Nidovirus papain-like proteases: Multifunctional enzymes with protease, deubiquitinating and deISGylating activities
Identifieur interne : 000875 ( Pmc/Checkpoint ); précédent : 000874; suivant : 000876Nidovirus papain-like proteases: Multifunctional enzymes with protease, deubiquitinating and deISGylating activities
Auteurs : Anna M. Mielech [États-Unis] ; Yafang Chen [États-Unis] ; Andrew D. Mesecar [États-Unis] ; Susan C. Baker [États-Unis]Source :
- Virus Research [ 0168-1702 ] ; 2014.
Abstract
Coronaviruses and arteriviruses encode papain-like protease domains that process the replicase polyprotein and are required for viral replication. Many viral papain-like proteases are multifunctional and have protease, deubiquitinating and deISGylating activity. Structural and enzymatic studies revealed the multifunctional nature of coronavirus and arterivirus papain-like proteases. Viral DUB and deISGylating activity is proposed to modulate the innate immune response. An arterivirus papain-like protease has been shown to modulate the innate immune response to viral infection.
Url:
DOI: 10.1016/j.virusres.2014.01.025
PubMed: 24512893
PubMed Central: 4125544
Affiliations:
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Mesecar</name><affiliation wicri:level="2"><nlm:aff id="aff0010">Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><affiliation wicri:level="2"><nlm:aff id="aff0005">Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153</wicri:regionArea><placeName><region type="state">Illinois</region></placeName></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">24512893</idno><idno type="pmc">4125544</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4125544</idno><idno type="RBID">PMC:4125544</idno><idno type="doi">10.1016/j.virusres.2014.01.025</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">001596</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001596</idno><idno type="wicri:Area/Pmc/Curation">001596</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001596</idno><idno type="wicri:Area/Pmc/Checkpoint">000875</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000875</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Nidovirus papain-like proteases: Multifunctional enzymes with protease, deubiquitinating and deISGylating activities</title><author><name sortKey="Mielech, Anna M" sort="Mielech, Anna M" uniqKey="Mielech A" first="Anna M." last="Mielech">Anna M. Mielech</name><affiliation wicri:level="2"><nlm:aff id="aff0005">Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153</wicri:regionArea><placeName><region type="state">Illinois</region></placeName></affiliation></author><author><name sortKey="Chen, Yafang" sort="Chen, Yafang" uniqKey="Chen Y" first="Yafang" last="Chen">Yafang Chen</name><affiliation wicri:level="2"><nlm:aff id="aff0010">Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><affiliation wicri:level="2"><nlm:aff id="aff0010">Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907</wicri:regionArea><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><affiliation wicri:level="2"><nlm:aff id="aff0005">Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153</wicri:regionArea><placeName><region type="state">Illinois</region></placeName></affiliation></author></analytic><series><title level="j">Virus Research</title><idno type="ISSN">0168-1702</idno><idno type="eISSN">1872-7492</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Highlights</title><p><list list-type="simple" id="lis0005"><list-item id="lsti0005"><label>•</label><p id="par0005">Coronaviruses and arteriviruses encode papain-like protease domains that process the replicase polyprotein and are required for viral replication.</p></list-item><list-item id="lsti0010"><label>•</label><p id="par0010">Many viral papain-like proteases are multifunctional and have protease, deubiquitinating and deISGylating activity.</p></list-item><list-item id="lsti0015"><label>•</label><p id="par0015">Structural and enzymatic studies revealed the multifunctional nature of coronavirus and arterivirus papain-like proteases.</p></list-item><list-item id="lsti0020"><label>•</label><p id="par0020">Viral DUB and deISGylating activity is proposed to modulate the innate immune response.</p></list-item><list-item id="lsti0025"><label>•</label><p id="par0025">An arterivirus papain-like protease has been shown to modulate the innate immune response to viral infection.</p></list-item></list></p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Baker, S" uniqKey="Baker S">S. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Virus Res</journal-id><journal-id journal-id-type="iso-abbrev">Virus Res</journal-id><journal-title-group><journal-title>Virus Research</journal-title></journal-title-group><issn pub-type="ppub">0168-1702</issn><issn pub-type="epub">1872-7492</issn><publisher><publisher-name>Elsevier B.V.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">24512893</article-id><article-id pub-id-type="pmc">4125544</article-id><article-id pub-id-type="publisher-id">S0168-1702(14)00040-9</article-id><article-id pub-id-type="doi">10.1016/j.virusres.2014.01.025</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Nidovirus papain-like proteases: Multifunctional enzymes with protease, deubiquitinating and deISGylating activities</article-title></title-group><contrib-group><contrib contrib-type="author" id="aut0005"><name><surname>Mielech</surname><given-names>Anna M.