Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling.
Identifieur interne : 002A17 ( Main/Exploration ); précédent : 002A16; suivant : 002A18Severe 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
Affiliations:
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 001927
- to stream PubMed, to step Curation: 001927
- to stream PubMed, to step Checkpoint: 001785
- to stream Ncbi, to step Merge: 001E90
- to stream Ncbi, to step Curation: 001E90
- to stream Ncbi, to step Checkpoint: 001E90
- to stream Main, to step Merge: 002A62
- to stream Main, to step Curation: 002A17
Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling.</title><author><name sortKey="Frieman, Matthew" sort="Frieman, Matthew" uniqKey="Frieman M" first="Matthew" last="Frieman">Matthew Frieman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina 27599</wicri:regionArea><wicri:noRegion>North Carolina 27599</wicri:noRegion></affiliation></author><author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name></author><author><name sortKey="Johnston, Robert E" sort="Johnston, Robert E" uniqKey="Johnston R" first="Robert E" last="Johnston">Robert E. Johnston</name></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2009">2009</date><idno type="RBID">pubmed:19369340</idno><idno type="pmid">19369340</idno><idno type="doi">10.1128/JVI.02220-08</idno><idno type="wicri:Area/PubMed/Corpus">001927</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001927</idno><idno type="wicri:Area/PubMed/Curation">001927</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001927</idno><idno type="wicri:Area/PubMed/Checkpoint">001785</idno><idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001785</idno><idno type="wicri:Area/Ncbi/Merge">001E90</idno><idno type="wicri:Area/Ncbi/Curation">001E90</idno><idno type="wicri:Area/Ncbi/Checkpoint">001E90</idno><idno type="wicri:Area/Main/Merge">002A62</idno><idno type="wicri:Area/Main/Curation">002A17</idno><idno type="wicri:Area/Main/Exploration">002A17</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling.</title><author><name sortKey="Frieman, Matthew" sort="Frieman, Matthew" uniqKey="Frieman M" first="Matthew" last="Frieman">Matthew Frieman</name><affiliation wicri:level="1"><nlm:affiliation>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina 27599, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Epidemiology, University of North Carolina, Chapel Hill, North Carolina 27599</wicri:regionArea><wicri:noRegion>North Carolina 27599</wicri:noRegion></affiliation></author><author><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name></author><author><name sortKey="Johnston, Robert E" sort="Johnston, Robert E" uniqKey="Johnston R" first="Robert E" last="Johnston">Robert E. Johnston</name></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name></author><author><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2009" type="published">2009</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Cysteine Endopeptidases (metabolism)</term><term>Humans</term><term>I-kappa B Proteins (metabolism)</term><term>Interferon Regulatory Factor-3 (metabolism)</term><term>Interferons (antagonists & inhibitors)</term><term>NF-KappaB Inhibitor alpha</term><term>NF-kappa B (metabolism)</term><term>Phosphorylation</term><term>SARS Virus (enzymology)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cysteine endopeptidases (métabolisme)</term><term>Facteur de transcription NF-kappa B (métabolisme)</term><term>Facteur-3 de régulation d'interféron (métabolisme)</term><term>Humains</term><term>Inhibiteur alpha de NF-KappaB</term><term>Interférons (antagonistes et inhibiteurs)</term><term>Lignée cellulaire</term><term>Phosphorylation</term><term>Protéines I-kappa B (métabolisme)</term><term>Protéines virales (métabolisme)</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Interferons</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>I-kappa B Proteins</term><term>Interferon Regulatory Factor-3</term><term>NF-kappa B</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Interférons</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term><term>Facteur de transcription NF-kappa B</term><term>Facteur-3 de régulation d'interféron</term><term>Protéines I-kappa B</term><term>Protéines virales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Humans</term><term>NF-KappaB Inhibitor alpha</term><term>Phosphorylation</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term><term>Inhibiteur alpha de NF-KappaB</term><term>Lignée cellulaire</term><term>Phosphorylation</term></keywords></textClass></profileDesc></teiHeader><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></TEI><affiliations><list><country><li>États-Unis</li></country></list><tree><noCountry><name sortKey="Baric, Ralph S" sort="Baric, Ralph S" uniqKey="Baric R" first="Ralph S" last="Baric">Ralph S. Baric</name><name sortKey="Johnston, Robert E" sort="Johnston, Robert E" uniqKey="Johnston R" first="Robert E" last="Johnston">Robert E. Johnston</name><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D" last="Mesecar">Andrew D. Mesecar</name><name sortKey="Ratia, Kiira" sort="Ratia, Kiira" uniqKey="Ratia K" first="Kiira" last="Ratia">Kiira Ratia</name></noCountry><country name="États-Unis"><noRegion><name sortKey="Frieman, Matthew" sort="Frieman, Matthew" uniqKey="Frieman M" first="Matthew" last="Frieman">Matthew Frieman</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002A17 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 002A17 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien
|wiki= Sante
|area= SrasV1
|flux= Main
|étape= Exploration
|type= RBID
|clé= pubmed:19369340
|texte= Severe acute respiratory syndrome coronavirus papain-like protease ubiquitin-like domain and catalytic domain regulate antagonism of IRF3 and NF-kappaB signaling.
}}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i -Sk "pubmed:19369340" \
| HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd \
| NlmPubMed2Wicri -a SrasV1
| This area was generated with Dilib version V0.6.33. |  |