ArticleNucleic acids research2019
Ebola virus VP35 has novel NTPase and helicase-like activities.
Article in Nucleic acids research, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 47 citations in OpenAlex.
- Towards broader-spectrum direct-acting antivirals against RNA viruses.Nature reviews. Microbiology · 2026Review
- A new role for an old player: The rabies virus phosphoprotein as an RNA chaperone, helicase, and immune evasion hub.Molecular therapy. Nucleic acids · 2026Article
- Rabies lyssavirus phosphoprotein possesses RNA duplex-unwinding activities.Molecular therapy. Nucleic acids · 2026Article
- Ebola virus disease: A persistent challenge in global health security.Open veterinary journal · 2026Review
- 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025Review
- Respiratory syncytial virus phosphoprotein has NTPase and helicase-like activities.Journal of virology · 2025Article
- How Can Plant-Derived Natural Products and Plant Biotechnology Help Against Emerging Viruses?International journal of molecular sciences · 2025Review
- The replication protein of duck circovirus unwinds dsDNA in an ATP-driven and metal ion-dependent manner from 3' to 5'.Frontiers in veterinary science · 2025Article
- The regulatory roles of STAT3 protein in the pathogenesis of viral infections.Frontiers in cellular and infection microbiology · 2025Review
- 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
- Picornavirus 2C proteins: structure-function relationships and interactions with host factors.Frontiers in cellular and infection microbiology · 2024Review
- Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories.Nature communications · 2023Article
- Article
- Ebola and Marburg virus VP35 coiled-coil validated as antiviral target by tripartite split-GFP complementation.iScience · 2022Article
- The nonstructural protein 2C of Coxsackie B virus has RNA helicase and chaperoning activities.Virologica Sinica · 2022Article
- Ubiquitination of Ebola virus VP35 at lysine 309 regulates viral transcription and assembly.PLoS pathogens · 2022Article
- Ebola virus VP35 hijacks the PKA-CREB1 pathway for replication and pathogenesis by AKIP1 association.Nature communications · 2022Article
- DistinctiveFrontiers in plant science · 2022Article
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
11 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Ebola virus (EBOV) is a non-segmented, negative-sense RNA virus (NNSV) in the family Filoviridae, and is recognized as one of the most lethal pathogens in the planet. For RNA viruses, cellular or virus-encoded RNA helicases play pivotal roles in viral life cycles by remodelling viral RNA structures and/or unwinding viral dsRNA produced during replication. However, no helicase or helicase-like activity has ever been found to associate with any NNSV-encoded proteins, and it is unknown whether the replication of NNSVs requires the participation of any viral or cellular helicase. Here, we show that despite of containing no conserved NTPase/helicase motifs, EBOV VP35 possesses the NTPase and helicase-like activities that can hydrolyse all types of NTPs and unwind RNA helices in an NTP-dependent manner, respectively. Moreover, guanidine hydrochloride, an FDA-approved compound and inhibitor of certain viral helicases, inhibited the NTPase and helicase-like activities of VP35 as well as the replication/transcription of an EBOV minigenome replicon in cells, highlighting the importance of VP35 helicase-like activity during EBOV life cycle. Together, our findings provide the first demonstration of the NTPase/helicase-like activity encoded by EBOV, and would foster our understanding of EBOV and NNSVs.
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