The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase.
Identifieur interne : 002289 ( Ncbi/Merge ); précédent : 002288; suivant : 002290The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase.
Auteurs : Dang Wang [République populaire de Chine] ; Liurong Fang ; Ping Li ; Li Sun ; Jinxiu Fan ; Qingye Zhang ; Rui Luo ; Xiangtao Liu ; Kui Li ; Huanchun Chen ; Zhongbin Chen ; Shaobo XiaoSource :
- Journal of virology [ 1098-5514 ] ; 2011.
Descripteurs français
- KwdFr :
- Endopeptidases (métabolisme), Humains, Interféron de type I (antagonistes et inhibiteurs), Lignée cellulaire, Modèles moléculaires, Protéines virales (métabolisme), Séquence conservée, Séquence d'acides aminés, Ubiquitine (métabolisme), Virus de la fièvre aphteuse (immunologie), Virus de la fièvre aphteuse (pathogénicité).
- MESH :
- antagonistes et inhibiteurs : Interféron de type I.
- immunologie : Virus de la fièvre aphteuse.
- métabolisme : Endopeptidases, Protéines virales, Ubiquitine.
- pathogénicité : Virus de la fièvre aphteuse.
- Humains, Lignée cellulaire, Modèles moléculaires, Séquence conservée, Séquence d'acides aminés.
English descriptors
- KwdEn :
- MESH :
- chemical , antagonists & inhibitors : Interferon Type I.
- chemical , metabolism : Endopeptidases, Ubiquitin, Viral Proteins.
- immunology : Foot-and-Mouth Disease Virus.
- pathogenicity : Foot-and-Mouth Disease Virus.
- Amino Acid Sequence, Cell Line, Conserved Sequence, Humans, Models, Molecular.
Abstract
The leader proteinase (L(pro)) of foot-and-mouth disease virus (FMDV) is a papain-like proteinase that plays an important role in FMDV pathogenesis. Previously, it has been shown that L(pro) is involved in the inhibition of the type I interferon (IFN) response by FMDV. However, the underlying mechanisms remain unclear. Here we demonstrate that FMDV Lb(pro), a shorter form of L(pro), has deubiquitinating activity. Sequence alignment and structural bioinformatics analyses revealed that the catalytic residues (Cys51 and His148) are highly conserved in FMDV Lb(pro) of all seven serotypes and that the topology of FMDV Lb(pro) is remarkably similar to that of ubiquitin-specific protease 14 (USP14), a cellular deubiquitylation enzyme (DUB), and to that of severe acute respiratory syndrome coronavirus (SARS-CoV) papain-like protease (PLpro), a coronaviral DUB. Both purified Lb(pro) protein and in vivo ectopically expressed Lb(pro) removed ubiquitin (Ub) moieties from cellular substrates, acting on both lysine-48- and lysine-63-linked polyubiquitin chains. Furthermore, Lb(pro) significantly inhibited ubiquitination of retinoic acid-inducible gene I (RIG-I), TANK-binding kinase 1 (TBK1), TNF receptor-associated factor 6 (TRAF6), and TRAF3, key signaling molecules in activation of type I IFN response. Mutations in Lb(pro) that ablate the catalytic activity (C51A or D163N/D164N) or disrupt the SAP (for SAF-A/B, Acinus, and PIAS) domain (I83A/L86A) abrogated the DUB activity of Lb(pro) as well as its ability to block signaling to the IFN-β promoter. Collectively, these results demonstrate that FMDV Lb(pro) possesses DUB activity in addition to serving as a viral proteinase and describe a novel mechanism evolved by FMDV to counteract host innate antiviral responses.
DOI: 10.1128/JVI.02589-10
PubMed: 21307201
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pubmed:21307201Le document en format XML
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type="abstract" xml:lang="en">The leader proteinase (L(pro)) of foot-and-mouth disease virus (FMDV) is a papain-like proteinase that plays an important role in FMDV pathogenesis. Previously, it has been shown that L(pro) is involved in the inhibition of the type I interferon (IFN) response by FMDV. However, the underlying mechanisms remain unclear. Here we demonstrate that FMDV Lb(pro), a shorter form of L(pro), has deubiquitinating activity. Sequence alignment and structural bioinformatics analyses revealed that the catalytic residues (Cys51 and His148) are highly conserved in FMDV Lb(pro) of all seven serotypes and that the topology of FMDV Lb(pro) is remarkably similar to that of ubiquitin-specific protease 14 (USP14), a cellular deubiquitylation enzyme (DUB), and to that of severe acute respiratory syndrome coronavirus (SARS-CoV) papain-like protease (PLpro), a coronaviral DUB. Both purified Lb(pro) protein and in vivo ectopically expressed Lb(pro) removed ubiquitin (Ub) moieties from cellular substrates, acting on both lysine-48- and lysine-63-linked polyubiquitin chains. Furthermore, Lb(pro) significantly inhibited ubiquitination of retinoic acid-inducible gene I (RIG-I), TANK-binding kinase 1 (TBK1), TNF receptor-associated factor 6 (TRAF6), and TRAF3, key signaling molecules in activation of type I IFN response. Mutations in Lb(pro) that ablate the catalytic activity (C51A or D163N/D164N) or disrupt the SAP (for SAF-A/B, Acinus, and PIAS) domain (I83A/L86A) abrogated the DUB activity of Lb(pro) as well as its ability to block signaling to the IFN-β promoter. Collectively, these results demonstrate that FMDV Lb(pro) possesses DUB activity in addition to serving as a viral proteinase and describe a novel mechanism evolved by FMDV to counteract host innate antiviral responses.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">21307201</PMID><DateCompleted><Year>2011</Year><Month>05</Month><Day>18</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>85</Volume><Issue>8</Issue><PubDate><Year>2011</Year><Month>Apr</Month></PubDate></JournalIssue><Title>Journal of virology</Title><ISOAbbreviation>J. Virol.