ArticleActa crystallographica. Section D, Structural biology2016
Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses.
Article in Acta crystallographica. Section D, Structural biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Conserved Filovirus Proteins as Targets of Broad-Spectrum Antivirals.bioRxiv : the preprint server for biology · 2025Article
- Assembly and transport of filovirus nucleocapsids.PLoS pathogens · 2022Review
- Ebola Virus Inclusion Body Formation and RNA Synthesis Are Controlled by a Novel Domain of Nucleoprotein Interacting with VP35.Journal of virology · 2020Article
- Identification of RUVBL1 and RUVBL2 as Novel Cellular Interactors of the Ebola Virus Nucleoprotein.Viruses · 2019Article
- Recent advances in marburgvirus research.F1000Research · 2019Review
- 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
- 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
- Analysis of Ebola virus polymerase domains to find strain-specific differences and to gain insight on their pathogenicity.Virusdisease · 2016Article
- Neglected filoviruses.FEMS microbiology reviews · 2016Review
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7 authors.
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Abstract
The Filoviridae family of negative-sense, single-stranded RNA (ssRNA) viruses is comprised of two species of Marburgvirus (MARV and RAVV) and five species of Ebolavirus, i.e. Zaire (EBOV), Reston (RESTV), Sudan (SUDV), Taï Forest (TAFV) and Bundibugyo (BDBV). In each of these viruses the 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. It is tightly associated with the viral RNA in the nucleocapsid, and during the lifecycle of the virus is essential for transcription, RNA replication, genome packaging and nucleocapsid assembly prior to membrane encapsulation. The structure of the unique C-terminal globular domain of the NP from EBOV has recently been determined and shown to be structurally unrelated to any other known protein [Dziubańska et al. (2014), Acta Cryst. D70, 2420-2429]. In this paper, a study of the C-terminal domains from the NP from the remaining four species of Ebolavirus, as well as from the MARV strain of Marburgvirus, is reported. As expected, the crystal structures of the BDBV and TAFV proteins show high structural similarity to that from EBOV, while the MARV protein behaves like a molten globule with a core residual structure that is significantly different from that of the EBOV protein.
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