Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase
Identifieur interne : 000811 ( PascalFrancis/Checkpoint ); précédent : 000810; suivant : 000812Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase
Auteurs : Konstantin A. Ivanov [Allemagne] ; Volker Thiel [Allemagne] ; Jessika C. Dobbe [Pays-Bas] ; Yvonne Van Der Meer [Pays-Bas] ; Eric J. Snijder [Pays-Bas] ; John Ziebuhr [Allemagne]Source :
- Journal of virology [ 0022-538X ] ; 2004.
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Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV), a newly identified group 2 coronavirus, is the causative agent of severe acute respiratory syndrome, a life-threatening form of pneumonia in humans. Coronavirus replication and transcription are highly specialized processes of cytoplasmic RNA synthesis that localize to virus-induced membrane structures and were recently proposed to involve a complex enzymatic machinery that, besides RNA-dependent RNA polymerase, helicase, and protease activities, also involves a series of RNA-processing enzymes that are not found in most other RNA virus families. Here, we characterized the enzymatic activities of a recombinant form of the SARS-CoV helicase (nonstructural protein [nsp] 13), a superfamily 1 helicase with an N-terminal zinc-binding domain. We report that nspl3 has both RNA and DNA duplex-unwinding activities. SARS-CoV nspl3 unwinds its substrates in a 5'-to-3' direction and features a remarkable processivity, allowing efficient strand separation of extended regions of double-stranded RNA and DNA. Characterization of the nspl3-associated (deoxy)nucleoside triphosphatase ([dNTPase) activities revealed that all natural nucleotides and deoxynucleotides are substrates of nspl3, with ATP, dATP, and GTP being hydrolyzed slightly more efficiently than other nucleotides. Furthermore, we established an RNA 5'-triphosphatase activity for the SARS-CoV nspl3 helicase which may be involved in the formation of the 5' cap structure of viral RNAs. The data suggest that the (d)NTPase and RNA 5'-triphosphatase activities of nspl3 have a common active site. Finally, we established that, in SARS-CoV-infected Vero E6 cells, nsp13 localizes to membranes that appear to be derived from the endoplasmic reticulum and are the likely site of SARS-CoV RNA synthesis.
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Ivanov</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Institute of urology and Immunology, University of Würzburg</s1><s2>Würzburg</s2><s3>DEU</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Basse-Franconie</region><settlement type="city">Wurtzbourg</settlement></placeName></affiliation></author><author><name sortKey="Thiel, Volker" sort="Thiel, Volker" uniqKey="Thiel V" first="Volker" last="Thiel">Volker Thiel</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Institute of urology and Immunology, University of Würzburg</s1><s2>Würzburg</s2><s3>DEU</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Basse-Franconie</region><settlement type="city">Wurtzbourg</settlement></placeName></affiliation></author><author><name sortKey="Dobbe, Jessika C" sort="Dobbe, Jessika C" uniqKey="Dobbe J" first="Jessika C." last="Dobbe">Jessika C. 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Ivanov</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Institute of urology and Immunology, University of Würzburg</s1><s2>Würzburg</s2><s3>DEU</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Basse-Franconie</region><settlement type="city">Wurtzbourg</settlement></placeName></affiliation></author><author><name sortKey="Thiel, Volker" sort="Thiel, Volker" uniqKey="Thiel V" first="Volker" last="Thiel">Volker Thiel</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Institute of urology and Immunology, University of Würzburg</s1><s2>Würzburg</s2><s3>DEU</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Basse-Franconie</region><settlement type="city">Wurtzbourg</settlement></placeName></affiliation></author><author><name