ArticleCell reports2015
An Intrinsically Disordered Peptide from Ebola Virus VP35 Controls Viral RNA Synthesis by Modulating Nucleoprotein-RNA Interactions.
Article in Cell reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 104 papers.
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Who cites it
104 citing papers in PubMed, 164 citations in OpenAlex.
- Molecular Insights into High-Pathogenicity RNA Viruses.Viruses · 2026Review
- Structure and assembly of Borna disease virus 1 nucleoprotein-RNA complexes.Science advances · 2026Article
- Article
- Sequence-Dependent Heterotypic Assemblies of Intrinsically Disordered Peptides.ChemistryEurope · 2026Article
- Discovery of three small-molecule inhibitors targetingThe Journal of general virology · 2025Article
- Molecular insights into nucleocapsid assembly and transport in Marburg and Ebola viruses.mBio · 2025Article
- 25 Years of Ebola Virus VP35 Research.Journal of molecular biology · 2025Review
- Ebola virus VP35 NNLNS motif modulates viral RNA synthesis and MIB2-mediated signaling.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- How Can Plant-Derived Natural Products and Plant Biotechnology Help Against Emerging Viruses?International journal of molecular sciences · 2025Review
- Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.Cell · 2024Article
- How does the polymerase of non-segmented negative strand RNA viruses commit to transcription or genome replication?Journal of virology · 2024Review
- 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
- Single-cell image-based genetic screens systematically identify regulators of Ebola virus subcellular infection dynamics.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
- Disruption of Ebola NPJournal of molecular biology · 2023Article
- Novel Antiviral Molecules against Ebola Virus Infection.International journal of molecular sciences · 2023Article
- Spatial and functional arrangement of Ebola virus polymerase inside phase-separated viral factories.Nature communications · 2023Article
- Modular characterization of SARS-CoV-2 nucleocapsid protein domain functions in nucleocapsid-like assembly.Molecular biomedicine · 2023Article
- Cryoelectron microscopic structure of the nucleoprotein-RNA complex of the European filovirus, Lloviu virus.PNAS nexus · 2023Article
44 more citing papers are in PubMed but not listed here.
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Authors and funding
16 authors at 5 institutions in 1 country.
Funding
Abstract
During viral RNA synthesis, Ebola virus (EBOV) nucleoprotein (NP) alternates between an RNA-template-bound form and a template-free form to provide the viral polymerase access to the RNA template. In addition, newly synthesized NP must be prevented from indiscriminately binding to noncognate RNAs. Here, we investigate the molecular bases for these critical processes. We identify an intrinsically disordered peptide derived from EBOV VP35 (NPBP, residues 20-48) that binds NP with high affinity and specificity, inhibits NP oligomerization, and releases RNA from NP-RNA complexes in vitro. The structure of the NPBP/ΔNPNTD complex, solved to 3.7 Å resolution, reveals how NPBP peptide occludes a large surface area that is important for NP-NP and NP-RNA interactions and for viral RNA synthesis. Together, our results identify a highly conserved viral interface that is important for EBOV replication and can be targeted for therapeutic development.
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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 OpenQuestion graph.