Unravelling the structure of viral replication complexes at super-resolution
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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 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.
Linnik , 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 . DOI: 10.3389/fpls.2013.00006
Frontiers in Plant Science
© 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.
This work was supported by Biotechnology and Biomedical Sciences Research Council grant BB/H018719/1
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