sortKey="Dobbe, Jessika C" sort="Dobbe, Jessika C" uniqKey="Dobbe J" first="Jessika C." last="Dobbe">Jessika C. Dobbe</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Molecular urology Laboratory, Department of Medical Microbiology, Leiden University Medical Center</s1><s2>Leiden</s2><s3>NLD</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation></author><author><name sortKey="Van Der Meer, Yvonne" sort="Van Der Meer, Yvonne" uniqKey="Van Der Meer Y" first="Yvonne" last="Van Der Meer">Yvonne Van Der Meer</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Molecular urology Laboratory, Department of Medical Microbiology, Leiden University Medical Center</s1><s2>Leiden</s2><s3>NLD</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation></author><author><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J." last="Snijder">Eric J. Snijder</name><affiliation wicri:level="3"><inist:fA14 i1="02"><s1>Molecular urology Laboratory, Department of Medical Microbiology, Leiden University Medical Center</s1><s2>Leiden</s2><s3>NLD</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></inist:fA14><country>Pays-Bas</country><placeName><settlement type="city">Leyde</settlement><region nuts="2" type="province">Hollande-Méridionale</region></placeName></affiliation></author><author><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name><affiliation wicri:level="3"><inist:fA14 i1="01"><s1>Institute of urology and Immunology, University of Würzburg</s1><s2>Würzburg</s2><s3>DEU</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></inist:fA14><country>Allemagne</country><placeName><region type="land" nuts="1">Bavière</region><region type="district" nuts="2">District de Basse-Franconie</region><settlement type="city">Wurtzbourg</settlement></placeName></affiliation></author></analytic><series><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno><imprint><date when="2004">2004</date></imprint></series></biblStruct></sourceDesc><seriesStmt><title level="j" type="main">Journal of virology</title><title level="j" type="abbreviated">J. virol.</title><idno type="ISSN">0022-538X</idno></seriesStmt></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Coronavirus</term><term>Enzymatic activity</term><term>Microbiology</term><term>Multiple</term><term>Severe acute respiratory syndrome</term><term>Virology</term></keywords><keywords scheme="Pascal" xml:lang="fr"><term>Coronavirus</term><term>Multiple</term><term>Activité enzymatique</term><term>Microbiologie</term><term>Virologie</term><term>Syndrome respiratoire aigu sévère</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Severe acute respiratory syndrome coronavirus (SARS-CoV), a newly identified group 2 coronavirus, is the causative agent of severe acute respiratory syndrome, a life-threatening form of pneumonia in humans. Coronavirus replication and transcription are highly specialized processes of cytoplasmic RNA synthesis that localize to virus-induced membrane structures and were recently proposed to involve a complex enzymatic machinery that, besides RNA-dependent RNA polymerase, helicase, and protease activities, also involves a series of RNA-processing enzymes that are not found in most other RNA virus families. Here, we characterized the enzymatic activities of a recombinant form of the SARS-CoV helicase (nonstructural protein [nsp] 13), a superfamily 1 helicase with an N-terminal zinc-binding domain. We report that nspl3 has both RNA and DNA duplex-unwinding activities. SARS-CoV nspl3 unwinds its substrates in a 5'-to-3' direction and features a remarkable processivity, allowing efficient strand separation of extended regions of double-stranded RNA and DNA. Characterization of the nspl3-associated (deoxy)nucleoside triphosphatase ([dNTPase) activities revealed that all natural nucleotides and deoxynucleotides are substrates of nspl3, with ATP, dATP, and GTP being hydrolyzed slightly more efficiently than other nucleotides. Furthermore, we established an RNA 5'-triphosphatase activity for the SARS-CoV nspl3 helicase which may be involved in the formation of the 5' cap structure of viral RNAs. The data suggest that the (d)NTPase and RNA 5'-triphosphatase activities of nspl3 have a common active site. Finally, we established that, in SARS-CoV-infected Vero E6 cells, nsp13 localizes to membranes that appear to be derived from the endoplasmic reticulum and are the likely site of SARS-CoV RNA synthesis.