Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities.
Identifieur interne : 001B31 ( Main/Curation ); précédent : 001B30; suivant : 001B32Nidovirus 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 [ 1872-7492 ] ; 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, members of the order Nidovirales, 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.
DOI: 10.1016/j.virusres.2014.01.025
PubMed: 24512893
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: Pour aller vers cette notice dans l'étape Curation :001A61
- to stream PubMed, to step Curation: Pour aller vers cette notice dans l'étape Curation :001A61
- to stream PubMed, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :001787
- to stream Ncbi, to step Merge: Pour aller vers cette notice dans l'étape Curation :000C82
- to stream Ncbi, to step Curation: Pour aller vers cette notice dans l'étape Curation :000C82
- to stream Ncbi, to step Checkpoint: Pour aller vers cette notice dans l'étape Curation :000C82
- to stream Main, to step Merge: Pour aller vers cette notice dans l'étape Curation :001B40
Links to Exploration step
pubmed:24512893Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">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:affiliation>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States.</nlm:affiliation>
<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:affiliation>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States.</nlm:affiliation>
<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:affiliation>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States.</nlm:affiliation>
<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:affiliation>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States. Electronic address: sbaker1@lumc.edu.</nlm:affiliation>
<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">PubMed</idno>
<date when="2014">2014</date>
<idno type="RBID">pubmed:24512893</idno>
<idno type="pmid">24512893</idno>
<idno type="doi">10.1016/j.virusres.2014.01.025</idno>
<idno type="wicri:Area/PubMed/Corpus">001A61</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001A61</idno>
<idno type="wicri:Area/PubMed/Curation">001A61</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Curation">001A61</idno>
<idno type="wicri:Area/PubMed/Checkpoint">001787</idno>
<idno type="wicri:explorRef" wicri:stream="Checkpoint" wicri:step="PubMed">001787</idno>
<idno type="wicri:Area/Ncbi/Merge">000C82</idno>
<idno type="wicri:Area/Ncbi/Curation">000C82</idno>
<idno type="wicri:Area/Ncbi/Checkpoint">000C82</idno>
<idno type="wicri:Area/Main/Merge">001B40</idno>
<idno type="wicri:Area/Main/Curation">001B31</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">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:affiliation>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States.</nlm:affiliation>
<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:affiliation>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States.</nlm:affiliation>
<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:affiliation>Department of Biological Sciences, Purdue University, Hockmeyer Hall of Structural Biology, 240 S. Martin Jischke Drive, West Lafayette, IN 47907, United States.</nlm:affiliation>
<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:affiliation>Department of Microbiology and Immunology, Loyola University Chicago, Stritch School of Medicine, 2160 S. First Avenue, Maywood, IL 60153, United States. Electronic address: sbaker1@lumc.edu.</nlm:affiliation>
<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="eISSN">1872-7492</idno>
<imprint><date when="2014" type="published">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">Coronaviruses and arteriviruses, members of the order Nidovirales, 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. </div>
</front>
</TEI>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Sante/explor/MersV1/Data/Main/Curation
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 001B31 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/Main/Curation/biblio.hfd -nk 001B31 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Sante |area= MersV1 |flux= Main |étape= Curation |type= RBID |clé= pubmed:24512893 |texte= Nidovirus papain-like proteases: multifunctional enzymes with protease, deubiquitinating and deISGylating activities. }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Curation/RBID.i -Sk "pubmed:24512893" \ | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Curation/biblio.hfd \ | NlmPubMed2Wicri -a MersV1
This area was generated with Dilib version V0.6.33. |