MERS-CoV papain-like protease has deISGylating and deubiquitinating activities
Identifieur interne : 001F63 ( Main/Exploration ); précédent : 001F62; suivant : 001F64MERS-CoV papain-like protease has deISGylating and deubiquitinating activities
Auteurs : Anna M. Mielech [États-Unis] ; Andy Kilianski [États-Unis] ; Yahira M. Baez-Santos [États-Unis] ; Andrew D. Mesecar [États-Unis] ; Susan C. Baker [États-Unis]Source :
- Virology [ 0042-6822 ] ; 2013.
Descripteurs français
- KwdFr :
- Coronaviridae (), Coronaviridae (enzymologie), Coronaviridae (génétique), Cytokines (génétique), Cytokines (métabolisme), Données de séquences moléculaires, Glycosylation, Humains, Infections à Coronaviridae (génétique), Infections à Coronaviridae (métabolisme), Infections à Coronaviridae (virologie), Lignée cellulaire, Papaïne (), Papaïne (génétique), Papaïne (métabolisme), Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Structure tertiaire des protéines, Séquence d'acides aminés, Ubiquitines (génétique), Ubiquitines (métabolisme), Ubiquitinylation, Virus du SRAS (enzymologie), Virus du SRAS (génétique).
- MESH :
- enzymologie : Coronaviridae, Virus du SRAS.
- génétique : Coronaviridae, Cytokines, Infections à Coronaviridae, Papaïne, Protéines virales, Ubiquitines, Virus du SRAS.
- métabolisme : Cytokines, Infections à Coronaviridae, Papaïne, Protéines virales, Ubiquitines.
- virologie : Infections à Coronaviridae.
- Coronaviridae, Données de séquences moléculaires, Glycosylation, Humains, Lignée cellulaire, Papaïne, Protéines virales, Structure tertiaire des protéines, Séquence d'acides aminés, Ubiquitinylation.
English descriptors
- KwdEn :
- Amino Acid Sequence, Cell Line, Coronaviridae (chemistry), Coronaviridae (enzymology), Coronaviridae (genetics), Coronaviridae Infections (genetics), Coronaviridae Infections (metabolism), Coronaviridae Infections (virology), Cytokines (genetics), Cytokines (metabolism), Glycosylation, Humans, Molecular Sequence Data, Papain (chemistry), Papain (genetics), Papain (metabolism), Protein Structure, Tertiary, SARS Virus (enzymology), SARS Virus (genetics), Ubiquitination, Ubiquitins (genetics), Ubiquitins (metabolism), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Papain, Viral Proteins.
- chemical , genetics : Cytokines, Papain, Ubiquitins, Viral Proteins.
- chemistry : Coronaviridae.
- enzymology : Coronaviridae, SARS Virus.
- genetics : Coronaviridae, Coronaviridae Infections, SARS Virus.
- metabolism : Coronaviridae Infections, Cytokines, Papain, Ubiquitins, Viral Proteins.
- virology : Coronaviridae Infections.
- Amino Acid Sequence, Cell Line, Glycosylation, Humans, Molecular Sequence Data, Protein Structure, Tertiary, Ubiquitination.
Abstract
Coronaviruses encode papain-like proteases (PLpro) that are often multifunctional enzymes with protease activity to process the viral replicase polyprotein and deubiquitinating (DUB)/deISGylating activity, which is hypothesized to modify the innate immune response to infection. Here, we investigate the predicted DUB activity of the PLpro domain of the recently described Middle East Respiratory Syndrome Coronavirus (MERS-CoV). We found that expression of MERS-CoV PLpro reduces the levels of ubiquitinated and ISGylated host cell proteins; consistent with multifunctional PLpro activity. Further, we compared the ability of MERS-CoV PLpro and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) PLpro to block innate immune signaling of proinflammatory cytokines. We show that expression of SARS-CoV and MERS-CoV PLpros blocks upregulation of cytokines CCL5, IFN-β and CXCL10 in stimulated cells. Overall these results indicate that the PLpro domains of MERS-CoV and SARS-CoV have the potential to modify the innate immune response to viral infection and contribute to viral pathogenesis.
