SrasV1, PubMed, Checkpoint, bibRecord, 002426

The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme.

Identifieur interne : 002426 ( PubMed/Checkpoint ); précédent : 002425; suivant : 002427

The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme.

Auteurs : Holger A. Lindner [Canada] ; Nasser Fotouhi-Ardakani ; Viktoria Lytvyn ; Paule Lachance ; Traian Sulea ; Robert Ménard

Source :

Journal of virology [ 0022-538X ] ; 2005.

RBID : pubmed:16306591

Descripteurs français

KwdFr :
- Cellules HeLa, Domaine catalytique, Données de séquences moléculaires, Humains, Papaïne (), Papaïne (métabolisme), Peptide hydrolases (génétique), Peptide hydrolases (métabolisme), Spécificité du substrat, Syndrome respiratoire aigu sévère (virologie), Séquence d'acides aminés, Ubiquitine (métabolisme), Virus du SRAS (enzymologie), Virus du SRAS (génétique).
MESH :
- enzymologie : Virus du SRAS.
- génétique : Peptide hydrolases, Virus du SRAS.
- métabolisme : Papaïne, Peptide hydrolases, Ubiquitine.
- virologie : Syndrome respiratoire aigu sévère.
- Cellules HeLa, Domaine catalytique, Données de séquences moléculaires, Humains, Papaïne, Spécificité du substrat, Séquence d'acides aminés.

English descriptors

KwdEn :
- Amino Acid Sequence, Catalytic Domain, HeLa Cells, Humans, Molecular Sequence Data, Papain (chemistry), Papain (metabolism), Peptide Hydrolases (genetics), Peptide Hydrolases (metabolism), SARS Virus (enzymology), SARS Virus (genetics), Severe Acute Respiratory Syndrome (virology), Substrate Specificity, Ubiquitin (metabolism).
MESH :
- chemical , chemistry : Papain.
- chemical , genetics : Peptide Hydrolases.
- chemical , metabolism : Papain, Peptide Hydrolases, Ubiquitin.
- enzymology : SARS Virus.
- genetics : SARS Virus.
- virology : Severe Acute Respiratory Syndrome.
- Amino Acid Sequence, Catalytic Domain, HeLa Cells, Humans, Molecular Sequence Data, Substrate Specificity.

Abstract

The severe acute respiratory syndrome coronavirus papain-like protease (SARS-CoV PLpro) is involved in the processing of the viral polyprotein and, thereby, contributes to the biogenesis of the virus replication complex. Structural bioinformatics has revealed a relationship for the SARS-CoV PLpro to herpesvirus-associated ubiquitin-specific protease (HAUSP), a ubiquitin-specific protease, indicating potential deubiquitinating activity in addition to its function in polyprotein processing (T. Sulea, H. A. Lindner, E. O. Purisima, and R. Menard, J. Virol. 79:4550-4551, 2005). In order to confirm this prediction, we overexpressed and purified SARS-CoV PLpro (amino acids [aa]1507 to 1858) from Escherichia coli. The purified enzyme hydrolyzed ubiquitin-7-amino-4-methylcoumarin (Ub-AMC), a general deubiquitinating enzyme substrate, with a catalytic efficiency of 13,100 M(-1)s(-1), 220-fold more efficiently than the small synthetic peptide substrate Z-LRGG-AMC, which incorporates the C-terminal four residues of ubiquitin. In addition, SARS-CoV PLpro was inhibited by the specific deubiquitinating enzyme inhibitor ubiquitin aldehyde, with an inhibition constant of 210 nM. The purified SARS-CoV PLpro disassembles branched polyubiquitin chains with lengths of two to seven (Ub2-7) or four (Ub4) units, which involves isopeptide bond cleavage. SARS-CoV PLpro processing activity was also detected against a protein fused to the C terminus of the ubiquitin-like modifier ISG15, both in vitro using the purified enzyme and in HeLa cells by coexpression with SARS-CoV PLpro (aa 1198 to 2009). These results clearly establish that SARS-CoV PLpro is a deubiquitinating enzyme, thereby confirming our earlier prediction. This unexpected activity for a coronavirus papain-like protease suggests a novel viral strategy to modulate the host cell ubiquitination machinery to its advantage.

