Nucleocapsid formation and RNA synthesis of Marburg virus is dependent on two coiled coil motifs in the nucleoprotein
dc.contributor.author | DiCarlo, Andrea | |
dc.contributor.author | Möller, Peggy | |
dc.contributor.author | Lander, Angelika | |
dc.contributor.author | Kolesnikova, Larissa | |
dc.contributor.author | Becker, Stephan | |
dc.date.accessioned | 2018-05-07T18:17:20Z | |
dc.date.available | 2018-05-07T18:17:20Z | |
dc.date.created | 2015-06-09 | |
dc.date.issued | 2007-10-24 | none |
dc.identifier.other | http://edoc.rki.de/oa/articles/reXQJaA67x4zE/PDF/26OnkJBMNyYsc.pdf | |
dc.identifier.uri | http://edoc.rki.de/176904/2076 | |
dc.description.abstract | The nucleoprotein (NP) of Marburg virus (MARV) is responsible for the encapsidation of viral genomic RNA and the formation of the helical nucleocapsid precursors that accumulate in intracellular inclusions in infected cells. To form the large helical MARV nucleocapsid, NP needs to interact with itself and the viral proteins VP30, VP35 and L, which are also part of the MARV nucleocapsid. In the present study, a conserved coiled coil motif in the central part of MARV NP was shown to be an important element for the interactions of NP with itself and VP35, the viral polymerase cofactor. Additionally, the coiled coil motif was essential for the formation of NP-induced intracellular inclusions and for the function of NP in the process of transcription and replication of viral RNA in a minigenome system. Transfer of the coiled coil motif to a reporter protein was sufficient to mediate interaction of the constructed fusion protein with the N-terminus of NP. The coiled coil motif is bipartite, constituted by two coiled coils which are separated by a flexible linker. | eng |
dc.language.iso | eng | |
dc.publisher | Robert Koch-Institut, Biologische Sicherheit | |
dc.subject | Humans | eng |
dc.subject | RNA Viral/genetics | eng |
dc.subject | Conserved Sequence | eng |
dc.subject | HeLa Cells | eng |
dc.subject | Marburgvirus/genetics | eng |
dc.subject | Marburgvirus/physiology | eng |
dc.subject | Nucleocapsid Proteins/chemistry | eng |
dc.subject | Nucleocapsid Proteins/physiology | eng |
dc.subject | Nucleoproteins/chemistry | eng |
dc.subject | Nucleoproteins/physiology | eng |
dc.subject | RNA Viral/biosynthesis | eng |
dc.subject | Transcription Genetic | eng |
dc.subject | Viral Proteins/physiology | eng |
dc.subject.ddc | 610 Medizin | |
dc.title | Nucleocapsid formation and RNA synthesis of Marburg virus is dependent on two coiled coil motifs in the nucleoprotein | |
dc.type | periodicalPart | |
dc.identifier.urn | urn:nbn:de:0257-10039676 | |
dc.identifier.doi | 10.1186/1743-422X-4-105 | |
dc.identifier.doi | http://dx.doi.org/10.25646/2001 | |
local.edoc.container-title | Virology Journal | |
local.edoc.fp-subtype | Artikel | |
local.edoc.type-name | Zeitschriftenartikel | |
local.edoc.container-type | periodical | |
local.edoc.container-type-name | Zeitschrift | |
local.edoc.container-url | http://www.virologyj.com/content/4/1/105 | |
local.edoc.container-publisher-name | BioMedCentral | |
local.edoc.container-volume | 4 | |
local.edoc.container-issue | 105 | |
local.edoc.container-year | 2007 |