The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity
Identifieur interne : 001545 ( Main/Exploration ); précédent : 001544; suivant : 001546The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity
Auteurs : Krystal Matthews [États-Unis] ; Alexandra Sch Fer [États-Unis] ; Alissa Pham [États-Unis] ; Matthew Frieman [États-Unis]Source :
- Virology Journal [ 1743-422X ] ; 2014.
Descripteurs français
- KwdFr :
- Cysteine endopeptidases (métabolisme), Facteur-3 de régulation d'interféron (antagonistes et inhibiteurs), Humains, Immunoprécipitation de la chromatine, Lignée cellulaire, Protéines virales (métabolisme), Test de retard de migration électrophorétique, Transfection, Ubiquitine (métabolisme), Virus du SRAS (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Facteur-3 de régulation d'interféron.
- enzymologie : Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines virales, Ubiquitine.
- Humains, Immunoprécipitation de la chromatine, Lignée cellulaire, Test de retard de migration électrophorétique, Transfection.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Interferon Regulatory Factor-3.
- chemical , metabolism : Cysteine Endopeptidases, Ubiquitin, Viral Proteins.
- enzymology : SARS Virus.
- Cell Line, Chromatin Immunoprecipitation, Electrophoretic Mobility Shift Assay, Humans, Transfection.
Abstract
The outcome of a viral infection is regulated by complex interactions of viral and host factors. SARS coronavirus (SARS-CoV) engages and regulates several innate immune response pathways during infection. We have previously shown that the SARS-CoV Papain-like Protease (PLpro) inhibits type I interferon (IFN) by inhibiting IRF3 phosphorylation thereby blocking downstream Interferon induction. This finding prompted us to identify other potential mechanisms of inhibition of PLpro on IFN induction.
We have used plasmids expressing PLpro and IRF3 including an IRF3 mutant that is constitutively active, called IRF3(5D). In these experiments we utilize transfections, chromatin immunoprecipitation, Electro-mobility Shift Assays (EMSA) and protein localization to identify where IRF3 and IRF3(5D) are inhibited by PLpro.
Here we show that PLpro also inhibits IRF3 activation at a step after phosphorylation and that this inhibition is dependent on the de-ubiquitination (DUB) activity of PLpro. We found that PLpro is able to block the type I IFN induction of a constitutively active IRF3, but does not inhibit IRF3 dimerization, nuclear localization or DNA binding. However, inhibition of PLpro’s DUB activity by mutagenesis blocked the IRF3 inhibition activity of PLpro, suggesting a role for IRF3 ubiquitination in induction of a type I IFN innate immune response.
These results demonstrate an additional mechanism that PLpro is able to inhibit IRF3 signaling. These data suggest novel innate immune antagonism activities of PLpro that may contribute to SARS-CoV pathogenesis.
The online version of this article (doi:10.1186/s12985-014-0209-9) contains supplementary material, which is available to authorized users.
Url:
DOI: 10.1186/s12985-014-0209-9
PubMed: 25481026
PubMed Central: 4272517
Affiliations:
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USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Maryland</region></placeName><wicri:cityArea>685 West Baltimore St., Room 380, Baltimore</wicri:cityArea></affiliation></author><author><name sortKey="Sch Fer, Alexandra" sort="Sch Fer, Alexandra" uniqKey="Sch Fer A" first="Alexandra" last="Sch Fer">Alexandra Sch Fer</name><affiliation wicri:level="2"><nlm:aff id="Aff2"><institution-wrap><institution-id institution-id-type="GRID">grid.10698.36</institution-id><institution-id institution-id-type="ISNI">0000000122483208</institution-id><institution>Department of Epidemiology,</institution><institution>University of North Carolina,</institution></institution-wrap>3304 Michael Hooker Research Building, Chapel Hill, NC 27599 USA</nlm:aff><country xml:lang="fr">États-Unis</country><placeName><region type="state">Caroline du Nord</region></placeName><wicri:cityArea>3304 Michael Hooker Research Building, Chapel Hill</wicri:cityArea></affiliation></author><author><name sortKey="Pham, Alissa" sort="Pham, Alissa" uniqKey="Pham A" first="Alissa" last="Pham">Alissa Pham</name><affiliation wicri:level="2"><nlm:aff id="Aff3"><institution-wrap><institution-id institution-id-type="GRID">grid.59734.3c</institution-id><institution-id institution-id-type="ISNI">0000000106702351</institution-id><institution>Department of Microbiology,</institution><institution>Icahn School of Medicine at Mt. 