SrasV1, PascalFrancis, Corpus, bibRecord, 000878

Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase

Identifieur interne : 000878 ( PascalFrancis/Corpus ); précédent : 000877; suivant : 000879

Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase

Auteurs : Konstantin A. Ivanov ; Volker Thiel ; Jessika C. Dobbe ; Yvonne Van Der Meer ; Eric J. Snijder ; John Ziebuhr

Source :

Journal of virology [ 0022-538X ] ; 2004.

RBID : Pascal:04-0314704

Descripteurs français

Pascal (Inist)
- Coronavirus, Multiple, Activité enzymatique, Microbiologie, Virologie, Syndrome respiratoire aigu sévère.

English descriptors

KwdEn :
- Coronavirus, Enzymatic activity, Microbiology, Multiple, Severe acute respiratory syndrome, Virology.

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.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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A08	`01`	`1`	`ENG`	`@1 Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase`
A11	`01`	`1`		`@1 IVANOV (Konstantin A.)`
A11	`02`	`1`		`@1 THIEL (Volker)`
A11	`03`	`1`		`@1 DOBBE (Jessika C.)`
A11	`04`	`1`		`@1 VAN DER MEER (Yvonne)`
A11	`05`	`1`		`@1 SNIJDER (Eric J.)`
A11	`06`	`1`		`@1 ZIEBUHR (John)`
A14	`01`			`@1 Institute of urology and Immunology, University of Würzburg @2 Würzburg @3 DEU @Z 1 aut. @Z 2 aut. @Z 6 aut.`
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A44				`@0 0000 @1 © 2004 INIST-CNRS. All rights reserved.`
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C01	`01`		`ENG`	@0 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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C03	`03`	`X`	`FRE`	`@0 Activité enzymatique @5 06`
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C03	`04`	`X`	`ENG`	`@0 Microbiology @5 07`
C03	`04`	`X`	`SPA`	`@0 Microbiología @5 07`
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C03	`06`	`X`	`FRE`	`@0 Syndrome respiratoire aigu sévère @2 NM @5 14`
C03	`06`	`X`	`ENG`	`@0 Severe acute respiratory syndrome @2 NM @5 14`
C03	`06`	`X`	`SPA`	`@0 Síndrome respiratorio agudo severo @2 NM @5 14`
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C07	`01`	`X`	`ENG`	`@0 Coronaviridae @2 NW`
C07	`01`	`X`	`SPA`	`@0 Coronaviridae @2 NW`
C07	`02`	`X`	`FRE`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`ENG`	`@0 Nidovirales @2 NW`
C07	`02`	`X`	`SPA`	`@0 Nidovirales @2 NW`
C07	`03`	`X`	`FRE`	`@0 Virus @2 NW`
C07	`03`	`X`	`ENG`	`@0 Virus @2 NW`
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C07	`04`	`X`	`ENG`	`@0 Viral disease @2 NM`
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N21				`@1 187`
N44	`01`			`@1 OTO`
N82				`@1 OTO`

Format Inist (serveur)

NO :	PASCAL 04-0314704 INIST
ET :	Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase
AU :	IVANOV (Konstantin A.); THIEL (Volker); DOBBE (Jessika C.); VAN DER MEER (Yvonne); SNIJDER (Eric J.); ZIEBUHR (John)
AF :	Institute of urology and Immunology, University of Würzburg/Würzburg/Allemagne (1 aut., 2 aut., 6 aut.); Molecular urology Laboratory, Department of Medical Microbiology, Leiden University Medical Center/Leiden/Pays-Bas (3 aut., 4 aut., 5 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2004; Vol. 78; No. 11; Pp. 5619-5632; Bibl. 92 ref.
LA :	Anglais
EA :	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.
CC :	002A05C10
FD :	Coronavirus; Multiple; Activité enzymatique; Microbiologie; Virologie; Syndrome respiratoire aigu sévère
FG :	Coronaviridae; Nidovirales; Virus; Virose; Infection; Appareil respiratoire pathologie; Poumon pathologie
ED :	Coronavirus; Multiple; Enzymatic activity; Microbiology; Virology; Severe acute respiratory syndrome
EG :	Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Respiratory disease; Lung disease
SD :	Coronavirus; Múltiple; Actividad enzimática; Microbiología; Virología; Síndrome respiratorio agudo severo
LO :	INIST-13592.354000111993960100
ID :	04-0314704

Links to Exploration step

Pascal:04-0314704

Le document en format XML

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<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>
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<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>
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<s2>NW</s2>
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<s2>NW</s2>
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<s2>NM</s2>
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<s2>NM</s2>
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<s2>NM</s2>
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<s5>19</s5>
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<server><NO>PASCAL 04-0314704 INIST</NO>
<ET>Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase</ET>
<AU>IVANOV (Konstantin A.); THIEL (Volker); DOBBE (Jessika C.); VAN DER MEER (Yvonne); SNIJDER (Eric J.); ZIEBUHR (John)</AU>
<AF>Institute of urology and Immunology, University of Würzburg/Würzburg/Allemagne (1 aut., 2 aut., 6 aut.); Molecular urology Laboratory, Department of Medical Microbiology, Leiden University Medical Center/Leiden/Pays-Bas (3 aut., 4 aut., 5 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2004; Vol. 78; No. 11; Pp. 5619-5632; Bibl. 92 ref.</SO>
<LA>Anglais</LA>
<EA>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.</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Multiple; Activité enzymatique; Microbiologie; Virologie; Syndrome respiratoire aigu sévère</FD>
<FG>Coronaviridae; Nidovirales; Virus; Virose; Infection; Appareil respiratoire pathologie; Poumon pathologie</FG>
<ED>Coronavirus; Multiple; Enzymatic activity; Microbiology; Virology; Severe acute respiratory syndrome</ED>
<EG>Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Respiratory disease; Lung disease</EG>
<SD>Coronavirus; Múltiple; Actividad enzimática; Microbiología; Virología; Síndrome respiratorio agudo severo</SD>
<LO>INIST-13592.354000111993960100</LO>
<ID>04-0314704</ID>
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Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase

Multiple enzymatic activities associated with severe acute respiratory syndrome coronavirus helicase

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