PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway.
Identifieur interne : 001543 ( PubMed/Corpus ); précédent : 001542; suivant : 001544PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway.
Auteurs : Gang Wang ; Gang Chen ; Dahai Zheng ; Genhong Cheng ; Hong TangSource :
- PloS one [ 1932-6203 ] ; 2011.
English descriptors
- KwdEn :
- Animals, Cells, Cultured, Interferon Type I (metabolism), Interferon Type I (physiology), Mice, Murine hepatitis virus (enzymology), Murine hepatitis virus (metabolism), Papain (chemistry), Papain (genetics), Papain (metabolism), Protein Processing, Post-Translational (genetics), Protein Processing, Post-Translational (physiology), Protein Structure, Tertiary (genetics), Protein Structure, Tertiary (physiology), Protein-Serine-Threonine Kinases (antagonists & inhibitors), Protein-Serine-Threonine Kinases (metabolism), Signal Transduction (genetics), Signal Transduction (physiology), Transfection, Ubiquitination (genetics), Viral Nonstructural Proteins (chemistry), Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Viral Nonstructural Proteins (physiology).
- MESH :
- chemical , antagonists & inhibitors : Protein-Serine-Threonine Kinases.
- chemical , chemistry : Papain, Viral Nonstructural Proteins.
- chemical , genetics : Papain, Viral Nonstructural Proteins.
- chemical , metabolism : Interferon Type I, Papain, Protein-Serine-Threonine Kinases, Viral Nonstructural Proteins.
- chemical , physiology : Interferon Type I, Viral Nonstructural Proteins.
- enzymology : Murine hepatitis virus.
- genetics : Protein Processing, Post-Translational, Protein Structure, Tertiary, Signal Transduction, Ubiquitination.
- metabolism : Murine hepatitis virus.
- physiology : Protein Processing, Post-Translational, Protein Structure, Tertiary, Signal Transduction.
- Animals, Cells, Cultured, Mice, Transfection.
Abstract
Coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) have evolved strategies to disable the innate immune system for productive replication and spread of infection. We have previously shown that papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, encodes a deubiquitinase (DUB) and inactivates IFN regulatory factor 3 (IRF3) thereby the type I interferon (IFN) response.
DOI: 10.1371/journal.pone.0017192
PubMed: 21364999
Links to Exploration step
pubmed:21364999Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway.</title><author><name sortKey="Wang, Gang" sort="Wang, Gang" uniqKey="Wang G" first="Gang" last="Wang">Gang Wang</name><affiliation><nlm:affiliation>Key Laboratory of Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Chen, Gang" sort="Chen, Gang" uniqKey="Chen G" first="Gang" last="Chen">Gang Chen</name></author><author><name sortKey="Zheng, Dahai" sort="Zheng, Dahai" uniqKey="Zheng D" first="Dahai" last="Zheng">Dahai Zheng</name></author><author><name sortKey="Cheng, Genhong" sort="Cheng, Genhong" uniqKey="Cheng G" first="Genhong" last="Cheng">Genhong Cheng</name></author><author><name sortKey="Tang, Hong" sort="Tang, Hong" uniqKey="Tang H" first="Hong" last="Tang">Hong Tang</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2011">2011</date><idno type="RBID">pubmed:21364999</idno><idno type="pmid">21364999</idno><idno type="doi">10.1371/journal.pone.0017192</idno><idno type="wicri:Area/PubMed/Corpus">001543</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001543</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway.</title><author><name sortKey="Wang, Gang" sort="Wang, Gang" uniqKey="Wang G" first="Gang" last="Wang">Gang Wang</name><affiliation><nlm:affiliation>Key Laboratory of Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</nlm:affiliation></affiliation></author><author><name sortKey="Chen, Gang" sort="Chen, Gang" uniqKey="Chen G" first="Gang" last="Chen">Gang Chen</name></author><author><name sortKey="Zheng, Dahai" sort="Zheng, Dahai" uniqKey="Zheng D" first="Dahai" last="Zheng">Dahai Zheng</name></author><author><name sortKey="Cheng, Genhong" sort="Cheng, Genhong" uniqKey="Cheng G" first="Genhong" last="Cheng">Genhong Cheng</name></author><author><name sortKey="Tang, Hong" sort="Tang, Hong" uniqKey="Tang H" first="Hong" last="Tang">Hong Tang</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2011" type="published">2011</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Interferon