PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production.
Identifieur interne : 001A42 ( PubMed/Corpus ); précédent : 001A41; suivant : 001A43PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production.
Auteurs : Dahai Zheng ; Gang Chen ; Beichu Guo ; Genhong Cheng ; Hong TangSource :
- Cell research [ 1748-7838 ] ; 2008.
English descriptors
- KwdEn :
- Animals, Cell Line, Cells, Cultured, Coronavirus (genetics), Coronavirus (metabolism), HeLa Cells, Humans, Interferon Regulatory Factor-3 (metabolism), Interferon Type I (genetics), Interferon Type I (metabolism), Interferon-alpha (genetics), Interferon-alpha (metabolism), Interferon-beta (genetics), Interferon-beta (metabolism), Mice, Murine hepatitis virus (genetics), Murine hepatitis virus (metabolism), Papain (metabolism), SARS Virus (genetics), SARS Virus (metabolism), Severe Acute Respiratory Syndrome (genetics), Severe Acute Respiratory Syndrome (metabolism), Severe Acute Respiratory Syndrome (virology), Ubiquitination, Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , genetics : Interferon Type I, Interferon-alpha, Interferon-beta, Viral Nonstructural Proteins.
- chemical , metabolism : Interferon Regulatory Factor-3, Interferon Type I, Interferon-alpha, Interferon-beta, Papain, Viral Nonstructural Proteins.
- genetics : Coronavirus, Murine hepatitis virus, SARS Virus, Severe Acute Respiratory Syndrome.
- metabolism : Coronavirus, Murine hepatitis virus, SARS Virus, Severe Acute Respiratory Syndrome.
- virology : Severe Acute Respiratory Syndrome.
- Animals, Cell Line, Cells, Cultured, HeLa Cells, Humans, Mice, Ubiquitination.
Abstract
Infections by coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) result in very little type I interferon (IFN) production by host cells, which is potentially responsible for the rapid viral growth and severe immunopathology associated with SARS. However, the molecular mechanisms for the low IFN production in cells infected with coronaviruses remain unclear. Here, we provide evidence that Papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, can bind to IRF3, cause its deubiquitination and prevent its nuclear translocation. As a consequence, co-expression of PLP2 strongly inhibits CARDIF-, TBK1- and IRF3-mediated IFNbeta reporter activities. In addition, we show that wild-type PLP2 but not the mutant PLP2 lacking the deubiquitinase (DUB) activity can reduce IFN induction and promote viral growth in cells infected with VSV. Thus, our study uncovered a viral DUB which coronaviruses may use to escape from the host innate antiviral responses.
DOI: 10.1038/cr.2008.294
PubMed: 18957937
Links to Exploration step
pubmed:18957937Le document en format XML
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type="chemical" qualifier="metabolism" xml:lang="en"><term>Interferon Regulatory Factor-3</term><term>Interferon Type I</term><term>Interferon-alpha</term><term>Interferon-beta</term><term>Papain</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronavirus</term><term>Murine hepatitis virus</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronavirus</term><term>Murine hepatitis virus</term><term>SARS Virus</term><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Severe Acute Respiratory Syndrome</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Cell Line</term><term>Cells, Cultured</term><term>HeLa Cells</term><term>Humans</term><term>Mice</term><term>Ubiquitination</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Infections by coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) result in very little type I interferon (IFN) production by host cells, which is potentially responsible for the rapid viral growth and severe immunopathology associated with SARS. However, the molecular mechanisms for the low IFN production in cells infected with coronaviruses remain unclear. Here, we provide evidence that Papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, can bind to IRF3, cause its deubiquitination and prevent its nuclear translocation. As a consequence, co-expression of PLP2 strongly inhibits CARDIF-, TBK1- and IRF3-mediated IFNbeta reporter activities. In addition, we show that wild-type PLP2 but not the mutant PLP2 lacking the deubiquitinase (DUB) activity can reduce IFN induction and promote viral growth in cells infected with VSV. Thus, our study uncovered a viral DUB which coronaviruses may use to escape from the host innate antiviral responses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">18957937</PMID><DateCompleted><Year>2008</Year><Month>12</Month><Day>02</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Electronic">1748-7838</ISSN><JournalIssue CitedMedium="Internet"><Volume>18</Volume><Issue>11</Issue><PubDate><Year>2008</Year><Month>Nov</Month></PubDate></JournalIssue><Title>Cell research</Title><ISOAbbreviation>Cell Res.</ISOAbbreviation></Journal><ArticleTitle>PLP2, a potent deubiquitinase from murine hepatitis virus, strongly inhibits cellular type I interferon production.</ArticleTitle><Pagination><MedlinePgn>1105-13</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1038/cr.2008.294</ELocationID><Abstract><AbstractText>Infections by coronaviruses such as severe acute respiratory syndrome (SARS) coronavirus (SCoV) and mouse hepatitis virus A59 (MHV-A59) result in very little type I interferon (IFN) production by host cells, which is potentially responsible for the rapid viral growth and severe immunopathology associated with SARS. However, the molecular mechanisms for the low IFN production in cells infected with coronaviruses remain unclear. Here, we provide evidence that Papain-like protease domain 2 (PLP2), a catalytic domain of the nonstructural protein 3 (nsp3) of MHV-A59, can bind to IRF3, cause its deubiquitination and prevent its nuclear translocation. As a consequence, co-expression of PLP2 strongly inhibits CARDIF-, TBK1- and IRF3-mediated IFNbeta reporter activities. In addition, we show that wild-type PLP2 but not the mutant PLP2 lacking the deubiquitinase (DUB) activity can reduce IFN induction and promote viral growth in cells infected with VSV. Thus, our study uncovered a viral DUB which coronaviruses may use to escape from the host innate antiviral responses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Zheng</LastName><ForeName>Dahai</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Center for Infection and Immunity, Institute of Biophysics, Chinese Academy of Sciences, 15 Da Tun Road, Chaoyang District, Beijing 100101, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Gang</ForeName><Initials>G</Initials></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Beichu</ForeName><Initials>B</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><PublicationTypeList><PublicationType UI="D016428">Journal 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