Structural Insights into the Interaction of Coronavirus Papain-Like Proteases and Interferon-Stimulated Gene Product 15 from Different Species
Identifieur interne : 000B77 ( Main/Exploration ); précédent : 000B76; suivant : 000B78Structural Insights into the Interaction of Coronavirus Papain-Like Proteases and Interferon-Stimulated Gene Product 15 from Different Species
Auteurs : Courtney M. Daczkowski [États-Unis] ; John V. Dzimianski [États-Unis] ; Jozlyn R. Clasman [États-Unis] ; Octavia Goodwin [États-Unis] ; Andrew D. Mesecar [États-Unis] ; Scott D. Pegan [États-Unis]Source :
- Journal of Molecular Biology [ 0022-2836 ] ; 2017.
Descripteurs français
- KwdFr :
- Animaux, Cinétique, Conformation des protéines, Coronavirus du syndrome respiratoire du Moyen-Orient (enzymologie), Cristallographie aux rayons X, Cysteine endopeptidases (), Cysteine endopeptidases (métabolisme), Humains, Liaison aux protéines, Protéines virales (), Protéines virales (métabolisme), Souris, Ubiquitines (), Ubiquitines (métabolisme), Virus de l'hépatite murine (enzymologie), Virus du SRAS (enzymologie).
- MESH :
- enzymologie : Coronavirus du syndrome respiratoire du Moyen-Orient, Virus de l'hépatite murine, Virus du SRAS.
- métabolisme : Cysteine endopeptidases, Protéines virales, Ubiquitines.
- Animaux, Cinétique, Conformation des protéines, Cristallographie aux rayons X, Cysteine endopeptidases, Humains, Liaison aux protéines, Protéines virales, Souris, Ubiquitines.
English descriptors
- KwdEn :
- Animals, Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), Humans, Kinetics, Mice, Middle East Respiratory Syndrome Coronavirus (enzymology), Murine hepatitis virus (enzymology), Protein Binding, Protein Conformation, SARS Virus (enzymology), Ubiquitins (chemistry), Ubiquitins (metabolism), Viral Proteins (chemistry), Viral Proteins (metabolism).
- MESH :
- chemical , chemistry : Cysteine Endopeptidases, Ubiquitins, Viral Proteins.
- chemical , metabolism : Cysteine Endopeptidases, Ubiquitins, Viral Proteins.
- enzymology : Middle East Respiratory Syndrome Coronavirus, Murine hepatitis virus, SARS Virus.
- Animals, Crystallography, X-Ray, Humans, Kinetics, Mice, Protein Binding, Protein Conformation.
Abstract
Severe acute respiratory syndrome coronavirus (SARS-CoV) and Middle East respiratory syndrome coronavirus (MERS-CoV) encode multifunctional papain-like proteases (PLPs) that have the ability to process the viral polyprotein to facilitate RNA replication and antagonize the host innate immune response. The latter function involves reversing the post-translational modification of cellular proteins conjugated with either ubiquitin (Ub) or Ub-like interferon-stimulated gene product 15 (ISG15). Ub is known to be highly conserved among eukaryotes, but surprisingly, ISG15 is highly divergent among animals. The ramifications of this sequence divergence to the recognition of ISG15 by coronavirus PLPs at a structural and biochemical level are poorly understood. Therefore, the activity of PLPs from SARS-CoV, MERS‐CoV, and mouse hepatitis virus was evaluated against seven ISG15s originating from an assortment of animal species susceptible, and not, to certain coronavirus infections. Excitingly, our kinetic, thermodynamic, and structural analysis revealed an array of different preferences among PLPs. Included in these studies is the first insight into a coronavirus PLP’s interface with ISG15 via SARS-CoV PLpro in complex with the principle binding domain of human ISG15 (hISG15) and mouse ISG15s (mISG15s). The first X-ray structure of the full-length mISG15 protein is also reported and highlights a unique, twisted hinge region of ISG15 that is not conserved in hISG15, suggesting a potential role in differential recognition. Taken together, this new information provides a structural and biochemical understanding of the distinct specificities among coronavirus PLPs observed and addresses a critical gap of how PLPs can interact with ISG15s from a wide variety of species.
Url:
DOI: 10.1016/j.jmb.2017.04.011
PubMed: 28438633
PubMed Central: 5634334
Affiliations:
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Le document en format XML
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Daczkowski</name><affiliation wicri:level="2"><nlm:aff id="af0005">Department of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Pharmaceutical and Biomedical Sciences, University of Georgia, Athens, GA 30602</wicri:regionArea><placeName><region type="state">Géorgie (États-Unis)</region></placeName></affiliation></author><author><name sortKey="Dzimianski, John V" sort="Dzimianski, John V" uniqKey="Dzimianski J" first="John V." last="Dzimianski">John V. 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The latter function involves reversing the post-translational modification of cellular proteins conjugated with either ubiquitin (Ub) or Ub-like interferon-stimulated gene product 15 (ISG15). Ub is known to be highly conserved among eukaryotes, but surprisingly, ISG15 is highly divergent among animals. The ramifications of this sequence divergence to the recognition of ISG15 by coronavirus PLPs at a structural and biochemical level are poorly understood. Therefore, the activity of PLPs from SARS-CoV, MERS‐CoV, and mouse hepatitis virus was evaluated against seven ISG15s originating from an assortment of animal species susceptible, and not, to certain coronavirus infections. Excitingly, our kinetic, thermodynamic, and structural analysis revealed an array of different preferences among PLPs. Included in these studies is the first insight into a coronavirus PLP’s interface with ISG15 via SARS-CoV PLpro in complex with the principle binding domain of human ISG15 (hISG15) and mouse ISG15s (mISG15s). The first X-ray structure of the full-length mISG15 protein is also reported and highlights a unique, twisted hinge region of ISG15 that is not conserved in hISG15, suggesting a potential role in differential recognition. Taken together, this new information provides a structural and biochemical understanding of the distinct specificities among coronavirus PLPs observed and addresses a critical gap of how PLPs can interact with ISG15s from a wide variety of species.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Perlman, S" uniqKey="Perlman S">S. Perlman</name></author><author><name sortKey="Netland, J" uniqKey="Netland J">J. 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Dzimianski</name><name sortKey="Goodwin, Octavia" sort="Goodwin, Octavia" uniqKey="Goodwin O" first="Octavia" last="Goodwin">Octavia Goodwin</name><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><name sortKey="Pegan, Scott D" sort="Pegan, Scott D" uniqKey="Pegan S" first="Scott D." last="Pegan">Scott D. Pegan</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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