ArticleProtein & cell2022
The two-stage interaction of Ebola virus VP40 with nucleoprotein results in a switch from viral RNA synthesis to virion assembly/budding.
Article in Protein & cell, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 18 citations in OpenAlex.
- Self-adjuvanting Ebola virus-like particles that incorporate a cellular interferon-inducing domain.Research square · 2026Article
- Molecular Insights into High-Pathogenicity RNA Viruses.Viruses · 2026Review
- Engineering Microbial Particles for Next-Generation Biomedical Platforms.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Integrated Metabolomic and Transcriptomic Analysis Reveals Host Response Mechanisms to Porcine Epidemic Diarrhea Virus Infection in Pigs.Veterinary sciences · 2026Article
- Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.Cell · 2024Article
- Article
- Impact of Ebola virus nucleoprotein on VP40 virus-like particle production: a computational approach.Communications biology · 2024Article
- Navigating the Complex Landscape of Ebola Infection Treatment: A Review of Emerging Pharmacological Approaches.Infectious diseases and therapy · 2024Review
- Ebola Virus Infection Induces HCAR2 Expression Leading to Cell Death.The Journal of infectious diseases · 2023Article
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- A Comparative NLP-Based Study on the Current Trends and Future Directions in COVID-19 Research.IEEE access : practical innovations, open solutions · 2021Article
Corrections and comments
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ebola virus (EBOV) is an enveloped negative-sense RNA virus and a member of the filovirus family. Nucleoprotein (NP) expression alone leads to the formation of inclusion bodies (IBs), which are critical for viral RNA synthesis. The matrix protein, VP40, not only plays a critical role in virus assembly/budding, but also can regulate transcription and replication of the viral genome. However, the molecular mechanism by which VP40 regulates viral RNA synthesis and virion assembly/budding is unknown. Here, we show that within IBs the N-terminus of NP recruits VP40 and is required for VLP-containing NP release. Furthermore, we find four point mutations (L692A, P697A, P698A and W699A) within the C-terminal hydrophobic core of NP result in a stronger VP40-NP interaction within IBs, sequestering VP40 within IBs, reducing VP40-VLP egress, abolishing the incorporation of NC-like structures into VP40-VLP, and inhibiting viral RNA synthesis, suggesting that the interaction of N-terminus of NP with VP40 induces a conformational change in the C-terminus of NP. Consequently, the C-terminal hydrophobic core of NP is exposed and binds VP40, thereby inhibiting RNA synthesis and initiating virion assembly/budding.
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