DOI: 10.1128/JVI.79.24.15199-15208.2005
PubMed: 16306591

Affiliations:

Canada

Links toward previous steps (curation, corpus...)

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pubmed:16306591

Le document en format XML

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<front><div type="abstract" xml:lang="en">The severe acute respiratory syndrome coronavirus papain-like protease (SARS-CoV PLpro) is involved in the processing of the viral polyprotein and, thereby, contributes to the biogenesis of the virus replication complex. Structural bioinformatics has revealed a relationship for the SARS-CoV PLpro to herpesvirus-associated ubiquitin-specific protease (HAUSP), a ubiquitin-specific protease, indicating potential deubiquitinating activity in addition to its function in polyprotein processing (T. Sulea, H. A. Lindner, E. O. Purisima, and R. Menard, J. Virol. 79:4550-4551, 2005). In order to confirm this prediction, we overexpressed and purified SARS-CoV PLpro (amino acids [aa]1507 to 1858) from Escherichia coli. The purified enzyme hydrolyzed ubiquitin-7-amino-4-methylcoumarin (Ub-AMC), a general deubiquitinating enzyme substrate, with a catalytic efficiency of 13,100 M(-1)s(-1), 220-fold more efficiently than the small synthetic peptide substrate Z-LRGG-AMC, which incorporates the C-terminal four residues of ubiquitin. In addition, SARS-CoV PLpro was inhibited by the specific deubiquitinating enzyme inhibitor ubiquitin aldehyde, with an inhibition constant of 210 nM. The purified SARS-CoV PLpro disassembles branched polyubiquitin chains with lengths of two to seven (Ub2-7) or four (Ub4) units, which involves isopeptide bond cleavage. SARS-CoV PLpro processing activity was also detected against a protein fused to the C terminus of the ubiquitin-like modifier ISG15, both in vitro using the purified enzyme and in HeLa cells by coexpression with SARS-CoV PLpro (aa 1198 to 2009). These results clearly establish that SARS-CoV PLpro is a deubiquitinating enzyme, thereby confirming our earlier prediction. This unexpected activity for a coronavirus papain-like protease suggests a novel viral strategy to modulate the host cell ubiquitination machinery to its advantage.</div>
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<Abstract><AbstractText>The severe acute respiratory syndrome coronavirus papain-like protease (SARS-CoV PLpro) is involved in the processing of the viral polyprotein and, thereby, contributes to the biogenesis of the virus replication complex. Structural bioinformatics has revealed a relationship for the SARS-CoV PLpro to herpesvirus-associated ubiquitin-specific protease (HAUSP), a ubiquitin-specific protease, indicating potential deubiquitinating activity in addition to its function in polyprotein processing (T. Sulea, H. A. Lindner, E. O. Purisima, and R. Menard, J. Virol. 79:4550-4551, 2005). In order to confirm this prediction, we overexpressed and purified SARS-CoV PLpro (amino acids [aa]1507 to 1858) from Escherichia coli. The purified enzyme hydrolyzed ubiquitin-7-amino-4-methylcoumarin (Ub-AMC), a general deubiquitinating enzyme substrate, with a catalytic efficiency of 13,100 M(-1)s(-1), 220-fold more efficiently than the small synthetic peptide substrate Z-LRGG-AMC, which incorporates the C-terminal four residues of ubiquitin. In addition, SARS-CoV PLpro was inhibited by the specific deubiquitinating enzyme inhibitor ubiquitin aldehyde, with an inhibition constant of 210 nM. The purified SARS-CoV PLpro disassembles branched polyubiquitin chains with lengths of two to seven (Ub2-7) or four (Ub4) units, which involves isopeptide bond cleavage. SARS-CoV PLpro processing activity was also detected against a protein fused to the C terminus of the ubiquitin-like modifier ISG15, both in vitro using the purified enzyme and in HeLa cells by coexpression with SARS-CoV PLpro (aa 1198 to 2009). These results clearly establish that SARS-CoV PLpro is a deubiquitinating enzyme, thereby confirming our earlier prediction. This unexpected activity for a coronavirus papain-like protease suggests a novel viral strategy to modulate the host cell ubiquitination machinery to its advantage.</AbstractText>
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The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme.

The papain-like protease from the severe acute respiratory syndrome coronavirus is a deubiquitinating enzyme.

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