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SARS coronavirus (SARS-CoV) engages and regulates several innate immune response pathways during infection. We have previously shown that the SARS-CoV Papain-like Protease (PLpro) inhibits type I interferon (IFN) by inhibiting IRF3 phosphorylation thereby blocking downstream Interferon induction. This finding prompted us to identify other potential mechanisms of inhibition of PLpro on IFN induction.</p></sec><sec><title>Methods</title><p>We have used plasmids expressing PLpro and IRF3 including an IRF3 mutant that is constitutively active, called IRF3(5D). In these experiments we utilize transfections, chromatin immunoprecipitation, Electro-mobility Shift Assays (EMSA) and protein localization to identify where IRF3 and IRF3(5D) are inhibited by PLpro.</p></sec><sec><title>Results</title><p>Here we show that PLpro also inhibits IRF3 activation at a step after phosphorylation and that this inhibition is dependent on the de-ubiquitination (DUB) activity of PLpro. We found that PLpro is able to block the type I IFN induction of a constitutively active IRF3, but does not inhibit IRF3 dimerization, nuclear localization or DNA binding. However, inhibition of PLpro’s DUB activity by mutagenesis blocked the IRF3 inhibition activity of PLpro, suggesting a role for IRF3 ubiquitination in induction of a type I IFN innate immune response.</p></sec><sec><title>Conclusion</title><p>These results demonstrate an additional mechanism that PLpro is able to inhibit IRF3 signaling. These data suggest novel innate immune antagonism activities of PLpro that may contribute to SARS-CoV pathogenesis.</p></sec><sec><title>Electronic supplementary material</title><p>The online version of this article (doi:10.1186/s12985-014-0209-9) contains supplementary material, which is available to authorized users.</p></sec></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Drosten, C" uniqKey="Drosten C">C Drosten</name></author><author><name sortKey="Gunther, S" uniqKey="Gunther S">S Gunther</name></author><author><name sortKey="Preiser, W" uniqKey="Preiser W">W Preiser</name></author><author><name sortKey="Van Der Werf, S" uniqKey="Van Der Werf S">S van der Werf</name></author><author><name sortKey="Brodt, Hr" uniqKey="Brodt H">HR Brodt</name></author><author><name sortKey="Becker, S" uniqKey="Becker S">S Becker</name></author><author><name sortKey="Rabenau, H" uniqKey="Rabenau H">H Rabenau</name></author><author><name sortKey="Panning, M" uniqKey="Panning M">M Panning</name></author><author><name sortKey="Kolesnikova, L" uniqKey="Kolesnikova L">L Kolesnikova</name></author><author><name sortKey="Fouchier, Ra" uniqKey="Fouchier R">RA Fouchier</name></author><author><name sortKey="Berger, A" uniqKey="Berger A">A Berger</name></author><author><name sortKey="Burguiere, Am" uniqKey="Burguiere A">AM Burguiere</name></author><author><name sortKey="Cinatl, J" uniqKey="Cinatl J">J Cinatl</name></author><author><name sortKey="Eickmann, M" uniqKey="Eickmann M">M Eickmann</name></author><author><name sortKey="Escriou, N" uniqKey="Escriou N">N Escriou</name></author><author><name sortKey="Grywna, K" uniqKey="Grywna K">K Grywna</name></author><author><name sortKey="Kramme, S" uniqKey="Kramme S">S Kramme</name></author><author><name sortKey="Manuguerra, Jc" uniqKey="Manuguerra J">JC Manuguerra</name></author><author><name sortKey="Muller, S" uniqKey="Muller S">S Muller</name></author><author><name 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uniqKey="Chen X">X Chen</name></author><author><name sortKey="Du, F" uniqKey="Du F">F Du</name></author><author><name sortKey="Grishin, Nv" uniqKey="Grishin N">NV Grishin</name></author><author><name sortKey="Chen, Zj" uniqKey="Chen Z">ZJ Chen</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Frieman, M" uniqKey="Frieman M">M Frieman</name></author><author><name sortKey="Heise, M" uniqKey="Heise M">M Heise</name></author><author><name sortKey="Baric, R" uniqKey="Baric R">R Baric</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Caroline du Nord</li><li>Maryland</li><li>État de New York</li></region></list><tree><country name="États-Unis"><region name="Maryland"><name sortKey="Matthews, Krystal" sort="Matthews, Krystal" uniqKey="Matthews K" first="Krystal" last="Matthews">Krystal Matthews</name></region><name sortKey="Frieman, Matthew" sort="Frieman, Matthew" uniqKey="Frieman M" first="Matthew" last="Frieman">Matthew Frieman</name><name sortKey="Pham, Alissa" sort="Pham, Alissa" uniqKey="Pham A" first="Alissa" last="Pham">Alissa Pham</name><name sortKey="Pham, Alissa" sort="Pham, Alissa" uniqKey="Pham A" first="Alissa" last="Pham">Alissa Pham</name><name sortKey="Sch Fer, Alexandra" sort="Sch Fer, Alexandra" uniqKey="Sch Fer A" first="Alexandra" last="Sch Fer">Alexandra Sch Fer</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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