SARS-CoV ORF1b-encoded nonstructural proteins 12-16: Replicative enzymes as antiviral targets
Identifieur interne : 000003 ( PascalFrancis/Checkpoint ); précédent : 000002; suivant : 000004SARS-CoV ORF1b-encoded nonstructural proteins 12-16: Replicative enzymes as antiviral targets
Auteurs : Lorenzo Subissi [France] ; Isabelle Imbert [France] ; François Ferron [France] ; Axelle Collet [France] ; Bruno Coutard [France] ; Etienne Decroly [France] ; Bruno Canard [France]Source :
- Antiviral research [ 0166-3542 ] ; 2014.
Descripteurs français
- Pascal (Inist)
- Wicri :
- topic : Enzyme.
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Abstract
The SARS (severe acute respiratory syndrome) pandemic caused ten years ago by the SARS-coronavirus (SARS-CoV) has stimulated a number of studies on the molecular biology of coronaviruses. This research has provided significant new insight into many mechanisms used by the coronavirus replication-transcription complex (RTC). The RTC directs and coordinates processes in order to replicate and transcribe the coronavirus genome, a single-stranded, positive-sense RNA of outstanding length (∼27-32 kilobases). Here, we review the up-to-date knowledge on SARS-CoV replicative enzymes encoded in the ORF1b, i.e., the main RNA-dependent RNA polymerase (nsp12), the helicase/triphosphatase (nsp13), two unusual ribonucleases (nsp14, nsp15) and RNA-cap methyltransferases (nsp14, nsp16). We also review how these enzymes co-operate with other viral co-factors (nsp7, nsp8, and nsp10) to regulate their activity. These last ten years of research on SARS-CoV have considerably contributed to unravel structural and functional details of one of the most fascinating replication/transcription machineries of the RNA virus world. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses".
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CNRS et Aix-Marseille Universite, ESIL Case 925</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Decroly, Etienne" sort="Decroly, Etienne" uniqKey="Decroly E" first="Etienne" last="Decroly">Etienne Decroly</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 - CNRS et Aix-Marseille Universite, ESIL Case 925</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 - CNRS et Aix-Marseille Universite, ESIL Case 925</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></inist:fA14><country>France</country><placeName><region type="region" nuts="2">Provence-Alpes-Côte d'Azur</region><settlement type="city">Marseille</settlement></placeName></affiliation></author></analytic><series><title level="j" type="main">Antiviral research</title><title level="j" type="abbreviated">Antivir. res.</title><idno type="ISSN">0166-3542</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Antiviral research</title><title level="j" type="abbreviated">Antivir. res.</title><idno type="ISSN">0166-3542</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral</term><term>Enzyme</term><term>Protein</term><term>Replication</term><term>Severe acute respiratory syndrome virus</term><term>Target</term><term>Targeting</term><term>Transcription</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Virus syndrome respiratoire aigu sévère</term><term>Protéine</term><term>Enzyme</term><term>Antiviral</term><term>Cible</term><term>Ciblage</term><term>Réplication</term><term>Transcription</term></keywords><keywords scheme="Wicri" type="topic" xml:lang="fr"><term>Enzyme</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The SARS (severe acute respiratory syndrome) pandemic caused ten years ago by the SARS-coronavirus (SARS-CoV) has stimulated a number of studies on the molecular biology of coronaviruses. This research has provided significant new insight into many mechanisms used by the coronavirus replication-transcription complex (RTC). The RTC directs and coordinates processes in order to replicate and transcribe the coronavirus genome, a single-stranded, positive-sense RNA of outstanding length (∼27-32 kilobases). Here, we review the up-to-date knowledge on SARS-CoV replicative enzymes encoded in the ORF1b, i.e., the main RNA-dependent RNA polymerase (nsp12), the helicase/triphosphatase (nsp13), two unusual ribonucleases (nsp14, nsp15) and RNA-cap methyltransferases (nsp14, nsp16). We also review how these enzymes co-operate with other viral co-factors (nsp7, nsp8, and nsp10) to regulate their activity. These last ten years of research on SARS-CoV have considerably contributed to unravel structural and functional details of one of the most fascinating replication/transcription machineries of the RNA virus world. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses".</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0166-3542</s0></fA01><fA02 i1="01"><s0>ARSRDR</s0></fA02><fA03 i2="1"><s0>Antivir. res.</s0></fA03><fA05><s2>101</s2></fA05><fA08 i1="01" i2="1" l="ENG"><s1>SARS-CoV ORF1b-encoded nonstructural proteins 12-16: Replicative enzymes as antiviral targets</s1></fA08><fA11 i1="01" i2="1"><s1>SUBISSI (Lorenzo)</s1></fA11><fA11 i1="02" i2="1"><s1>IMBERT (Isabelle)</s1></fA11><fA11 i1="03" i2="1"><s1>FERRON (François)</s1></fA11><fA11 i1="04" i2="1"><s1>COLLET (Axelle)</s1></fA11><fA11 i1="05" i2="1"><s1>COUTARD (Bruno)</s1></fA11><fA11 i1="06" i2="1"><s1>DECROLY (Etienne)</s1></fA11><fA11 i1="07" i2="1"><s1>CANARD (Bruno)</s1></fA11><fA14 i1="01"><s1>Laboratoire Architecture et Fonction des Macromolecules Biologiques (AFMB), UMR 7257 - CNRS et Aix-Marseille Universite, ESIL Case 925</s1><s2>13288 Marseille</s2><s3>FRA</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ><sZ>6 aut.