ArticleProceedings of the National Academy of Sciences of the United States of America2018
Ebola virus proteins NP, VP35, and VP24 are essential and sufficient to mediate nucleocapsid transport.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 77 citations in OpenAlex.
- Molecular Insights into High-Pathogenicity RNA Viruses.Viruses · 2026Review
- Platelet-like particles released from Ebola virus-infected megakaryocytic cells behave like virus-like particles.PLoS pathogens · 2026Article
- Molecular responses of human retinal pigment epithelial cells to ebolavirus VP24.Molecular vision · 2026Article
- Drug Repurposing Investigation for Combating Ebola Virus Disease: Database Mining, Docking Calculations, Molecular Dynamics, and Density Functional Theory Study.ChemistryOpen · 2025Article
- Molecular insights into nucleocapsid assembly and transport in Marburg and Ebola viruses.mBio · 2025Article
- Direct Intercellular Transport Mode of Filovirus Nucleocapsids.International journal of molecular sciences · 2025Article
- Article
- How Can Plant-Derived Natural Products and Plant Biotechnology Help Against Emerging Viruses?International journal of molecular sciences · 2025Review
- Autographa californica multiple nucleopolyhedrovirus Ac51 interacts with Ac66 and facilitates its nuclear localization to promote the nuclear egress of nucleocapsids.Journal of virology · 2025Article
- Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24.Nature communications · 2025Article
- Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.Cell · 2024Article
- Identification of Prospective Ebola Virus VP35 and VP40 Protein Inhibitors from Myxobacterial Natural Products.Biomolecules · 2024Article
- Molecular insights into the Ebola virus life cycle.Nature microbiology · 2024Review
- Impact of Ebola virus nucleoprotein on VP40 virus-like particle production: a computational approach.Communications biology · 2024Article
- The Role of Ebola Virus VP24 Nuclear Trafficking Signals in Infectious Particle Production.bioRxiv : the preprint server for biology · 2024Article
- Ebola virus inclusion bodies are liquid organelles whose formation is facilitated by nucleoprotein oligomerization.Emerging microbes & infections · 2023Article
- Ebola Virus Uses Tunneling Nanotubes as an Alternate Route of Dissemination.The Journal of infectious diseases · 2023Article
- Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories.Nature communications · 2023Article
- The Ebola virus VP40 matrix layer undergoes endosomal disassembly essential for membrane fusion.The EMBO journal · 2023Article
- Extracellular vesicle storm during the course of Ebola virus infection in primates.Frontiers in cellular and infection microbiology · 2023Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The intracytoplasmic movement of nucleocapsids is a crucial step in the life cycle of enveloped viruses. Determination of the viral components necessary for viral nucleocapsid transport competency is complicated by the dynamic and complex nature of nucleocapsid assembly and the lack of appropriate model systems. Here, we established a live-cell imaging system based on the ectopic expression of fluorescent Ebola virus (EBOV) fusion proteins, allowing the visualization and analysis of the movement of EBOV nucleocapsid-like structures with different protein compositions. Only three of the five EBOV nucleocapsid proteins-nucleoprotein, VP35, and VP24-were necessary and sufficient to form transport-competent nucleocapsid-like structures. The transport of these structures was found to be dependent on actin polymerization and to have dynamics that were undistinguishable from those of nucleocapsids in EBOV-infected cells. The intracytoplasmic movement of nucleocapsid-like structures was completely independent of the viral matrix protein VP40 and the viral surface glycoprotein GP. However, VP40 greatly enhanced the efficiency of nucleocapsid recruitment into filopodia, the sites of EBOV budding.
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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 Socratic graph.