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dc.contributor.authorLinnik, Olga
dc.contributor.authorLiesche, Johannes
dc.contributor.authorTilsner, Jens
dc.contributor.authorOparka, Karl J.
dc.date.accessioned2013-05-30T11:31:01Z
dc.date.available2013-05-30T11:31:01Z
dc.date.issued2013-01-31
dc.identifier.citationLinnik , O , Liesche , J , Tilsner , J & Oparka , K J 2013 , ' Unravelling the structure of viral replication complexes at super-resolution ' , Frontiers in Plant Science , vol. 4 , 6 . https://doi.org/10.3389/fpls.2013.00006en
dc.identifier.otherPURE: 42962449
dc.identifier.otherPURE UUID: 1eaac5a8-3fa9-4e99-8e13-1982f399de30
dc.identifier.otherScopus: 84879153876
dc.identifier.otherORCID: /0000-0003-3873-0650/work/60630852
dc.identifier.urihttps://hdl.handle.net/10023/3573
dc.descriptionThis work was supported by Biotechnology and Biomedical Sciences Research Council grant BB/H018719/1en
dc.description.abstractDuring infection, many RNA viruses produce characteristic inclusion bodies that contain both viral and host components. These structures were first described over a century ago and originally termed “X-bodies,” as their function was not immediately appreciated. Whilst some inclusion bodies may represent cytopathic by-products of viral protein over-accumulation, X-bodies have emerged as virus “factories,” quasi-organelles that coordinate diverse viral infection processes such as replication, protein expression, evasion of host defenses, virion assembly, and intercellular transport. Accordingly, they are now generally referred to as viral replication complexes (VRCs). We previously used confocal fluorescence microscopy to unravel the complex structure of X-bodies produced by Potato virus X (PVX). Here we used 3D-structured illumination (3D-SIM) super-resolution microscopy to map the PVX X-body at a finer scale. We identify a previously unrecognized membrane structure induced by the PVX “triple gene block” (TGB) proteins, providing new insights into the complex interplay between virus and host within the X-body.
dc.language.isoeng
dc.relation.ispartofFrontiers in Plant Scienceen
dc.rights© 2013 Linnik, Liesche, Tilsner and Oparka. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in other forums, provided the original authors and source are credited and subject to any copyright notices concerning any third-party graphics etc.en
dc.subjectPVXen
dc.subjectViral replication complexen
dc.subject3D-SIMen
dc.subjectSuper-resolutionen
dc.subjectTGB proteinsen
dc.subjectEndoplasmic reticulumen
dc.subjectGolgien
dc.subjectQR355 Virologyen
dc.subject.lccQR355en
dc.titleUnravelling the structure of viral replication complexes at super-resolutionen
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/10.3389/fpls.2013.00006
dc.description.statusPeer revieweden


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