Molecular architecture of the nucleoprotein C-terminal domain from the Ebola and Marburg viruses
| Autor: | Urszula Derewenda, Jeffrey F. Ellena, Laura E. Baker, Daniel A. Engel, Katarzyna B. Handing, Darkhan Utepbergenov, Zygmunt S. Derewenda |
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| Rok vydání: | 2016 |
| Předmět: |
Models
Molecular 0301 basic medicine Protein Conformation Viral protein Molecular Sequence Data Filoviridae Crystallography X-Ray medicine.disease_cause Viral Proteins 03 medical and health sciences Structural Biology Marburg virus disease medicine Animals Marburg Virus Disease Amino Acid Sequence Ebolavirus biology Viral nucleocapsid RNA Hemorrhagic Fever Ebola biology.organism_classification Marburgvirus Research Papers Virology Nucleoprotein Nucleoproteins 030104 developmental biology Sequence Alignment |
| Zdroj: | Acta Crystallographica Section D Structural Biology. 72:49-58 |
| ISSN: | 2059-7983 |
| DOI: | 10.1107/s2059798315021439 |
| Popis: | TheFiloviridaefamily of negative-sense, single-stranded RNA (ssRNA) viruses is comprised of two species ofMarburgvirus(MARV and RAVV) and five species ofEbolavirus,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 [Dziubańskaet 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 ofEbolavirus, as well as from the MARV strain ofMarburgvirus, 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. |
| Databáze: | OpenAIRE |
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