</given-names></name><xref rid="aff0005" ref-type="aff">a</xref></contrib><contrib contrib-type="author" id="aut0010"><name><surname>Chen</surname><given-names>Yafang</given-names></name><xref rid="aff0010" ref-type="aff">b</xref></contrib><contrib contrib-type="author" id="aut0015"><name><surname>Mesecar</surname><given-names>Andrew D.</given-names></name><xref rid="aff0010" ref-type="aff">b</xref></contrib><contrib contrib-type="author" id="aut0020"><name><surname>Baker</surname><given-names>Susan C.</given-names></name><email>sbaker1@lumc.edu</email><xref rid="aff0005" ref-type="aff">a</xref><xref rid="cor0005" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="aff0005"><label>a</label>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States</aff><aff id="aff0010"><label>b</label>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States</aff><author-notes><corresp id="cor0005"><label>⁎</label>Corresponding author. Tel.: +1 708 216 6910; fax: +1 708 216 9574. <email>sbaker1@lumc.edu</email></corresp></author-notes><pub-date pub-type="pmc-release"><day>7</day><month>2</month><year>2014</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><day>19</day><month>12</month><year>2014</year></pub-date><pub-date pub-type="epub"><day>7</day><month>2</month><year>2014</year></pub-date><volume>194</volume><fpage>184</fpage><lpage>190</lpage><permissions><copyright-statement>Copyright © 2014 Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2014</copyright-year><copyright-holder>Elsevier B.V.</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract abstract-type="author-highlights" id="abs0005"><title>Highlights</title><p><list list-type="simple" id="lis0005"><list-item id="lsti0005"><label>•</label><p id="par0005">Coronaviruses and arteriviruses encode papain-like protease domains that process the replicase polyprotein and are required for viral replication.</p></list-item><list-item id="lsti0010"><label>•</label><p id="par0010">Many viral papain-like proteases are multifunctional and have protease, deubiquitinating and deISGylating activity.</p></list-item><list-item id="lsti0015"><label>•</label><p id="par0015">Structural and enzymatic studies revealed the multifunctional nature of coronavirus and arterivirus papain-like proteases.</p></list-item><list-item id="lsti0020"><label>•</label><p id="par0020">Viral DUB and deISGylating activity is proposed to modulate the innate immune response.</p></list-item><list-item id="lsti0025"><label>•</label><p id="par0025">An arterivirus papain-like protease has been shown to modulate the innate immune response to viral infection.</p></list-item></list></p></abstract><abstract id="abs0010"><p>Coronaviruses and arteriviruses, members of the order <italic>Nidovirales</italic>, are positive strand RNA viruses that encode large replicase polyproteins that are processed by viral proteases to generate the nonstructural proteins which mediate viral RNA synthesis. The viral papain-like proteases (PLPs) are critical for processing the amino-terminal end of the replicase and are attractive targets for antiviral therapies. With the analysis of the papain-like protease of Severe Acute Respiratory Syndrome coronavirus (SARS-CoV), came the realization of the multifunctional nature of these enzymes. Structural and enzymatic studies revealed that SARS-CoV PLpro can act as both a protease to cleave peptide bonds and also as a deubiquitinating (DUB) enzyme to cleave the isopeptide bonds found in polyubiquitin chains. Furthermore, viral DUBs can also remove the protective effect of conjugated ubiquitin-like molecules such as interferon stimulated gene 15 (ISG15). Extension of these studies to other coronaviruses and arteriviruses led to the realization that viral protease/DUB activity is conserved in many family members. Overexpression studies revealed that viral protease/DUB activity can modulate or block activation of the innate immune response pathway. Importantly, mutations that alter DUB activity but not viral protease activity have been identified and arteriviruses expressing DUB mutants stimulated higher levels of acute inflammatory cytokines after infection. Further understanding of the multifunctional nature of the Nidovirus PLP/DUBs may facilitate vaccine development. Here, we review studies describing the PLPs’ enzymatic activity and their role in virus pathogenesis.</p></abstract><kwd-group id="kwd0005"><title>Keywords</title><kwd>Coronavirus</kwd><kwd>Arterivirus</kwd><kwd>Papain-like protease</kwd><kwd>Deubiquitinating enzyme</kwd><kwd>DeISGylating activity</kwd><kwd>MERS-CoV</kwd></kwd-group></article-meta></front></pmc><affiliations><list><country><li>États-Unis</li></country><region><li>Illinois</li><li>Indiana</li></region></list><tree><country name="États-Unis"><region name="Illinois"><name sortKey="Mielech, Anna M" sort="Mielech, Anna M" uniqKey="Mielech A" first="Anna M." last="Mielech">Anna M. Mielech</name></region><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><name sortKey="Chen, Yafang" sort="Chen, Yafang" uniqKey="Chen Y" first="Yafang" last="Chen">Yafang Chen</name><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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