Inhibitor recognition specificity of MERS-CoV papain-like protease may differ from that of SARS-CoV.
Identifieur interne : 001681 ( PubMed/Curation ); précédent : 001680; suivant : 001682Inhibitor recognition specificity of MERS-CoV papain-like protease may differ from that of SARS-CoV.
Auteurs : Hyun Lee [États-Unis] ; Hao Lei [États-Unis] ; Bernard D. Santarsiero [États-Unis] ; Joseph L. Gatuz [États-Unis] ; Shuyi Cao [États-Unis] ; Amy J. Rice [États-Unis] ; Kavankumar Patel [États-Unis] ; Michael Z. Szypulinski [États-Unis] ; Isabel Ojeda ; Arun K. Ghosh [États-Unis] ; Michael E. Johnson [États-Unis]Source :
- ACS chemical biology [ 1554-8937 ] ; 2015.
Descripteurs français
- KwdFr :
- Antiviraux (), Cinétique, Coronavirus du syndrome respiratoire du Moyen-Orient (), Coronavirus du syndrome respiratoire du Moyen-Orient (enzymologie), Cysteine endopeptidases (), Domaine catalytique, Données de séquences moléculaires, Endopeptidases (), Humains, Inhibiteurs de protéases (), Liaison aux protéines, Modèles moléculaires, Protéines recombinantes (), Protéines virales (), Protéines virales (antagonistes et inhibiteurs), Régulation allostérique, Résonance plasmonique de surface, Spécificité d'espèce, Structure secondaire des protéines, Séquence d'acides aminés, Tests de criblage à haut débit, Ubiquitin thiolesterase (), Ubiquitin thiolesterase (antagonistes et inhibiteurs), Virus du SRAS (), Virus du SRAS (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Protéines virales, Ubiquitin thiolesterase.
- enzymologie : Coronavirus du syndrome respiratoire du Moyen-Orient, Virus du SRAS.
- Antiviraux, Cinétique, Coronavirus du syndrome respiratoire du Moyen-Orient, Cysteine endopeptidases, Domaine catalytique, Données de séquences moléculaires, Endopeptidases, Humains, Inhibiteurs de protéases, Liaison aux protéines, Modèles moléculaires, Protéines recombinantes, Protéines virales, Régulation allostérique, Résonance plasmonique de surface, Spécificité d'espèce, Structure secondaire des protéines, Séquence d'acides aminés, Tests de criblage à haut débit, Ubiquitin thiolesterase, Virus du SRAS.
English descriptors
- KwdEn :
- Allosteric Regulation, Amino Acid Sequence, Antiviral Agents (chemistry), Catalytic Domain, Cysteine Endopeptidases (chemistry), Endopeptidases (chemistry), High-Throughput Screening Assays, Humans, Kinetics, Middle East Respiratory Syndrome Coronavirus (chemistry), Middle East Respiratory Syndrome Coronavirus (enzymology), Models, Molecular, Molecular Sequence Data, Protease Inhibitors (chemistry), Protein Binding, Protein Structure, Secondary, Recombinant Proteins (chemistry), SARS Virus (chemistry), SARS Virus (enzymology), Species Specificity, Surface Plasmon Resonance, Ubiquitin Thiolesterase (antagonists & inhibitors), Ubiquitin Thiolesterase (chemistry), Viral Proteins (antagonists & inhibitors), Viral Proteins (chemistry).
- MESH :
- chemical , antagonists & inhibitors : Ubiquitin Thiolesterase, Viral Proteins.
- chemical , chemistry : Antiviral Agents, Cysteine Endopeptidases, Endopeptidases, Protease Inhibitors, Recombinant Proteins, Ubiquitin Thiolesterase, Viral Proteins.
- chemistry : Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- enzymology : Middle East Respiratory Syndrome Coronavirus, SARS Virus.
- Allosteric Regulation, Amino Acid Sequence, Catalytic Domain, High-Throughput Screening Assays, Humans, Kinetics, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Structure, Secondary, Species Specificity, Surface Plasmon Resonance.
Abstract
The Middle East Respiratory Syndrome coronavirus (MERS-CoV) papain-like protease (PLpro) blocking loop 2 (BL2) structure differs significantly from that of SARS-CoV PLpro, where it has been proven to play a crucial role in SARS-CoV PLpro inhibitor binding. Four SARS-CoV PLpro lead inhibitors were tested against MERS-CoV PLpro, none of which were effective against MERS-CoV PLpro. Structure and sequence alignments revealed that two residues, Y269 and Q270, responsible for inhibitor binding to SARS-CoV PLpro, were replaced by T274 and A275 in MERS-CoV PLpro, making critical binding interactions difficult to form for similar types of inhibitors. High-throughput screening (HTS) of 25 000 compounds against both PLpro enzymes identified a small fragment-like noncovalent dual inhibitor. Mode of inhibition studies by enzyme kinetics and competition surface plasmon resonance (SPR) analyses suggested that this compound acts as a competitive inhibitor with an IC50 of 6 μM against MERS-CoV PLpro, indicating that it binds to the active site, whereas it acts as an allosteric inhibitor against SARS-CoV PLpro with an IC50 of 11 μM. These results raised the possibility that inhibitor recognition specificity of MERS-CoV PLpro may differ from that of SARS-CoV PLpro. In addition, inhibitory activity of this compound was selective for SARS-CoV and MERS-CoV PLpro enzymes over two human homologues, the ubiquitin C-terminal hydrolases 1 and 3 (hUCH-L1 and hUCH-L3).
