Sumoylation at the Host-Pathogen Interface
Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own proteins,...
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pubmed-36858632013-06-19 Sumoylation at the Host-Pathogen Interface Wilson, Van G. Review Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own proteins, several viral pathogens have been shown to modulate overall host sumoylation levels. Given the large number of cellular targets for SUMO addition and the breadth of critical cellular processes that are regulated via sumoylation, viral modulation of overall sumoylation presumably alters the cellular environment to ensure that it is favorable for viral reproduction and/or persistence. Like some viruses, certain bacterial plant pathogens also target the sumoylation system, usually decreasing sumoylation to disrupt host anti-pathogen responses. The recent demonstration that Listeria monocytogenes also disrupts host sumoylation, and that this is required for efficient infection, extends the plant pathogen observations to a human pathogen and suggests that pathogen modulation of host sumoylation may be more widespread than previously appreciated. This review will focus on recent aspects of how pathogens modulate the host sumoylation system and how this benefits the pathogen. MDPI 2012-04-05 /pmc/articles/PMC3685863/ /pubmed/23795346 http://dx.doi.org/10.3390/biom2020203 Text en © 2012 by the authors; licensee MDPI, Basel, Switzerland. http://creativecommons.org/licenses/by/3.0/ This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/). |
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Open Access Journal |
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Foreign Institution |
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US National Center for Biotechnology Information |
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NCBI PubMed |
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Online Access |
language |
English |
format |
Online |
author |
Wilson, Van G. |
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Wilson, Van G. Sumoylation at the Host-Pathogen Interface |
author_facet |
Wilson, Van G. |
author_sort |
Wilson, Van G. |
title |
Sumoylation at the Host-Pathogen Interface |
title_short |
Sumoylation at the Host-Pathogen Interface |
title_full |
Sumoylation at the Host-Pathogen Interface |
title_fullStr |
Sumoylation at the Host-Pathogen Interface |
title_full_unstemmed |
Sumoylation at the Host-Pathogen Interface |
title_sort |
sumoylation at the host-pathogen interface |
description |
Many viral proteins have been shown to be sumoylated with corresponding regulatory effects on their protein function, indicating that this host cell modification process is widely exploited by viral pathogens to control viral activity. In addition to using sumoylation to regulate their own proteins, several viral pathogens have been shown to modulate overall host sumoylation levels. Given the large number of cellular targets for SUMO addition and the breadth of critical cellular processes that are regulated via sumoylation, viral modulation of overall sumoylation presumably alters the cellular environment to ensure that it is favorable for viral reproduction and/or persistence. Like some viruses, certain bacterial plant pathogens also target the sumoylation system, usually decreasing sumoylation to disrupt host anti-pathogen responses. The recent demonstration that Listeria monocytogenes also disrupts host sumoylation, and that this is required for efficient infection, extends the plant pathogen observations to a human pathogen and suggests that pathogen modulation of host sumoylation may be more widespread than previously appreciated. This review will focus on recent aspects of how pathogens modulate the host sumoylation system and how this benefits the pathogen. |
publisher |
MDPI |
publishDate |
2012 |
url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3685863/ |
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