Type I (metabolism)</term><term>Interferon Type I (physiology)</term><term>Mice</term><term>Murine hepatitis virus (enzymology)</term><term>Murine hepatitis virus (metabolism)</term><term>Papain (chemistry)</term><term>Papain (genetics)</term><term>Papain (metabolism)</term><term>Protein Processing, Post-Translational (genetics)</term><term>Protein Processing, Post-Translational (physiology)</term><term>Protein Structure, Tertiary (genetics)</term><term>Protein Structure, Tertiary (physiology)</term><term>Protein-Serine-Threonine Kinases (antagonists & inhibitors)</term><term>Protein-Serine-Threonine Kinases (metabolism)</term><term>Signal Transduction (genetics)</term><term>Signal Transduction (physiology)</term><term>Transfection</term><term>Ubiquitination (genetics)</term><term>Viral Nonstructural Proteins (chemistry)</term><term>Viral Nonstructural Proteins (genetics)</term><term>Viral Nonstructural Proteins (metabolism)</term><term>Viral Nonstructural Proteins (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Protein-Serine-Threonine Kinases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Papain</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Papain</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Interferon Type I</term><term>Papain</term><term>Protein-Serine-Threonine Kinases</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="physiology" xml:lang="en"><term>Interferon Type I</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Protein Processing, Post-Translational</term><term>Protein Structure, Tertiary</term><term>Signal Transduction</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Murine hepatitis virus</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Protein Processing, Post-Translational</term><term>Protein Structure, Tertiary</term><term>Signal Transduction</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cells, Cultured</term><term>Mice</term><term>Transfection</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) have evolved strategies to disable the innate immune system for productive replication and spread of infection. We have previously shown that papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, encodes a deubiquitinase (DUB) and inactivates IFN regulatory factor 3 (IRF3) thereby the type I interferon (IFN) response.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21364999</PMID><DateCompleted><Year>2011</Year><Month>09</Month><Day>01</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>6</Volume><Issue>2</Issue><PubDate><Year>2011</Year><Month>Feb</Month><Day>18</Day></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>PLP2 of mouse hepatitis virus A59 (MHV-A59) targets TBK1 to negatively regulate cellular type I interferon signaling pathway.</ArticleTitle><Pagination><MedlinePgn>e17192</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0017192</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) have evolved strategies to disable the innate immune system for productive replication and spread of infection. We have previously shown that papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, encodes a deubiquitinase (DUB) and inactivates IFN regulatory factor 3 (IRF3) thereby the type I interferon (IFN) response.</AbstractText><AbstractText Label="PRINCIPAL FINDINGS" NlmCategory="RESULTS">Here we provide further evidence that PLP2 may also target TANK-binding kinase-1 (TBK1), the upstream kinase of IRF3 in the IFN signaling pathway. Overexpression experiments showed that PLP2 deubiquitinated TBK1 and reduced its kinase activity, hence inhibited IFN-β reporter activity. Albeit promiscuous in deubiquitinating cellular proteins, PLP2 inactivated TBK1 and IFN-β response in TNF receptor associated factor 3 (TRAF3) deficient cells, suggesting that targeting TBK1 would be sufficient for PLP2 to inhibit IRF3 activation. This notion was further supported by in vitro kinase assays, in which prior treatment of TBK1 with PLP2 inhibited its kinase activity to phosphorylate IRF3. Intriguing enough, results of PLP2 overexpression system and MHV-A59 infection system proved that PLP2 formed an inactive complex with TBK1 and IRF3 in the cytoplasm and the presence of PLP2 stabilized the hypo-phosphorylated IRF3-TBK1 complex in a dose-dependent manner.