Molecular architecture of the nucleoprotein C‐terminal domain from the Ebola and Marburg viruses. Issue 1 (1st January 2016)

• Record Type: Journal Article
• Authors: Baker, Laura E.; Ellena, Jeffrey F.; Handing, Katarzyna B.; Derewenda, Urszula; Utepbergenov, Darkhan; Engel, Daniel A.; Derewenda, Zygmunt S.
• Is Part Of: Acta crystallographica. Volume 72:Issue 1(2016)
• Page Start: 49
• Page End: 58
• Publication Date: 2016-01-01
• Subjects: viral proteins viral proteins -- Ebolavirus Ebolavirus -- Marburgvirus Marburgvirus -- nucleoprotein nucleoprotein -- Filoviridae Filoviridae; X-ray crystallography -- Periodicals; Crystallography -- Periodicals; Molecular biology -- Periodicals; Molecular structure -- Periodicals; Biomolecules -- Structure -- Periodicals; Cytology -- Periodicals; Biomolecules -- Structure; Crystallography; Cytology; Molecular biology; Molecular structure; X-ray crystallography; Periodicals; 548
• DOI: 10.1107/S2059798315021439
• Languages: English
• ISSNs: 2059-7983

Abstract

Abstract : Crystal structures of the C‐terminal domains of the Ebolavirus Ebolavirus nucleoproteins (NP Ct Ct ) from the Bundibugyo and Taï Forest species (BDBV and TAFV, respectively) have been determined. The structures show high similarity to that reported for the Zaire Ebolavirus Ebolavirus NP Ct Ct . However, NMR data revealed that the corresponding domain from the NP of the related MARV species of Marburgvirus Marburgvirus is distinctly different. Abstract : The Filoviridae Filoviridae family of negative‐sense, single‐stranded RNA (ssRNA) viruses is comprised of two species of Marburgvirus Marburgvirus (MARV and RAVV) and five species of Ebolavirus Ebolavirus, i.e. 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. et al. (2014), Acta Cryst Acta Cryst . D70 70, 2420–2429]. In this paper, a study of the C‐terminal domains from the NP from the remaining four species of Ebolavirus Ebolavirus, as well as from the MARV strain of Marburgvirus 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.