ArticleActa crystallographica. Section D, Biological crystallography2014
The structure of the C-terminal domain of the Zaire ebolavirus nucleoprotein.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed, 42 citations in OpenAlex.
- Intracellular Ebola virus nucleocapsid assembly revealed by in situ cryo-electron tomography.Cell · 2024Article
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- 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
- Fragment screening targeting Ebola virus nucleoprotein C-terminal domain identifies lead candidates.Antiviral research · 2020Article
- Ebola Virus Inclusion Body Formation and RNA Synthesis Are Controlled by a Novel Domain of Nucleoprotein Interacting with VP35.Journal of virology · 2020Article
- Global phosphoproteomic analysis of Ebola virions reveals a novel role for VP35 phosphorylation-dependent regulation of genome transcription.Cellular and molecular life sciences : CMLS · 2020Article
- Backbone resonance assignments and secondary structure of Ebola nucleoprotein 600-739 construct.Biomolecular NMR assignments · 2019Article
- Review
- The structure of the C-terminal domain of the nucleoprotein from the Bundibugyo strain of the Ebola virus in complex with a pan-specific synthetic Fab.Acta crystallographica. Section D, Structural biology · 2018Article
- Article
- Crystal Structure of the Marburg Virus Nucleoprotein Core Domain Chaperoned by a VP35 Peptide Reveals a Conserved Drug Target for Filovirus.Journal of virology · 2017Article
- The lifecycle of the Ebola virus in host cells.Oncotarget · 2017Review
- Ebola virus VP30 and nucleoprotein interactions modulate viral RNA synthesis.Nature communications · 2017Article
- Unveiling a Drift Resistant Cryptotope withinFrontiers in immunology · 2017Article
- In vitro assembly of Ebola virus nucleocapsid-like complex expressed in E. coli.Protein & cell · 2016Article
- The Ebola Virus VP30-NP Interaction Is a Regulator of Viral RNA Synthesis.PLoS pathogens · 2016Article
- Article
- Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.Acta crystallographica. Section D, Structural biology · 2016Article
- Ebolavirus is evolving but not changing: No evidence for functional change in EBOV from 1976 to the 2014 outbreak.Virology · 2015Article
- Insight into the Ebola virus nucleocapsid assembly mechanism: crystal structure of Ebola virus nucleoprotein core domain at 1.8 Å resolution.Protein & cell · 2015Article
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5 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Ebolavirus (EBOV) causes severe hemorrhagic fever with a mortality rate of up to 90%. EBOV is a member of the order Mononegavirales and, like other viruses in this taxonomic group, contains a negative-sense single-stranded (ss) RNA. The EBOV ssRNA encodes seven distinct proteins. One of them, the nucleoprotein (NP), is the most abundant viral protein in the infected cell and within the viral nucleocapsid. Like other EBOV proteins, NP is multifunctional. It is tightly associated with the viral genome and is essential for viral transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. NP is unusual among the Mononegavirales in that it contains two distinct regions, or putative domains, the C-terminal of which shows no homology to any known proteins and is purported to be a hub for protein-protein interactions within the nucleocapsid. The atomic structure of NP remains unknown. Here, the boundaries of the N- and C-terminal domains of NP from Zaire EBOV are defined, it is shown that they can be expressed as highly stable recombinant proteins in Escherichia coli, and the atomic structure of the C-terminal domain (residues 641-739) derived from analysis of two distinct crystal forms at 1.98 and 1.75 Å resolution is described. The structure reveals a novel tertiary fold that is distantly reminiscent of the β-grasp architecture.
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