SrasV1, PascalFrancis, Corpus, bibRecord, 000759

The severe acute respiratory syndrome coronavirus Nspl5 protein is an endoribonuclease that prefers manganese as a cofactor

Identifieur interne : 000759 ( PascalFrancis/Corpus ); précédent : 000758; suivant : 000760

The severe acute respiratory syndrome coronavirus Nspl5 protein is an endoribonuclease that prefers manganese as a cofactor

Auteurs : Kanchan Bhardwaj ; Linda Guarino ; C. Cheng Kao

Source :

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

RBID : Pascal:05-0000622

Descripteurs français

Pascal (Inist)
- Coronavirus, Grave, Malade état grave, Aigu, Voie respiratoire, Protéine, Microbiologie, Virologie, Syndrome respiratoire aigu sévère, Forme grave.

English descriptors

KwdEn :
- Acute, Coronavirus, Critically ill, Microbiology, Protein, Respiratory tract, Severe, Severe acute respiratory syndrome, Virology.

Abstract

Nonstructural protein 15 (Nspl5) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nspl5 but with different kinetics for cleavage. Mn²⁺ at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg²⁺ and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn²⁺ needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nspl5 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.

Notice en format standard (ISO 2709)

Pour connaître la documentation sur le format Inist Standard.

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C01	`01`		`ENG`	@0 Nonstructural protein 15 (Nspl5) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nspl5 but with different kinetics for cleavage. Mn²⁺ at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg²⁺ and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn²⁺ needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nspl5 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.
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N44	`01`			`@1 OTO`
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Format Inist (serveur)

NO :	PASCAL 05-0000622 INIST
ET :	The severe acute respiratory syndrome coronavirus Nspl5 protein is an endoribonuclease that prefers manganese as a cofactor
AU :	BHARDWAJ (Kanchan); GUARINO (Linda); CHENG KAO (C.)
AF :	Department of Biochemistry and Biophysics, Texas A&M University/College Station, Texas/Etats-Unis (1 aut., 2 aut., 3 aut.)
DT :	Publication en série; Niveau analytique
SO :	Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2004; Vol. 78; No. 22; Pp. 12218-12224; Bibl. 33 ref.
LA :	Anglais
EA :	Nonstructural protein 15 (Nspl5) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nspl5 but with different kinetics for cleavage. Mn²⁺ at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg²⁺ and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn²⁺ needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nspl5 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.
CC :	002A05C10
FD :	Coronavirus; Grave; Malade état grave; Aigu; Voie respiratoire; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère; Forme grave
FG :	Coronaviridae; Nidovirales; Virus; Virose; Infection; Appareil respiratoire pathologie; Poumon pathologie; Appareil respiratoire
ED :	Coronavirus; Severe; Critically ill; Acute; Respiratory tract; Protein; Microbiology; Virology; Severe acute respiratory syndrome
EG :	Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Respiratory disease; Lung disease; Respiratory system
SD :	Coronavirus; Grave; Enfermo estado grave; Agudo; Vía respiratoria; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo
LO :	INIST-13592.354000122578960130
ID :	05-0000622

Links to Exploration step

Pascal:05-0000622

Le document en format XML

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<front><div type="abstract" xml:lang="en">Nonstructural protein 15 (Nspl5) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nspl5 but with different kinetics for cleavage. Mn<sup>2+</sup>
 at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg<sup>2+</sup>
 and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn<sup>2+</sup>
 needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nspl5 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</div>
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 at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg<sup>2+</sup>
 and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn<sup>2+</sup>
 needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nspl5 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</s0>
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<server><NO>PASCAL 05-0000622 INIST</NO>
<ET>The severe acute respiratory syndrome coronavirus Nspl5 protein is an endoribonuclease that prefers manganese as a cofactor</ET>
<AU>BHARDWAJ (Kanchan); GUARINO (Linda); CHENG KAO (C.)</AU>
<AF>Department of Biochemistry and Biophysics, Texas A&M University/College Station, Texas/Etats-Unis (1 aut., 2 aut., 3 aut.)</AF>
<DT>Publication en série; Niveau analytique</DT>
<SO>Journal of virology; ISSN 0022-538X; Etats-Unis; Da. 2004; Vol. 78; No. 22; Pp. 12218-12224; Bibl. 33 ref.</SO>
<LA>Anglais</LA>
<EA>Nonstructural protein 15 (Nspl5) of the severe acute respiratory syndrome coronavirus (SARS-CoV) produced in Escherichia coli has endoribonuclease activity that preferentially cleaved 5' of uridylates of RNAs. Blocking either the 5' or 3' terminus did not affect cleavage. Double- and single-stranded RNAs were both substrates for Nspl5 but with different kinetics for cleavage. Mn<sup>2+</sup>
 at 2 to 10 mM was needed for optimal endoribonuclease activity, but Mg<sup>2+</sup>
 and several other divalent metals were capable of supporting only a low level of activity. Concentrations of Mn<sup>2+</sup>
 needed for endoribonuclease activity induced significant conformation change(s) in the protein, as measured by changes in tryptophan fluorescence. A similar endoribonucleolytic activity was detected for the orthologous protein from another coronavirus, demonstrating that the endoribonuclease activity of Nspl5 may be common to coronaviruses. This work presents an initial biochemical characterization of a novel coronavirus endoribonuclease.</EA>
<CC>002A05C10</CC>
<FD>Coronavirus; Grave; Malade état grave; Aigu; Voie respiratoire; Protéine; Microbiologie; Virologie; Syndrome respiratoire aigu sévère; Forme grave</FD>
<FG>Coronaviridae; Nidovirales; Virus; Virose; Infection; Appareil respiratoire pathologie; Poumon pathologie; Appareil respiratoire</FG>
<ED>Coronavirus; Severe; Critically ill; Acute; Respiratory tract; Protein; Microbiology; Virology; Severe acute respiratory syndrome</ED>
<EG>Coronaviridae; Nidovirales; Virus; Viral disease; Infection; Respiratory disease; Lung disease; Respiratory system</EG>
<SD>Coronavirus; Grave; Enfermo estado grave; Agudo; Vía respiratoria; Proteína; Microbiología; Virología; Síndrome respiratorio agudo severo</SD>
<LO>INIST-13592.354000122578960130</LO>
<ID>05-0000622</ID>
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The severe acute respiratory syndrome coronavirus Nspl5 protein is an endoribonuclease that prefers manganese as a cofactor

The severe acute respiratory syndrome coronavirus Nspl5 protein is an endoribonuclease that prefers manganese as a cofactor

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