Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling.
Identifieur interne : 001E90 ( Ncbi/Curation ); précédent : 001E89; suivant : 001E91Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling.
Auteurs : Matthew Frieman [États-Unis] ; Kiira Ratia ; Robert E. Johnston ; Andrew D. Mesecar ; Ralph S. BaricSource :
- Journal of virology [ 1098-5514 ] ; 2009.
Descripteurs français
- KwdFr :
- Cysteine endopeptidases (métabolisme), Facteur de transcription NF-kappa B (métabolisme), Facteur-3 de régulation d'interféron (métabolisme), Humains, Inhibiteur alpha de NF-KappaB, Interférons (antagonistes et inhibiteurs), Lignée cellulaire, Phosphorylation, Protéines I-kappa B (métabolisme), Protéines virales (métabolisme), Virus du SRAS (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Interférons.
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Facteur de transcription NF-kappa B, Facteur-3 de régulation d'interféron, Protéines I-kappa B, Protéines virales.
- Humains, Inhibiteur alpha de NF-KappaB, Lignée cellulaire, Phosphorylation.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Interferons.
- chemical , metabolism : Cysteine Endopeptidases, I-kappa B Proteins, Interferon Regulatory Factor-3, NF-kappa B, Viral Proteins.
- enzymology : SARS Virus.
- Cell Line, Humans, NF-KappaB Inhibitor alpha, Phosphorylation.
Abstract
The outcome of a viral infection is regulated in part by the complex coordination of viral and host interactions that compete for the control and optimization of virus replication. Severe acute respiratory syndrome coronavirus (SARS-CoV) intimately engages and regulates the host innate immune responses during infection. Using a novel interferon (IFN) antagonism screen, we show that the SARS-CoV proteome contains several replicase, structural, and accessory proteins that antagonize the IFN pathway. In this study, we focus on the SARS-CoV papain-like protease (PLP), which engages and antagonizes the IFN induction and NF-kappaB signaling pathways. PLP blocks these pathways by affecting activation of the important signaling proteins in each pathway, IRF3 and NF-kappaB. We also show that the ubiquitin-like domain of PLP is necessary for pathway antagonism but not sufficient by itself to block these pathways regardless of the enzymatic activity of the protease. The potential mechanism of PLP antagonism and its role in pathogenesis are discussed.
DOI: 10.1128/JVI.02220-08
PubMed: 19369340
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pubmed:19369340Le document en format XML
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<front><div type="abstract" xml:lang="en">The outcome of a viral infection is regulated in part by the complex coordination of viral and host interactions that compete for the control and optimization of virus replication. Severe acute respiratory syndrome coronavirus (SARS-CoV) intimately engages and regulates the host innate immune responses during infection. Using a novel interferon (IFN) antagonism screen, we show that the SARS-CoV proteome contains several replicase, structural, and accessory proteins that antagonize the IFN pathway. In this study, we focus on the SARS-CoV papain-like protease (PLP), which engages and antagonizes the IFN induction and NF-kappaB signaling pathways. PLP blocks these pathways by affecting activation of the important signaling proteins in each pathway, IRF3 and NF-kappaB. We also show that the ubiquitin-like domain of PLP is necessary for pathway antagonism but not sufficient by itself to block these pathways regardless of the enzymatic activity of the protease. The potential mechanism of PLP antagonism and its role in pathogenesis are discussed.</div>
</front>
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