Url:
DOI: 10.1016/j.virol.2013.11.040
PubMed: 24503068
PubMed Central: 3957432
Affiliations:
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Le document en format XML
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Mielech</name><affiliation wicri:level="4"><nlm:aff id="aff0005">Department Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153</wicri:regionArea><placeName><region type="state">Illinois</region><settlement type="city">Chicago</settlement></placeName><orgName type="university">Université de Chicago</orgName></affiliation></author><author><name sortKey="Kilianski, Andy" sort="Kilianski, Andy" uniqKey="Kilianski A" first="Andy" last="Kilianski">Andy Kilianski</name><affiliation wicri:level="4"><nlm:aff id="aff0005">Department Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153</wicri:regionArea><placeName><region type="state">Illinois</region><settlement type="city">Chicago</settlement></placeName><orgName type="university">Université de Chicago</orgName></affiliation></author><author><name sortKey="Baez Santos, Yahira M" sort="Baez Santos, Yahira M" uniqKey="Baez Santos Y" first="Yahira M." last="Baez-Santos">Yahira M. Baez-Santos</name><affiliation wicri:level="2"><nlm:aff id="aff0010">Department of Biological Sciences, Purdue University, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, 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, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biological Sciences, Purdue University, 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="4"><nlm:aff id="aff0005">Department Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department Microbiology and Immunology, Loyola University of Chicago, Stritch School of Medicine, 2160 S. First Ave., Maywood, IL 60153</wicri:regionArea><placeName><region type="state">Illinois</region><settlement type="city">Chicago</settlement></placeName><orgName type="university">Université de Chicago</orgName></affiliation></author></analytic><series><title level="j">Virology</title><idno type="ISSN">0042-6822</idno><idno type="eISSN">1096-0341</idno><imprint><date when="2013">2013</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Line</term><term>Coronaviridae (chemistry)</term><term>Coronaviridae (enzymology)</term><term>Coronaviridae (genetics)</term><term>Coronaviridae Infections (genetics)</term><term>Coronaviridae Infections (metabolism)</term><term>Coronaviridae Infections (virology)</term><term>Cytokines (genetics)</term><term>Cytokines (metabolism)</term><term>Glycosylation</term><term>Humans</term><term>Molecular Sequence Data</term><term>Papain (chemistry)</term><term>Papain (genetics)</term><term>Papain (metabolism)</term><term>Protein Structure, Tertiary</term><term>SARS Virus (enzymology)</term><term>SARS Virus (genetics)</term><term>Ubiquitination</term><term>Ubiquitins (genetics)</term><term>Ubiquitins (metabolism)</term><term>Viral Proteins (chemistry)</term><term>Viral Proteins (genetics)</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Coronaviridae ()</term><term>Coronaviridae (enzymologie)</term><term>Coronaviridae (génétique)</term><term>Cytokines (génétique)</term><term>Cytokines (métabolisme)</term><term>Données de séquences moléculaires</term><term>Glycosylation</term><term>Humains</term><term>Infections à Coronaviridae (génétique)</term><term>Infections à Coronaviridae (métabolisme)</term><term>Infections à Coronaviridae (virologie)</term><term>Lignée cellulaire</term><term>Papaïne ()</term><term>Papaïne (génétique)</term><term>Papaïne (métabolisme)</term><term>Protéines virales ()</term><term>Protéines virales (génétique)</term><term>Protéines virales (métabolisme)</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Ubiquitines (génétique)</term><term>Ubiquitines (métabolisme)</term><term>Ubiquitinylation</term><term>Virus du SRAS (enzymologie)</term><term>Virus du SRAS (génétique)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Papain</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cytokines</term><term>Papain</term><term>Ubiquitins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Coronaviridae</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coronaviridae</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coronaviridae</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Coronaviridae</term><term>Coronaviridae Infections</term><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Coronaviridae</term><term>Cytokines</term><term>Infections à Coronaviridae</term><term>Papaïne</term><term>Protéines virales</term><term>Ubiquitines</term><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Coronaviridae Infections</term><term>Cytokines</term><term>Papain</term><term>Ubiquitins</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cytokines</term><term>Infections à Coronaviridae</term><term>Papaïne</term><term>Protéines virales</term><term>Ubiquitines</term></keywords><keywords scheme="MESH" qualifier="virologie" xml:lang="fr"><term>Infections à Coronaviridae</term></keywords><keywords scheme="MESH" qualifier="virology" xml:lang="en"><term>Coronaviridae Infections</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Cell Line</term><term>Glycosylation</term><term>Humans</term><term>Molecular Sequence Data</term><term>Protein Structure, Tertiary</term><term>Ubiquitination</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Coronaviridae</term><term>Données de séquences moléculaires</term><term>Glycosylation</term><term>Humains</term><term>Lignée cellulaire</term><term>Papaïne</term><term>Protéines virales</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Ubiquitinylation</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p>Coronaviruses encode papain-like proteases (PLpro) that are often multifunctional enzymes with protease activity to process the viral replicase polyprotein and deubiquitinating (DUB)/deISGylating activity, which is hypothesized to modify the innate immune response to infection. Here, we investigate the predicted DUB activity of the PLpro domain of the recently described Middle East Respiratory Syndrome Coronavirus (MERS-CoV). We found that expression of MERS-CoV PLpro reduces the levels of ubiquitinated and ISGylated host cell proteins; consistent with multifunctional PLpro activity. Further, we compared the ability of MERS-CoV PLpro and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) PLpro to block innate immune signaling of proinflammatory cytokines. We show that expression of SARS-CoV and MERS-CoV PLpros blocks upregulation of cytokines CCL5, IFN-β and CXCL10 in stimulated cells. Overall these results indicate that the PLpro domains of MERS-CoV and SARS-CoV have the potential to modify the innate immune response to viral infection and contribute to viral pathogenesis.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Assiri, A" uniqKey="Assiri A">A. 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Gorbalenya</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Illinois</li><li>Indiana</li></region><settlement><li>Chicago</li></settlement><orgName><li>Université de Chicago</li></orgName></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="Baez Santos, Yahira M" sort="Baez Santos, Yahira M" uniqKey="Baez Santos Y" first="Yahira M." last="Baez-Santos">Yahira M. Baez-Santos</name><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><name sortKey="Kilianski, Andy" sort="Kilianski, Andy" uniqKey="Kilianski A" first="Andy" last="Kilianski">Andy Kilianski</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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