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dc.contributor.authorvan Knippenberg, Ingeborg
dc.contributor.authorFragkoudis, Rennos
dc.contributor.authorElliott, Richard M.
dc.date.accessioned2013-08-05T14:31:04Z
dc.date.available2013-08-05T14:31:04Z
dc.date.issued2013-05-08
dc.identifier.citationvan Knippenberg , I , Fragkoudis , R & Elliott , R M 2013 , ' The transient nature of bunyamwera orthobunyavirus NSs protein expression : effects of increased stability of NSs protein on virus replication ' PLoS One , vol. 8 , no. 5 , 64137 . DOI: 10.1371/journal.pone.0064137en
dc.identifier.issn1932-6203
dc.identifier.otherPURE: 62947300
dc.identifier.otherPURE UUID: 1cdaa433-e103-435c-a45f-8489955e3237
dc.identifier.otherWOS: 000319055600086
dc.identifier.otherScopus: 84877291633
dc.identifier.urihttp://hdl.handle.net/10023/3914
dc.description.abstractThe NSs proteins of bunyaviruses are the viral interferon antagonists, counteracting the host's antiviral response to infection. During high-multiplicity infection of cultured mammalian cells with Bunyamwera orthobunyavirus (BUNV), NSs is rapidly degraded after reaching peak levels of expression at 12hpi. Through the use of inhibitors this was shown to be the result of proteasomal degradation. A recombinant virus (rBUN4KR), in which all four lysine residues in NSs were replaced by arginine residues, expresses an NSs protein (NSs4KR) that is resistant to degradation, confirming that degradation is lysine-dependent. However, despite repeated attempts, no direct ubiquitylation of NSs in infected cells could be demonstrated. This suggests that degradation of NSs, although lysine-dependent, may be achieved through an indirect mechanism. Infection of cultured mammalian cells or mice indicated no disadvantage for the virus in having a non-degradable NSs protein: in fact rBUN4KR had a slight growth advantage over wtBUNV in interferon-competent cells, presumably due to the increased and prolonged presence of NSs. In cultured mosquito cells there was no difference in growth between wild-type BUNV and rBUN4KR, but surprisingly NSs4KR was not stabilised compared to the wild-type NSs protein.en
dc.format.extent10en
dc.language.isoeng
dc.relation.ispartofPLoS Oneen
dc.rights© 2013 van Knippenberg et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.en
dc.subjectInterferon regulatorY FACTOR-3en
dc.subjectUbiquitin-proteasome systemen
dc.subjectCultured-cellsen
dc.subjectMosquito cellsen
dc.subjectInhibitionen
dc.subjectInductionen
dc.subjectProducten
dc.subjectSTAT2en
dc.subjectPhosphorylationen
dc.subjectParamyxovirusesen
dc.subjectQR355 Virologyen
dc.subject.lccQR355en
dc.titleThe transient nature of bunyamwera orthobunyavirus NSs protein expression : effects of increased stability of NSs protein on virus replicationen
dc.typeJournal articleen
dc.description.versionPublisher PDFen
dc.contributor.institutionUniversity of St Andrews. School of Biologyen
dc.contributor.institutionUniversity of St Andrews. Biomedical Sciences Research Complexen
dc.identifier.doihttps://doi.org/10.1371/journal.pone.0064137
dc.description.statusPeer revieweden


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