The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity.
Identifieur interne : 000E94 ( PubMed/Corpus ); précédent : 000E93; suivant : 000E95The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity.
Auteurs : Krystal Matthews ; Alexandra Sch Fer ; Alissa Pham ; Matthew FriemanSource :
- Virology journal [ 1743-422X ] ; 2014.
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.
DOI: 10.1186/s12985-014-0209-9
PubMed: 25481026
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity.</title><author><name sortKey="Matthews, Krystal" sort="Matthews, Krystal" uniqKey="Matthews K" first="Krystal" last="Matthews">Krystal Matthews</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, University of Maryland at Baltimore, 685 West Baltimore St., Room 380, Baltimore, MD, 21201, USA. kmatthews@som.umaryland.edu.</nlm:affiliation></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><nlm:affiliation>Department of Epidemiology, University of North Carolina, 3304 Michael Hooker Research Building, Chapel Hill, NC, 27599, USA. aschaefe@email.unc.edu.</nlm:affiliation></affiliation></author><author><name sortKey="Pham, Alissa" sort="Pham, Alissa" uniqKey="Pham A" first="Alissa" last="Pham">Alissa Pham</name><affiliation><nlm:affiliation>Department of Microbiology, Icahn School of Medicine at Mt. Sinai, New York, NY, 10029, USA. alissapham@gmail.com.</nlm:affiliation></affiliation></author><author><name sortKey="Frieman, Matthew" sort="Frieman, Matthew" uniqKey="Frieman M" first="Matthew" last="Frieman">Matthew Frieman</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, University of Maryland at Baltimore, 685 West Baltimore St., Room 380, Baltimore, MD, 21201, USA. mfrieman@som.umaryland.edu.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2014">2014</date><idno type="RBID">pubmed:25481026</idno><idno type="pmid">25481026</idno><idno type="doi">10.1186/s12985-014-0209-9</idno><idno type="wicri:Area/PubMed/Corpus">000E94</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000E94</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity.</title><author><name sortKey="Matthews, Krystal" sort="Matthews, Krystal" uniqKey="Matthews K" first="Krystal" last="Matthews">Krystal Matthews</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, University of Maryland at Baltimore, 685 West Baltimore St., Room 380, Baltimore, MD, 21201, USA. kmatthews@som.umaryland.edu.</nlm:affiliation></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><nlm:affiliation>Department of Epidemiology, University of North Carolina, 3304 Michael Hooker Research Building, Chapel Hill, NC, 27599, USA. aschaefe@email.unc.edu.</nlm:affiliation></affiliation></author><author><name sortKey="Pham, Alissa" sort="Pham, Alissa" uniqKey="Pham A" first="Alissa" last="Pham">Alissa Pham</name><affiliation><nlm:affiliation>Department of Microbiology, Icahn School of Medicine at Mt. Sinai, New York, NY, 10029, USA. alissapham@gmail.com.</nlm:affiliation></affiliation></author><author><name sortKey="Frieman, Matthew" sort="Frieman, Matthew" uniqKey="Frieman M" first="Matthew" last="Frieman">Matthew Frieman</name><affiliation><nlm:affiliation>Department of Microbiology and Immunology, University of Maryland at Baltimore, 685 West Baltimore St., Room 380, Baltimore, MD, 21201, USA. mfrieman@som.umaryland.edu.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Virology journal</title><idno type="eISSN">1743-422X</idno><imprint><date when="2014" type="published">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cell Line</term><term>Chromatin Immunoprecipitation</term><term>Cysteine Endopeptidases (metabolism)</term><term>Electrophoretic Mobility Shift Assay</term><term>Humans</term><term>Interferon Regulatory Factor-3 (antagonists & inhibitors)</term><term>SARS Virus (enzymology)</term><term>Transfection</term><term>Ubiquitin (metabolism)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Interferon Regulatory Factor-3</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Ubiquitin</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Cell Line</term><term>Chromatin Immunoprecipitation</term><term>Electrophoretic Mobility Shift Assay</term><term>Humans</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">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.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">25481026</PMID><DateCompleted><Year>2015</Year><Month>10</Month><Day>12</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1743-422X</ISSN><JournalIssue CitedMedium="Internet"><Volume>11</Volume><PubDate><Year>2014</Year><Month>Dec</Month><Day>07</Day></PubDate></JournalIssue><Title>Virology journal</Title><ISOAbbreviation>Virol. J.</ISOAbbreviation></Journal><ArticleTitle>The SARS coronavirus papain like protease can inhibit IRF3 at a post activation step that requires deubiquitination activity.</ArticleTitle><Pagination><MedlinePgn>209</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1186/s12985-014-0209-9</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">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.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">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.</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">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.</AbstractText><AbstractText Label="CONCLUSION" NlmCategory="CONCLUSIONS">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.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Matthews</LastName><ForeName>Krystal</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, University of Maryland at Baltimore, 685 West Baltimore St., Room 380, Baltimore, MD, 21201, USA. kmatthews@som.umaryland.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Schäfer</LastName><ForeName>Alexandra</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Epidemiology, University of North Carolina, 3304 Michael Hooker Research Building, Chapel Hill, NC, 27599, USA. aschaefe@email.unc.edu.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pham</LastName><ForeName>Alissa</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Microbiology, Icahn School of Medicine at Mt. Sinai, New York, NY, 10029, USA. alissapham@gmail.com.</Affiliation></AffiliationInfo><AffiliationInfo><Affiliation>Current Address: NYU Langone Medical Center, Department of Pathology, 538 Medical Science Building, New York, NY, 10016, USA. alissapham@gmail.com.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Frieman</LastName><ForeName>Matthew</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>Department of Microbiology and Immunology, University of Maryland at Baltimore, 685 West Baltimore St., Room 380, Baltimore, MD, 21201, USA. mfrieman@som.umaryland.edu.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>K22 AI077797</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>K22AI077797</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D052061">Research Support, N.I.H., Extramural</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2014</Year><Month>12</Month><Day>07</Day></ArticleDate></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>Virol J</MedlineTA><NlmUniqueID>101231645</NlmUniqueID><ISSNLinking>1743-422X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C494232">IRF3 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D050838">Interferon Regulatory Factor-3</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D025801">Ubiquitin</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="C099456">3C-like proteinase, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D047369" MajorTopicYN="N">Chromatin Immunoprecipitation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D024202" MajorTopicYN="N">Electrophoretic Mobility Shift Assay</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050838" MajorTopicYN="N">Interferon Regulatory Factor-3</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014162" MajorTopicYN="N">Transfection</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025801" MajorTopicYN="N">Ubiquitin</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate 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