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">These results suggest that PLP2 not only inactivates TBK1, but also prevents IRF3 nuclear translocation hence inhibits IFN transcription activation. Identification of the conserved DUB activity of PLP2 in suppression of IFN signaling would provide a useful clue to the development of therapeutics against coronaviruses infection.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Gang</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Key Laboratory of Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, Beijing, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Gang</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Dahai</ForeName><Initials>D</Initials></Author><Author ValidYN="Y"><LastName>Cheng</LastName><ForeName>Genhong</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Tang</LastName><ForeName>Hong</ForeName><Initials>H</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>R01 AI069120</GrantID><Acronym>AI</Acronym><Agency>NIAID NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2011</Year><Month>02</Month><Day>18</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007370">Interferon Type I</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C089383">nsP3 protein, virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="D017346">Protein-Serine-Threonine Kinases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.7.11.1</RegistryNumber><NameOfSubstance UI="C403191">TBK1 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="D010206">Papain</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="C000657884">papain-like protease, Coronavirus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007370" MajorTopicYN="N">Interferon Type I</DescriptorName><QualifierName UI="Q000378" 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IdType="pubmed">17823124</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2007 Nov 2;282(44):32208-21</Citation><ArticleIdList><ArticleId IdType="pubmed">17761676</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2007 Dec 7;318(5856):1628-32</Citation><ArticleIdList><ArticleId IdType="pubmed">17991829</ArticleId></ArticleIdList></Reference><Reference><Citation>Virus Res. 2008 Apr;133(1):101-12</Citation><ArticleIdList><ArticleId IdType="pubmed">17451827</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2008 Apr;82(8):3984-96</Citation><ArticleIdList><ArticleId IdType="pubmed">18272581</ArticleId></ArticleIdList></Reference><Reference><Citation>Biochem Soc Trans. 2008 Jun;36(Pt 3):453-8</Citation><ArticleIdList><ArticleId IdType="pubmed">18481980</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 May 23;283(21):14269-76</Citation><ArticleIdList><ArticleId IdType="pubmed">18362155</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2008 Jul 4;283(27):18621-6</Citation><ArticleIdList><ArticleId IdType="pubmed">18467330</ArticleId></ArticleIdList></Reference><Reference><Citation>Cytokine. 2008 Sep;43(3):359-67</Citation><ArticleIdList><ArticleId IdType="pubmed">18707898</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Res. 2008 Nov;18(11):1096-104</Citation><ArticleIdList><ArticleId IdType="pubmed">18711448</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Res. 2008 Nov;18(11):1105-13</Citation><ArticleIdList><ArticleId IdType="pubmed">18957937</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2009 Jan 9;284(2):1097-105</Citation><ArticleIdList><ArticleId IdType="pubmed">19010780</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Res. 2009 Jan;19(1):3-4</Citation><ArticleIdList><ArticleId IdType="pubmed">19125153</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2009 Apr;83(7):3069-77</Citation><ArticleIdList><ArticleId IdType="pubmed">19153231</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2009 Jul;83(13):6689-705</Citation><ArticleIdList><ArticleId IdType="pubmed">19369340</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Immunol. 2009 Jul;10(7):744-52</Citation><ArticleIdList><ArticleId IdType="pubmed">19483718</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Immunol. 