</ISOAbbreviation></Journal><ArticleTitle>The leader proteinase of foot-and-mouth disease virus negatively regulates the type I interferon pathway by acting as a viral deubiquitinase.</ArticleTitle><Pagination><MedlinePgn>3758-66</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.02589-10</ELocationID><Abstract><AbstractText>The leader proteinase (L(pro)) of foot-and-mouth disease virus (FMDV) is a papain-like proteinase that plays an important role in FMDV pathogenesis. Previously, it has been shown that L(pro) is involved in the inhibition of the type I interferon (IFN) response by FMDV. However, the underlying mechanisms remain unclear. Here we demonstrate that FMDV Lb(pro), a shorter form of L(pro), has deubiquitinating activity. Sequence alignment and structural bioinformatics analyses revealed that the catalytic residues (Cys51 and His148) are highly conserved in FMDV Lb(pro) of all seven serotypes and that the topology of FMDV Lb(pro) is remarkably similar to that of ubiquitin-specific protease 14 (USP14), a cellular deubiquitylation enzyme (DUB), and to that of severe acute respiratory syndrome coronavirus (SARS-CoV) papain-like protease (PLpro), a coronaviral DUB. Both purified Lb(pro) protein and in vivo ectopically expressed Lb(pro) removed ubiquitin (Ub) moieties from cellular substrates, acting on both lysine-48- and lysine-63-linked polyubiquitin chains. Furthermore, Lb(pro) significantly inhibited ubiquitination of retinoic acid-inducible gene I (RIG-I), TANK-binding kinase 1 (TBK1), TNF receptor-associated factor 6 (TRAF6), and TRAF3, key signaling molecules in activation of type I IFN response. Mutations in Lb(pro) that ablate the catalytic activity (C51A or D163N/D164N) or disrupt the SAP (for SAF-A/B, Acinus, and PIAS) domain (I83A/L86A) abrogated the DUB activity of Lb(pro) as well as its ability to block signaling to the IFN-β promoter. Collectively, these results demonstrate that FMDV Lb(pro) possesses DUB activity in addition to serving as a viral proteinase and describe a novel mechanism evolved by FMDV to counteract host innate antiviral responses.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Dang</ForeName><Initials>D</Initials><AffiliationInfo><Affiliation>Laboratory of Infectious Diseases, College of Veterinary Medicine, Huazhong Agricultural University, 1 Shi-zi-shan Street, Wuhan 430070, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Fang</LastName><ForeName>Liurong</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Ping</ForeName><Initials>P</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Li</ForeName><Initials>L</Initials></Author><Author ValidYN="Y"><LastName>Fan</LastName><ForeName>Jinxiu</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Zhang</LastName><ForeName>Qingye</ForeName><Initials>Q</Initials></Author><Author ValidYN="Y"><LastName>Luo</LastName><ForeName>Rui</ForeName><Initials>R</Initials></Author><Author ValidYN="Y"><LastName>Liu</LastName><ForeName>Xiangtao</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Li</LastName><ForeName>Kui</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Huanchun</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Zhongbin</ForeName><Initials>Z</Initials></Author><Author ValidYN="Y"><LastName>Xiao</LastName><ForeName>Shaobo</ForeName><Initials>S</Initials></Author></AuthorList><Language>eng</Language><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>09</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>J Virol</MedlineTA><NlmUniqueID>0113724</NlmUniqueID><ISSNLinking>0022-538X</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007370">Interferon Type I</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.-</RegistryNumber><NameOfSubstance UI="D010450">Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.99.-</RegistryNumber><NameOfSubstance UI="C088747">leader proteinase, foot-and-mouth disease virus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017124" MajorTopicYN="N">Conserved Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010450" MajorTopicYN="N">Endopeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D029544" MajorTopicYN="N">Foot-and-Mouth Disease Virus</DescriptorName><QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName><QualifierName UI="Q000472" MajorTopicYN="Y">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007370" 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first="Liurong" last="Fang">Liurong Fang</name><name sortKey="Li, Kui" sort="Li, Kui" uniqKey="Li K" first="Kui" last="Li">Kui Li</name><name sortKey="Li, Ping" sort="Li, Ping" uniqKey="Li P" first="Ping" last="Li">Ping Li</name><name sortKey="Liu, Xiangtao" sort="Liu, Xiangtao" uniqKey="Liu X" first="Xiangtao" last="Liu">Xiangtao Liu</name><name sortKey="Luo, Rui" sort="Luo, Rui" uniqKey="Luo R" first="Rui" last="Luo">Rui Luo</name><name sortKey="Sun, Li" sort="Sun, Li" uniqKey="Sun L" first="Li" last="Sun">Li Sun</name><name sortKey="Xiao, Shaobo" sort="Xiao, Shaobo" uniqKey="Xiao S" first="Shaobo" last="Xiao">Shaobo Xiao</name><name sortKey="Zhang, Qingye" sort="Zhang, Qingye" uniqKey="Zhang Q" first="Qingye" last="Zhang">Qingye Zhang</name></noCountry><country name="République populaire de Chine"><region name="Hubei"><name sortKey="Wang, Dang" sort="Wang, Dang" uniqKey="Wang D" first="Dang" last="Wang">Dang Wang</name></region></country></tree></affiliations></record>Pour manipuler 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