A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.

Plus-stranded RNA viruses replicate in infected cells by assembling viral replicase complexes consisting of viral- and host-coded proteins. Previous genome-wide screens with Tomato bushy stunt tombusvirus (TBSV) in a yeast model host revealed the involvement of seven ESCRT (endosomal sorting complex...

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Main Authors: Daniel Barajas, Yi Jiang, Peter D Nagy
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2009-12-01
Series:PLoS Pathogens
Online Access:http://europepmc.org/articles/PMC2791863?pdf=render
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spelling doaj-4d18b37f63134e349813223902deb47b2020-11-24T22:09:19ZengPublic Library of Science (PLoS)PLoS Pathogens1553-73661553-73742009-12-01512e100070510.1371/journal.ppat.1000705A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.Daniel BarajasYi JiangPeter D NagyPlus-stranded RNA viruses replicate in infected cells by assembling viral replicase complexes consisting of viral- and host-coded proteins. Previous genome-wide screens with Tomato bushy stunt tombusvirus (TBSV) in a yeast model host revealed the involvement of seven ESCRT (endosomal sorting complexes required for transport) proteins in viral replication. In this paper, we show that the expression of dominant negative Vps23p, Vps24p, Snf7p, and Vps4p ESCRT factors inhibited virus replication in the plant host, suggesting that tombusviruses co-opt selected ESCRT proteins for the assembly of the viral replicase complex. We also show that TBSV p33 replication protein interacts with Vps23p ESCRT-I and Bro1p accessory ESCRT factors. The interaction with p33 leads to the recruitment of Vps23p to the peroxisomes, the sites of TBSV replication. The viral replicase showed reduced activity and the minus-stranded viral RNA in the replicase became more accessible to ribonuclease when derived from vps23Delta or vps24Delta yeast, suggesting that the protection of the viral RNA is compromised within the replicase complex assembled in the absence of ESCRT proteins. The recruitment of ESCRT proteins is needed for the precise assembly of the replicase complex, which might help the virus evade recognition by the host defense surveillance system and/or prevent viral RNA destruction by the gene silencing machinery.http://europepmc.org/articles/PMC2791863?pdf=render
collection DOAJ
language English
format Article
sources DOAJ
author Daniel Barajas
Yi Jiang
Peter D Nagy
spellingShingle Daniel Barajas
Yi Jiang
Peter D Nagy
A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.
PLoS Pathogens
author_facet Daniel Barajas
Yi Jiang
Peter D Nagy
author_sort Daniel Barajas
title A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.
title_short A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.
title_full A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.
title_fullStr A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.
title_full_unstemmed A unique role for the host ESCRT proteins in replication of Tomato bushy stunt virus.
title_sort unique role for the host escrt proteins in replication of tomato bushy stunt virus.
publisher Public Library of Science (PLoS)
series PLoS Pathogens
issn 1553-7366
1553-7374
publishDate 2009-12-01
description Plus-stranded RNA viruses replicate in infected cells by assembling viral replicase complexes consisting of viral- and host-coded proteins. Previous genome-wide screens with Tomato bushy stunt tombusvirus (TBSV) in a yeast model host revealed the involvement of seven ESCRT (endosomal sorting complexes required for transport) proteins in viral replication. In this paper, we show that the expression of dominant negative Vps23p, Vps24p, Snf7p, and Vps4p ESCRT factors inhibited virus replication in the plant host, suggesting that tombusviruses co-opt selected ESCRT proteins for the assembly of the viral replicase complex. We also show that TBSV p33 replication protein interacts with Vps23p ESCRT-I and Bro1p accessory ESCRT factors. The interaction with p33 leads to the recruitment of Vps23p to the peroxisomes, the sites of TBSV replication. The viral replicase showed reduced activity and the minus-stranded viral RNA in the replicase became more accessible to ribonuclease when derived from vps23Delta or vps24Delta yeast, suggesting that the protection of the viral RNA is compromised within the replicase complex assembled in the absence of ESCRT proteins. The recruitment of ESCRT proteins is needed for the precise assembly of the replicase complex, which might help the virus evade recognition by the host defense surveillance system and/or prevent viral RNA destruction by the gene silencing machinery.
url http://europepmc.org/articles/PMC2791863?pdf=render
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