordinated by the M-layer. Furthermore, envelope glycoproteins clustered in pairs, a feature that may have implications for the conformation of fusion (F) glycoprotein epitopes that are the principal target for vaccine and monoclonal antibody development. We also report the presence, in authentic virus infections, of N-RNA rings packaged within RSV virions. These data provide molecular insight into the organisation of the virion and the mechanism of its assembly.
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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.