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Molecular architecture of the nucleoprotein C‐terminal domain from the Ebola and Marburg viruses
Author(s) -
Baker Laura E.,
Ellena Jeffrey F.,
Handing Katarzyna B.,
Derewenda Urszula,
Utepbergenov Darkhan,
Engel Daniel A.,
Derewenda Zygmunt S.
Publication year - 2016
Publication title -
acta crystallographica section d
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.374
H-Index - 138
ISSN - 2059-7983
DOI - 10.1107/s2059798315021439
Subject(s) - nucleoprotein , filoviridae , marburg virus , ebola virus , virology , ebolavirus , vp40 , rna , biology , lassa virus , virus , gene , genetics , paramyxoviridae , viral disease
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 . D 70 , 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.