</div></front></TEI><inist><standard h6="B"><pA><fA01 i1="01" i2="1"><s0>0022-538X</s0></fA01><fA03 i2="1"><s0>J. virol.</s0></fA03><fA05><s2>78</s2></fA05><fA06><s2>11</s2></fA06><fA08 i1="01" i2="1" l="ENG"><s1>Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase</s1></fA08><fA11 i1="01" i2="1"><s1>IVANOV (Konstantin A.)</s1></fA11><fA11 i1="02" i2="1"><s1>THIEL (Volker)</s1></fA11><fA11 i1="03" i2="1"><s1>DOBBE (Jessika C.)</s1></fA11><fA11 i1="04" i2="1"><s1>VAN DER MEER (Yvonne)</s1></fA11><fA11 i1="05" i2="1"><s1>SNIJDER (Eric J.)</s1></fA11><fA11 i1="06" i2="1"><s1>ZIEBUHR (John)</s1></fA11><fA14 i1="01"><s1>Institute of urology and Immunology, University of Würzburg</s1><s2>Würzburg</s2><s3>DEU</s3><sZ>1 aut.</sZ><sZ>2 aut.</sZ><sZ>6 aut.</sZ></fA14><fA14 i1="02"><s1>Molecular urology Laboratory, Department of Medical Microbiology, Leiden University Medical Center</s1><s2>Leiden</s2><s3>NLD</s3><sZ>3 aut.</sZ><sZ>4 aut.</sZ><sZ>5 aut.</sZ></fA14><fA20><s1>5619-5632</s1></fA20><fA21><s1>2004</s1></fA21><fA23 i1="01"><s0>ENG</s0></fA23><fA43 i1="01"><s1>INIST</s1><s2>13592</s2><s5>354000111993960100</s5></fA43><fA44><s0>0000</s0><s1>© 2004 INIST-CNRS. All rights reserved.</s1></fA44><fA45><s0>92 ref.</s0></fA45><fA47 i1="01" i2="1"><s0>04-0314704</s0></fA47><fA60><s1>P</s1></fA60><fA61><s0>A</s0></fA61><fA64 i1="01" i2="1"><s0>Journal of virology</s0></fA64><fA66 i1="01"><s0>USA</s0></fA66><fC01 i1="01" l="ENG"><s0>Severe acute respiratory syndrome coronavirus (SARS-CoV), a newly identified group 2 coronavirus, is the causative agent of severe acute respiratory syndrome, a life-threatening form of pneumonia in humans. Coronavirus replication and transcription are highly specialized processes of cytoplasmic RNA synthesis that localize to virus-induced membrane structures and were recently proposed to involve a complex enzymatic machinery that, besides RNA-dependent RNA polymerase, helicase, and protease activities, also involves a series of RNA-processing enzymes that are not found in most other RNA virus families. Here, we characterized the enzymatic activities of a recombinant form of the SARS-CoV helicase (nonstructural protein [nsp] 13), a superfamily 1 helicase with an N-terminal zinc-binding domain. We report that nspl3 has both RNA and DNA duplex-unwinding activities. SARS-CoV nspl3 unwinds its substrates in a 5'-to-3' direction and features a remarkable processivity, allowing efficient strand separation of extended regions of double-stranded RNA and DNA. Characterization of the nspl3-associated (deoxy)nucleoside triphosphatase ([dNTPase) activities revealed that all natural nucleotides and deoxynucleotides are substrates of nspl3, with ATP, dATP, and GTP being hydrolyzed slightly more efficiently than other nucleotides. Furthermore, we established an RNA 5'-triphosphatase activity for the SARS-CoV nspl3 helicase which may be involved in the formation of the 5' cap structure of viral RNAs. The data suggest that the (d)NTPase and RNA 5'-triphosphatase activities of nspl3 have a common active site. Finally, we established that, in SARS-CoV-infected Vero E6 cells, nsp13 localizes to membranes that appear to be derived from the endoplasmic reticulum and are the likely site of SARS-CoV RNA synthesis.