2009 Oct;10(10):1073-80</Citation><ArticleIdList><ArticleId IdType="pubmed">19701189</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2010 Jan 15;327(5963):291-5</Citation><ArticleIdList><ArticleId IdType="pubmed">20075244</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2010 May;84(9):4619-29</Citation><ArticleIdList><ArticleId IdType="pubmed">20181693</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2010 Jun;84(11):5656-69</Citation><ArticleIdList><ArticleId IdType="pubmed">20357099</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2003 Apr;77(8):4597-608</Citation><ArticleIdList><ArticleId IdType="pubmed">12663766</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Immunol. 2003 May;4(5):491-6</Citation><ArticleIdList><ArticleId IdType="pubmed">12692549</ArticleId></ArticleIdList></Reference><Reference><Citation>Science. 2003 May 16;300(5622):1148-51</Citation><ArticleIdList><ArticleId IdType="pubmed">12702806</ArticleId></ArticleIdList></Reference><Reference><Citation>J Exp Med. 2004 Jun 21;199(12):1651-8</Citation><ArticleIdList><ArticleId IdType="pubmed">15210743</ArticleId></ArticleIdList></Reference><Reference><Citation>Nat Immunol. 2004 Jul;5(7):730-7</Citation><ArticleIdList><ArticleId IdType="pubmed">15208624</ArticleId></ArticleIdList></Reference><Reference><Citation>FEBS Lett. 2004 Oct 8;576(1-2):86-90</Citation><ArticleIdList><ArticleId IdType="pubmed">15474016</ArticleId></ArticleIdList></Reference><Reference><Citation>Immunity. 1996 Nov;5(5):407-15</Citation><ArticleIdList><ArticleId IdType="pubmed">8934568</ArticleId></ArticleIdList></Reference><Reference><Citation>Proc Natl Acad Sci U S A. 2004 Dec 7;101(49):17264-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15563593</ArticleId></ArticleIdList></Reference><Reference><Citation>BMC Immunol. 2005;6:2</Citation><ArticleIdList><ArticleId IdType="pubmed">15655079</ArticleId></ArticleIdList></Reference><Reference><Citation>J Neurosci. 2005 Feb 23;25(8):2002-9</Citation><ArticleIdList><ArticleId IdType="pubmed">15728840</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Res. 2005 Jun;15(6):407-22</Citation><ArticleIdList><ArticleId IdType="pubmed">15987599</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2005 Dec;79(24):15189-98</Citation><ArticleIdList><ArticleId IdType="pubmed">16306590</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2006 Jan 11;25(1):108-17</Citation><ArticleIdList><ArticleId IdType="pubmed">16362036</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2006 Jan 12;439(7073):208-11</Citation><ArticleIdList><ArticleId IdType="pubmed">16306936</ArticleId></ArticleIdList></Reference><Reference><Citation>J Biol Chem. 2006 Jan 27;281(4):2095-103</Citation><ArticleIdList><ArticleId IdType="pubmed">16306043</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell. 2006 Feb 24;124(4):783-801</Citation><ArticleIdList><ArticleId IdType="pubmed">16497588</ArticleId></ArticleIdList></Reference><Reference><Citation>Nature. 2006 Jul 6;442(7098):39-44</Citation><ArticleIdList><ArticleId IdType="pubmed">16823444</ArticleId></ArticleIdList></Reference><Reference><Citation>EMBO J. 2006 Jul 26;25(14):3257-63</Citation><ArticleIdList><ArticleId IdType="pubmed">16858409</ArticleId></ArticleIdList></Reference><Reference><Citation>Immunity. 2006 Sep;25(3):361-72</Citation><ArticleIdList><ArticleId IdType="pubmed">16979568</ArticleId></ArticleIdList></Reference><Reference><Citation>J Immunol. 2006 Oct 15;177(8):5059-67</Citation><ArticleIdList><ArticleId IdType="pubmed">17015689</ArticleId></ArticleIdList></Reference><Reference><Citation>J Virol. 2007 Jan;81(2):568-74</Citation><ArticleIdList><ArticleId IdType="pubmed">17079305</ArticleId></ArticleIdList></Reference><Reference><Citation>J Mol Med (Berl). 2006 Sep;84(9):712-25</Citation><ArticleIdList><ArticleId IdType="pubmed">16924467</ArticleId></ArticleIdList></Reference><Reference><Citation>Annu Rev Immunol. 2007;25:443-72</Citation><ArticleIdList><ArticleId IdType="pubmed">17243893</ArticleId></ArticleIdList></Reference><Reference><Citation>Virology. 2007 Apr 25;361(1):18-26</Citation><ArticleIdList><ArticleId IdType="pubmed">17316733</ArticleId></ArticleIdList></Reference><Reference><Citation>Cell Microbiol. 2007 Nov;9(11):2700-15</Citation><ArticleIdList><ArticleId IdType="pubmed">17608743</ArticleId></ArticleIdList></Reference></ReferenceList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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