</sZ><sZ>7 aut.</sZ></fA14><fA20><s1>122-130</s1></fA20><fA21><s1>2014</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>18839</s2><s5>354000500744760160</s5></fA43><fA44><s0>0000</s0><s1>© 2014 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>1 p.3/4</s0></fA45><fA47 i1="01" i2="1"><s0>14-0035787</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Antiviral research</s0></fA64><fA66 i1="01"><s0>GBR</s0></fA66><fC01 i1="01" l="ENG"><s0>The SARS (severe acute respiratory syndrome) pandemic caused ten years ago by the SARS-coronavirus (SARS-CoV) has stimulated a number of studies on the molecular biology of coronaviruses. This research has provided significant new insight into many mechanisms used by the coronavirus replication-transcription complex (RTC). The RTC directs and coordinates processes in order to replicate and transcribe the coronavirus genome, a single-stranded, positive-sense RNA of outstanding length (∼27-32 kilobases). Here, we review the up-to-date knowledge on SARS-CoV replicative enzymes encoded in the ORF1b, i.e., the main RNA-dependent RNA polymerase (nsp12), the helicase/triphosphatase (nsp13), two unusual ribonucleases (nsp14, nsp15) and RNA-cap methyltransferases (nsp14, nsp16). We also review how these enzymes co-operate with other viral co-factors (nsp7, nsp8, and nsp10) to regulate their activity. These last ten years of research on SARS-CoV have considerably contributed to unravel structural and functional details of one of the most fascinating replication/transcription machineries of the RNA virus world. This paper forms part of a series of invited articles in Antiviral Research on "From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses".</s0></fC01><fC02 i1="01" i2="X"><s0>002B02S05</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Virus syndrome respiratoire aigu sévère</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Severe acute respiratory syndrome virus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Severe acute respiratory syndrome virus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Protéine</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Protein</s0><s5>02</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Proteína</s0><s5>02</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Enzyme</s0><s2>FE</s2><s5>03</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Enzyme</s0><s2>FE</s2><s5>03</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Enzima</s0><s2>FE</s2><s5>03</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Antiviral</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Antiviral</s0><s5>04</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Antiviral</s0><s5>04</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Cible</s0><s5>05</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Target</s0><s5>05</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Blanco</s0><s5>05</s5></fC03><fC03 i1="06" i2="X" l="FRE"><s0>Ciblage</s0><s5>06</s5></fC03><fC03 i1="06" i2="X" l="ENG"><s0>Targeting</s0><s5>06</s5></fC03><fC03 i1="06" i2="X" l="SPA"><s0>Blancado</s0><s5>06</s5></fC03><fC03 i1="07" i2="X" l="FRE"><s0>Réplication</s0><s5>08</s5></fC03><fC03 i1="07" i2="X" l="ENG"><s0>Replication</s0><s5>08</s5></fC03><fC03 i1="07" i2="X" l="SPA"><s0>Replicación</s0><s5>08</s5></fC03><fC03 i1="08" i2="X" l="FRE"><s0>Transcription</s0><s5>09</s5></fC03><fC03 i1="08" i2="X" l="ENG"><s0>Transcription</s0><s5>09</s5></fC03><fC03 i1="08" i2="X" l="SPA"><s0>Transcripción</s0><s5>09</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Coronavirus</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Coronavirus</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fN21><s1>041</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard></inist><affiliations><list><country><li>France</li></country><region><li>Provence-Alpes-Côte d'Azur</li></region><settlement><li>Marseille</li></settlement></list><tree><country name="France"><region name="Provence-Alpes-Côte d'Azur"><name sortKey="Subissi, Lorenzo" sort="Subissi, Lorenzo" uniqKey="Subissi L" first="Lorenzo" last="Subissi">Lorenzo Subissi</name></region><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><name sortKey="Collet, Axelle" sort="Collet, Axelle" uniqKey="Collet A" first="Axelle" last="Collet">Axelle Collet</name><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><name sortKey="Decroly, Etienne" sort="Decroly, Etienne" uniqKey="Decroly E" first="Etienne" last="Decroly">Etienne Decroly</name><name sortKey="Ferron, Francois" sort="Ferron, Francois" uniqKey="Ferron F" first="François" last="Ferron">François Ferron</name><name sortKey="Imbert, Isabelle" sort="Imbert, Isabelle" uniqKey="Imbert I" first="Isabelle" last="Imbert">Isabelle Imbert</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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