Unravelling the structure of viral replication complexes at super-resolution
During 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 repre...
| Main Authors: | , , , |
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| Format: | Article |
| Language: | English |
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Frontiers Media S.A.
2013-01-01
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| Series: | Frontiers in Plant Science |
| Subjects: | |
| Online Access: | http://journal.frontiersin.org/Journal/10.3389/fpls.2013.00006/full |
| _version_ | 1819152802074591232 |
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| author | Olga eLinnik Johannes eLiesche Jens eTilsner Jens eTilsner Karl eOparka |
| author_facet | Olga eLinnik Johannes eLiesche Jens eTilsner Jens eTilsner Karl eOparka |
| author_sort | Olga eLinnik |
| collection | DOAJ |
| description | During 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 defences, 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 unrecognised 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. |
| first_indexed | 2024-12-22T14:55:04Z |
| format | Article |
| id | doaj.art-b1247f29c19742069c64705b12e6b1ff |
| institution | Directory Open Access Journal |
| issn | 1664-462X |
| language | English |
| last_indexed | 2024-12-22T14:55:04Z |
| publishDate | 2013-01-01 |
| publisher | Frontiers Media S.A. |
| record_format | Article |
| series | Frontiers in Plant Science |
| spelling | doaj.art-b1247f29c19742069c64705b12e6b1ff2022-12-21T18:22:15ZengFrontiers Media S.A.Frontiers in Plant Science1664-462X2013-01-01410.3389/fpls.2013.0000640704Unravelling the structure of viral replication complexes at super-resolutionOlga eLinnik0Johannes eLiesche1Jens eTilsner2Jens eTilsner3Karl eOparka4University of EdinburghUniversity of CopenhagenUniversity of St AndrewsThe James Hutton InstituteUniversity of EdinburghDuring 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 defences, 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 unrecognised 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.http://journal.frontiersin.org/Journal/10.3389/fpls.2013.00006/fullEndoplasmic ReticulumGolgiPVXviral replication complex3D-SIMsuper-resolution |
| spellingShingle | Olga eLinnik Johannes eLiesche Jens eTilsner Jens eTilsner Karl eOparka Unravelling the structure of viral replication complexes at super-resolution Frontiers in Plant Science Endoplasmic Reticulum Golgi PVX viral replication complex 3D-SIM super-resolution |
| title | Unravelling the structure of viral replication complexes at super-resolution |
| title_full | Unravelling the structure of viral replication complexes at super-resolution |
| title_fullStr | Unravelling the structure of viral replication complexes at super-resolution |
| title_full_unstemmed | Unravelling the structure of viral replication complexes at super-resolution |
| title_short | Unravelling the structure of viral replication complexes at super-resolution |
| title_sort | unravelling the structure of viral replication complexes at super resolution |
| topic | Endoplasmic Reticulum Golgi PVX viral replication complex 3D-SIM super-resolution |
| url | http://journal.frontiersin.org/Journal/10.3389/fpls.2013.00006/full |
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