ArticleJournal of virology2020
The Integrity of the YxxL Motif of Ebola Virus VP24 Is Important for the Transport of Nucleocapsid-Like Structures and for the Regulation of Viral RNA Synthesis.
Article in Journal of virology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 20 citations in OpenAlex.
- To be or not to be phosphorylated: understanding the role of Ebola virus nucleoprotein in the dynamic interplay with the transcriptional activator VP30 and the host phosphatase PP2A-B56.Emerging microbes & infections · 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
- Structural basis for Ebola virus nucleocapsid assembly and function regulated by VP24.Nature communications · 2025Article
- The Role of Ebola Virus VP24 Nuclear Trafficking Signals in Infectious Particle Production.bioRxiv : the preprint server for biology · 2024Article
- High-efficiency genetic engineering toolkit for virus based on lambda red-mediated recombination.Biotechnology letters · 2023Article
- Article
- Exosomal transmission of viruses, a two-edged biological sword.Cell communication and signaling : CCS · 2023Review
- Role of VP30 Phosphorylation in Ebola Virus Nucleocapsid Assembly and Transport.Journal of virology · 2022Article
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- Ubiquitination of Ebola virus VP35 at lysine 309 regulates viral transcription and assembly.PLoS pathogens · 2022Article
- New Perspectives on the Biogenesis of Viral Inclusion Bodies in Negative-Sense RNA Virus Infections.Cells · 2021Review
- Article
- Ebola Virus Nucleocapsid-Like Structures Utilize Arp2/3 Signaling for Intracellular Long-Distance Transport.Cells · 2020Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
While it is well appreciated that late domains in the viral matrix proteins are crucial to mediate efficient virus budding, little is known about roles of late domains in the viral nucleocapsid proteins. Here, we characterized the functional relevance of a YxxL motif with potential late-domain function in the Ebola virus nucleocapsid protein VP24. Mutations in the YxxL motif had two opposing effects on the functions of VP24. On the one hand, the mutation affected the regulatory function of VP24 in viral RNA transcription and replication, which correlated with an increased incorporation of minigenomes into released transcription- and replication-competent virus-like particles (trVLPs). Consequently, cells infected with those trVLPs showed higher levels of viral transcription. On the other hand, mutations of the YxxL motif greatly impaired the intracellular transport of nucleocapsid-like structures (NCLSs) composed of the viral proteins NP, VP35, and VP24 and the length of released trVLPs. Attempts to rescue recombinant Ebola virus expressing YxxL-deficient VP24 failed, underlining the importance of this motif for the viral life cycle.
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