MersV1, PubMed, Checkpoint, bibRecord, 001842

MERS-CoV papain-like protease has deISGylating and deubiquitinating activities.

Identifieur interne : 001842 ( PubMed/Checkpoint ); précédent : 001841; suivant : 001843

MERS-CoV papain-like protease has deISGylating and deubiquitinating activities.

Auteurs : Anna M. Mielech [États-Unis] ; Andy Kilianski [États-Unis] ; Yahira M. Baez-Santos [États-Unis] ; Andrew D. Mesecar [États-Unis] ; Susan C. Baker [États-Unis]

Source :

Virology [ 1096-0341 ] ; 2014.

RBID : pubmed:24503068

Descripteurs français

KwdFr :
- Coronaviridae (), Coronaviridae (enzymologie), Coronaviridae (génétique), Cytokines (génétique), Cytokines (métabolisme), Données de séquences moléculaires, Glycosylation, Humains, Infections à Coronaviridae (génétique), Infections à Coronaviridae (métabolisme), Infections à Coronaviridae (virologie), Lignée cellulaire, Papaïne (), Papaïne (génétique), Papaïne (métabolisme), Protéines virales (), Protéines virales (génétique), Protéines virales (métabolisme), Structure tertiaire des protéines, Séquence d'acides aminés, Ubiquitines (génétique), Ubiquitines (métabolisme), Ubiquitinylation, Virus du SRAS (enzymologie), Virus du SRAS (génétique).
MESH :
- enzymologie : Coronaviridae, Virus du SRAS.
- génétique : Coronaviridae, Cytokines, Infections à Coronaviridae, Papaïne, Protéines virales, Ubiquitines, Virus du SRAS.
- métabolisme : Cytokines, Infections à Coronaviridae, Papaïne, Protéines virales, Ubiquitines.
- virologie : Infections à Coronaviridae.
- Coronaviridae, Données de séquences moléculaires, Glycosylation, Humains, Lignée cellulaire, Papaïne, Protéines virales, Structure tertiaire des protéines, Séquence d'acides aminés, Ubiquitinylation.

English descriptors

KwdEn :
- Amino Acid Sequence, Cell Line, Coronaviridae (chemistry), Coronaviridae (enzymology), Coronaviridae (genetics), Coronaviridae Infections (genetics), Coronaviridae Infections (metabolism), Coronaviridae Infections (virology), Cytokines (genetics), Cytokines (metabolism), Glycosylation, Humans, Molecular Sequence Data, Papain (chemistry), Papain (genetics), Papain (metabolism), Protein Structure, Tertiary, SARS Virus (enzymology), SARS Virus (genetics), Ubiquitination, Ubiquitins (genetics), Ubiquitins (metabolism), Viral Proteins (chemistry), Viral Proteins (genetics), Viral Proteins (metabolism).
MESH :
- chemical , chemistry : Papain, Viral Proteins.
- chemical , genetics : Cytokines, Papain, Ubiquitins, Viral Proteins.
- chemistry : Coronaviridae.
- enzymology : Coronaviridae, SARS Virus.
- genetics : Coronaviridae, Coronaviridae Infections, SARS Virus.
- metabolism : Coronaviridae Infections, Cytokines, Papain, Ubiquitins, Viral Proteins.
- virology : Coronaviridae Infections.
- Amino Acid Sequence, Cell Line, Glycosylation, Humans, Molecular Sequence Data, Protein Structure, Tertiary, Ubiquitination.

Abstract

Coronaviruses encode papain-like proteases (PLpro) that are often multifunctional enzymes with protease activity to process the viral replicase polyprotein and deubiquitinating (DUB)/deISGylating activity, which is hypothesized to modify the innate immune response to infection. Here, we investigate the predicted DUB activity of the PLpro domain of the recently described Middle East Respiratory Syndrome Coronavirus (MERS-CoV). We found that expression of MERS-CoV PLpro reduces the levels of ubiquitinated and ISGylated host cell proteins; consistent with multifunctional PLpro activity. Further, we compared the ability of MERS-CoV PLpro and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) PLpro to block innate immune signaling of proinflammatory cytokines. We show that expression of SARS-CoV and MERS-CoV PLpros blocks upregulation of cytokines CCL5, IFN-β and CXCL10 in stimulated cells. Overall these results indicate that the PLpro domains of MERS-CoV and SARS-CoV have the potential to modify the innate immune response to viral infection and contribute to viral pathogenesis.

DOI: 10.1016/j.virol.2013.11.040
PubMed: 24503068

Affiliations:

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<front><div type="abstract" xml:lang="en">Coronaviruses encode papain-like proteases (PLpro) that are often multifunctional enzymes with protease activity to process the viral replicase polyprotein and deubiquitinating (DUB)/deISGylating activity, which is hypothesized to modify the innate immune response to infection. Here, we investigate the predicted DUB activity of the PLpro domain of the recently described Middle East Respiratory Syndrome Coronavirus (MERS-CoV). We found that expression of MERS-CoV PLpro reduces the levels of ubiquitinated and ISGylated host cell proteins; consistent with multifunctional PLpro activity. Further, we compared the ability of MERS-CoV PLpro and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) PLpro to block innate immune signaling of proinflammatory cytokines. We show that expression of SARS-CoV and MERS-CoV PLpros blocks upregulation of cytokines CCL5, IFN-β and CXCL10 in stimulated cells. Overall these results indicate that the PLpro domains of MERS-CoV and SARS-CoV have the potential to modify the innate immune response to viral infection and contribute to viral pathogenesis.</div>
</front>
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<Abstract><AbstractText>Coronaviruses encode papain-like proteases (PLpro) that are often multifunctional enzymes with protease activity to process the viral replicase polyprotein and deubiquitinating (DUB)/deISGylating activity, which is hypothesized to modify the innate immune response to infection. Here, we investigate the predicted DUB activity of the PLpro domain of the recently described Middle East Respiratory Syndrome Coronavirus (MERS-CoV). We found that expression of MERS-CoV PLpro reduces the levels of ubiquitinated and ISGylated host cell proteins; consistent with multifunctional PLpro activity. Further, we compared the ability of MERS-CoV PLpro and Severe Acute Respiratory Syndrome Coronavirus (SARS-CoV) PLpro to block innate immune signaling of proinflammatory cytokines. We show that expression of SARS-CoV and MERS-CoV PLpros blocks upregulation of cytokines CCL5, IFN-β and CXCL10 in stimulated cells. Overall these results indicate that the PLpro domains of MERS-CoV and SARS-CoV have the potential to modify the innate immune response to viral infection and contribute to viral pathogenesis.</AbstractText>
<CopyrightInformation>© 2013 Published by Elsevier Inc.</CopyrightInformation>
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MERS-CoV papain-like protease has deISGylating and deubiquitinating activities.

MERS-CoV papain-like protease has deISGylating and deubiquitinating activities.

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