ArticlePLoS pathogens2016
The Ebola Virus VP30-NP Interaction Is a Regulator of Viral RNA Synthesis.
Article in PLoS pathogens, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
49 citing papers in PubMed.
- The development of biologically contained Sudan virus as an alternative and safe tool for fundamental filovirus research.Emerging microbes & infections · 2026Article
- Host-virus determinants of Ebola virus persistence in a human cerebral organoid model.Nature microbiology · 2026Article
- AI-Driven Discovery and BSL-4 Validation of Cross-Filovirus Ebola-Marburg Inhibitors and their Synergistic Combinations.bioRxiv : the preprint server for biology · 2026Article
- Development of VP30-targeted nanoparticles using DPS4 fusion peptides for the inhibition of Ebola virus.Journal of nanobiotechnology · 2026Article
- Review
- 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
- Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 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
- The cellular protein phosphatase 2A is a crucial host factor for Marburg virus transcription.Journal of virology · 2024Article
- Impact of Ebola virus nucleoprotein on VP40 virus-like particle production: a computational approach.Communications biology · 2024Article
- Identification of motif-based interactions between SARS-CoV-2 protein domains and human peptide ligands pinpoint antiviral targets.Nature communications · 2023Article
- Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories.Nature communications · 2023Article
- Serine-arginine protein kinases and their targets in viral infection and their inhibition.Cellular and molecular life sciences : CMLS · 2023Review
- Role of VP30 Phosphorylation in Ebola Virus Nucleocapsid Assembly and Transport.Journal of virology · 2022Article
- CAPG Is Required for Ebola Virus Infection by Controlling Virus Egress from Infected Cells.Viruses · 2022Article
- The two-stage interaction of Ebola virus VP40 with nucleoprotein results in a switch from viral RNA synthesis to virion assembly/budding.Protein & cell · 2022Article
- Structural and Functional Aspects of Ebola Virus Proteins.Pathogens (Basel, Switzerland) · 2021Review
- Non-canonical proline-tyrosine interactions with multiple host proteins regulate Ebola virus infection.The EMBO journal · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
Filoviruses are capable of causing deadly hemorrhagic fevers. All nonsegmented negative-sense RNA-virus nucleocapsids are composed of a nucleoprotein (NP), a phosphoprotein (VP35) and a polymerase (L). However, the VP30 RNA-synthesis co-factor is unique to the filoviruses. The assembly, structure, and function of the filovirus RNA replication complex remain unclear. Here, we have characterized the interactions of Ebola, Sudan and Marburg virus VP30 with NP using in vitro biochemistry, structural biology and cell-based mini-replicon assays. We have found that the VP30 C-terminal domain interacts with a short peptide in the C-terminal region of NP. Further, we have solved crystal structures of the VP30-NP complex for both Ebola and Marburg viruses. These structures reveal that a conserved, proline-rich NP peptide binds a shallow hydrophobic cleft on the VP30 C-terminal domain. Structure-guided Ebola virus VP30 mutants have altered affinities for the NP peptide. Correlation of these VP30-NP affinities with the activity for each of these mutants in a cell-based mini-replicon assay suggests that the VP30-NP interaction plays both essential and inhibitory roles in Ebola virus RNA synthesis.
Indexed as
Identifiers
What OpenQuestion holds
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.