</s0></fC01><fC02 i1="01" i2="X"><s0>002A05C10</s0></fC02><fC03 i1="01" i2="X" l="FRE"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="ENG"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="01" i2="X" l="SPA"><s0>Coronavirus</s0><s2>NW</s2><s5>01</s5></fC03><fC03 i1="02" i2="X" l="FRE"><s0>Multiple</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="ENG"><s0>Multiple</s0><s5>05</s5></fC03><fC03 i1="02" i2="X" l="SPA"><s0>Múltiple</s0><s5>05</s5></fC03><fC03 i1="03" i2="X" l="FRE"><s0>Activité enzymatique</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="ENG"><s0>Enzymatic activity</s0><s5>06</s5></fC03><fC03 i1="03" i2="X" l="SPA"><s0>Actividad enzimática</s0><s5>06</s5></fC03><fC03 i1="04" i2="X" l="FRE"><s0>Microbiologie</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="ENG"><s0>Microbiology</s0><s5>07</s5></fC03><fC03 i1="04" i2="X" l="SPA"><s0>Microbiología</s0><s5>07</s5></fC03><fC03 i1="05" i2="X" l="FRE"><s0>Virologie</s0><s5>08</s5></fC03><fC03 i1="05" i2="X" l="ENG"><s0>Virology</s0><s5>08</s5></fC03><fC03 i1="05" i2="X" l="SPA"><s0>Virología</s0><s5>08</s5></fC03><fC03 i1="06" i2="X" l="FRE"><s0>Syndrome respiratoire aigu sévère</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="06" i2="X" l="ENG"><s0>Severe acute respiratory syndrome</s0><s2>NM</s2><s5>14</s5></fC03><fC03 i1="06" i2="X" l="SPA"><s0>Síndrome respiratorio agudo severo</s0><s2>NM</s2><s5>14</s5></fC03><fC07 i1="01" i2="X" l="FRE"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="ENG"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="01" i2="X" l="SPA"><s0>Coronaviridae</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="FRE"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="ENG"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="02" i2="X" l="SPA"><s0>Nidovirales</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="FRE"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="ENG"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="03" i2="X" l="SPA"><s0>Virus</s0><s2>NW</s2></fC07><fC07 i1="04" i2="X" l="FRE"><s0>Virose</s0><s2>NM</s2></fC07><fC07 i1="04" i2="X" l="ENG"><s0>Viral disease</s0><s2>NM</s2></fC07><fC07 i1="04" i2="X" l="SPA"><s0>Virosis</s0><s2>NM</s2></fC07><fC07 i1="05" i2="X" l="FRE"><s0>Infection</s0><s2>NM</s2></fC07><fC07 i1="05" i2="X" l="ENG"><s0>Infection</s0><s2>NM</s2></fC07><fC07 i1="05" i2="X" l="SPA"><s0>Infección</s0><s2>NM</s2></fC07><fC07 i1="06" i2="X" l="FRE"><s0>Appareil respiratoire pathologie</s0><s5>19</s5></fC07><fC07 i1="06" i2="X" l="ENG"><s0>Respiratory disease</s0><s5>19</s5></fC07><fC07 i1="06" i2="X" l="SPA"><s0>Aparato respiratorio patología</s0><s5>19</s5></fC07><fC07 i1="07" i2="X" l="FRE"><s0>Poumon pathologie</s0><s5>20</s5></fC07><fC07 i1="07" i2="X" l="ENG"><s0>Lung disease</s0><s5>20</s5></fC07><fC07 i1="07" i2="X" l="SPA"><s0>Pulmón patología</s0><s5>20</s5></fC07><fN21><s1>187</s1></fN21><fN44 i1="01"><s1>OTO</s1></fN44><fN82><s1>OTO</s1></fN82></pA></standard></inist><affiliations><list><country><li>Allemagne</li><li>Pays-Bas</li></country><region><li>Bavière</li><li>District de Basse-Franconie</li><li>Hollande-Méridionale</li></region><settlement><li>Leyde</li><li>Wurtzbourg</li></settlement></list><tree><country name="Allemagne"><region name="Bavière"><name sortKey="Ivanov, Konstantin A" sort="Ivanov, Konstantin A" uniqKey="Ivanov K" first="Konstantin A." last="Ivanov">Konstantin A. Ivanov</name></region><name sortKey="Thiel, Volker" sort="Thiel, Volker" uniqKey="Thiel V" first="Volker" last="Thiel">Volker Thiel</name><name sortKey="Ziebuhr, John" sort="Ziebuhr, John" uniqKey="Ziebuhr J" first="John" last="Ziebuhr">John Ziebuhr</name></country><country name="Pays-Bas"><region name="Hollande-Méridionale"><name sortKey="Dobbe, Jessika C" sort="Dobbe, Jessika C" uniqKey="Dobbe J" first="Jessika C." last="Dobbe">Jessika C. Dobbe</name></region><name sortKey="Snijder, Eric J" sort="Snijder, Eric J" uniqKey="Snijder E" first="Eric J." last="Snijder">Eric J. Snijder</name><name sortKey="Van Der Meer, Yvonne" sort="Van Der Meer, Yvonne" uniqKey="Van Der Meer Y" first="Yvonne" last="Van Der Meer">Yvonne Van Der Meer</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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