DOI: 10.1021/cb500917m
PubMed: 25746232
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Allosteric Regulation</term>
<term>Amino Acid Sequence</term>
<term>Antiviral Agents (chemistry)</term>
<term>Catalytic Domain</term>
<term>Cysteine Endopeptidases (chemistry)</term>
<term>Endopeptidases (chemistry)</term>
<term>High-Throughput Screening Assays</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Middle East Respiratory Syndrome Coronavirus (chemistry)</term>
<term>Middle East Respiratory Syndrome Coronavirus (enzymology)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protease Inhibitors (chemistry)</term>
<term>Protein Binding</term>
<term>Protein Structure, Secondary</term>
<term>Recombinant Proteins (chemistry)</term>
<term>SARS Virus (chemistry)</term>
<term>SARS Virus (enzymology)</term>
<term>Species Specificity</term>
<term>Surface Plasmon Resonance</term>
<term>Ubiquitin Thiolesterase (antagonists & inhibitors)</term>
<term>Ubiquitin Thiolesterase (chemistry)</term>
<term>Viral Proteins (antagonists & inhibitors)</term>
<term>Viral Proteins (chemistry)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Antiviraux ()</term>
<term>Cinétique</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient ()</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient (enzymologie)</term>
<term>Cysteine endopeptidases ()</term>
<term>Domaine catalytique</term>
<term>Données de séquences moléculaires</term>
<term>Endopeptidases ()</term>
<term>Humains</term>
<term>Inhibiteurs de protéases ()</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Protéines recombinantes ()</term>
<term>Protéines virales ()</term>
<term>Protéines virales (antagonistes et inhibiteurs)</term>
<term>Régulation allostérique</term>
<term>Résonance plasmonique de surface</term>
<term>Spécificité d'espèce</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Tests de criblage à haut débit</term>
<term>Ubiquitin thiolesterase ()</term>
<term>Ubiquitin thiolesterase (antagonistes et inhibiteurs)</term>
<term>Virus du SRAS ()</term>
<term>Virus du SRAS (enzymologie)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Ubiquitin Thiolesterase</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Antiviral Agents</term>
<term>Cysteine Endopeptidases</term>
<term>Endopeptidases</term>
<term>Protease Inhibitors</term>
<term>Recombinant Proteins</term>
<term>Ubiquitin Thiolesterase</term>
<term>Viral Proteins</term>
</keywords>
<keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Protéines virales</term>
<term>Ubiquitin thiolesterase</term>
</keywords>
<keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Virus du SRAS</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Middle East Respiratory Syndrome Coronavirus</term>
<term>SARS Virus</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Allosteric Regulation</term>
<term>Amino Acid Sequence</term>
<term>Catalytic Domain</term>
<term>High-Throughput Screening Assays</term>
<term>Humans</term>
<term>Kinetics</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Structure, Secondary</term>
<term>Species Specificity</term>
<term>Surface Plasmon Resonance</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Antiviraux</term>
<term>Cinétique</term>
<term>Coronavirus du syndrome respiratoire du Moyen-Orient</term>
<term>Cysteine endopeptidases</term>
<term>Domaine catalytique</term>
<term>Données de séquences moléculaires</term>
<term>Endopeptidases</term>
<term>Humains</term>
<term>Inhibiteurs de protéases</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Protéines recombinantes</term>
<term>Protéines virales</term>
<term>Régulation allostérique</term>
<term>Résonance plasmonique de surface</term>
<term>Spécificité d'espèce</term>
<term>Structure secondaire des protéines</term>
<term>Séquence d'acides aminés</term>
<term>Tests de criblage à haut débit</term>
<term>Ubiquitin thiolesterase</term>
<term>Virus du SRAS</term>
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<front><div type="abstract" xml:lang="en">The Middle East Respiratory Syndrome coronavirus (MERS-CoV) papain-like protease (PLpro) blocking loop 2 (BL2) structure differs significantly from that of SARS-CoV PLpro, where it has been proven to play a crucial role in SARS-CoV PLpro inhibitor binding. Four SARS-CoV PLpro lead inhibitors were tested against MERS-CoV PLpro, none of which were effective against MERS-CoV PLpro. Structure and sequence alignments revealed that two residues, Y269 and Q270, responsible for inhibitor binding to SARS-CoV PLpro, were replaced by T274 and A275 in MERS-CoV PLpro, making critical binding interactions difficult to form for similar types of inhibitors. High-throughput screening (HTS) of 25 000 compounds against both PLpro enzymes identified a small fragment-like noncovalent dual inhibitor. Mode of inhibition studies by enzyme kinetics and competition surface plasmon resonance (SPR) analyses suggested that this compound acts as a competitive inhibitor with an IC50 of 6 μM against MERS-CoV PLpro, indicating that it binds to the active site, whereas it acts as an allosteric inhibitor against SARS-CoV PLpro with an IC50 of 11 μM. These results raised the possibility that inhibitor recognition specificity of MERS-CoV PLpro may differ from that of SARS-CoV PLpro. In addition, inhibitory activity of this compound was selective for SARS-CoV and MERS-CoV PLpro enzymes over two human homologues, the ubiquitin C-terminal hydrolases 1 and 3 (hUCH-L1 and hUCH-L3). </div>
</front>
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<Title>ACS chemical biology</Title>
