Nidovirus papain-like proteases: Multifunctional enzymes with protease, deubiquitinating and deISGylating activities
Identifieur interne : 001612 ( Main/Exploration ); précédent : 001611; suivant : 001613Nidovirus 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.
Descripteurs français
- KwdFr :
- MESH :
- enzymologie : Nidovirales.
- métabolisme : Enzymes multifonctionnelles, Peptide hydrolases, Ubiquitin-specific proteases.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Multifunctional Enzymes, Peptide Hydrolases, Ubiquitin-Specific Proteases.
- enzymology : Nidovirales.
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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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><keywords scheme="KwdEn" xml:lang="en"><term>Multifunctional Enzymes (metabolism)</term><term>Nidovirales (enzymology)</term><term>Peptide Hydrolases (metabolism)</term><term>Ubiquitin-Specific Proteases (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Enzymes multifonctionnelles (métabolisme)</term><term>Nidovirales (enzymologie)</term><term>Peptide hydrolases (métabolisme)</term><term>Ubiquitin-specific proteases (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Multifunctional Enzymes</term><term>Peptide Hydrolases</term><term>Ubiquitin-Specific Proteases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Nidovirales</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Nidovirales</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Enzymes multifonctionnelles</term><term>Peptide hydrolases</term><term>Ubiquitin-specific proteases</term></keywords></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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Tang</name></author></analytic></biblStruct></listBibl></div1></back></TEI><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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