<ISOAbbreviation>ACS Chem. Biol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Inhibitor recognition specificity of MERS-CoV papain-like protease may differ from that of SARS-CoV.</ArticleTitle>
<Pagination><MedlinePgn>1456-65</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/cb500917m</ELocationID>
<Abstract><AbstractText>The Middle East Respiratory Syndrome coronavirus (MERS-CoV) papain-like protease (PLpro) blocking loop 2 (BL2) structure differs significantly from that of SARS-CoV PLpro, where it has been proven to play a crucial role in SARS-CoV PLpro inhibitor binding. Four SARS-CoV PLpro lead inhibitors were tested against MERS-CoV PLpro, none of which were effective against MERS-CoV PLpro. Structure and sequence alignments revealed that two residues, Y269 and Q270, responsible for inhibitor binding to SARS-CoV PLpro, were replaced by T274 and A275 in MERS-CoV PLpro, making critical binding interactions difficult to form for similar types of inhibitors. High-throughput screening (HTS) of 25 000 compounds against both PLpro enzymes identified a small fragment-like noncovalent dual inhibitor. Mode of inhibition studies by enzyme kinetics and competition surface plasmon resonance (SPR) analyses suggested that this compound acts as a competitive inhibitor with an IC50 of 6 μM against MERS-CoV PLpro, indicating that it binds to the active site, whereas it acts as an allosteric inhibitor against SARS-CoV PLpro with an IC50 of 11 μM. These results raised the possibility that inhibitor recognition specificity of MERS-CoV PLpro may differ from that of SARS-CoV PLpro. In addition, inhibitory activity of this compound was selective for SARS-CoV and MERS-CoV PLpro enzymes over two human homologues, the ubiquitin C-terminal hydrolases 1 and 3 (hUCH-L1 and hUCH-L3). </AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lee</LastName>
<ForeName>Hyun</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Lei</LastName>
<ForeName>Hao</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Santarsiero</LastName>
<ForeName>Bernard D</ForeName>
<Initials>BD</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Gatuz</LastName>
<ForeName>Joseph L</ForeName>
<Initials>JL</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Cao</LastName>
<ForeName>Shuyi</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Rice</LastName>
<ForeName>Amy J</ForeName>
<Initials>AJ</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Patel</LastName>
<ForeName>Kavankumar</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Szypulinski</LastName>
<ForeName>Michael Z</ForeName>
<Initials>MZ</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
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<ForeName>Isabel</ForeName>
<Initials>I</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ghosh</LastName>
<ForeName>Arun K</ForeName>
<Initials>AK</Initials>
<AffiliationInfo><Affiliation>‡Departments of Chemistry and Medicinal Chemistry, Purdue University, 560 Oval Drive, West Lafayette, Indiana 47907, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Johnson</LastName>
<ForeName>Michael E</ForeName>
<Initials>ME</Initials>
<AffiliationInfo><Affiliation>†Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, 900 S. Ashland, Chicago, Illinois 60607, United States.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
<GrantList CompleteYN="Y"><Grant><GrantID>R37 GM053386</GrantID>
<Acronym>GM</Acronym>
<Agency>NIGMS NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>R56 AI089535</GrantID>
<Acronym>AI</Acronym>
<Agency>NIAID NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32 DE018381</GrantID>
<Acronym>DE</Acronym>
<Agency>NIDCR NIH HHS</Agency>
<Country>United States</Country>
</Grant>
<Grant><GrantID>T32-DE018381</GrantID>
<Acronym>DE</Acronym>
<Agency>NIDCR NIH HHS</Agency>
<Country>United States</Country>
</Grant>
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<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
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<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>03</Month>
<Day>16</Day>
</ArticleDate>
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<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>ACS Chem Biol</MedlineTA>
<NlmUniqueID>101282906</NlmUniqueID>
<ISSNLinking>1554-8929</ISSNLinking>
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<NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance>
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<Chemical><RegistryNumber>0</RegistryNumber>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName UI="D000494" MajorTopicYN="N">Allosteric Regulation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
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<MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName>
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<MeshHeading><DescriptorName UI="D065207" MajorTopicYN="N">Middle East Respiratory Syndrome Coronavirus</DescriptorName>
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<MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName>
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<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
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<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
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<MeshHeading><DescriptorName UI="D013045" MajorTopicYN="N">Species Specificity</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D020349" MajorTopicYN="N">Surface Plasmon Resonance</DescriptorName>
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<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
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