SrasV1, PubMed, Checkpoint, bibRecord, 000C82

Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.

Identifieur interne : 000C82 ( PubMed/Checkpoint ); précédent : 000C81; suivant : 000C83

Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.

Auteurs : Fenghua Wang [République populaire de Chine] ; Cheng Chen [République populaire de Chine] ; Xuemeng Liu [République populaire de Chine] ; Kailin Yang [États-Unis] ; Xiaoling Xu [République populaire de Chine] ; Haitao Yang [République populaire de Chine]

Source :

Journal of virology [ 1098-5514 ] ; 2016.

RBID : pubmed:26656689

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence, Coronavirus, Feline (enzymology), Crystallography, X-Ray, Cysteine Endopeptidases (chemistry), Cysteine Endopeptidases (metabolism), Models, Molecular, Molecular Sequence Data, Protease Inhibitors (chemistry), Protease Inhibitors (metabolism), Protein Binding, Protein Conformation, Zinc (chemistry), Zinc (metabolism).
MESH :
- chemical , chemistry : Cysteine Endopeptidases, Protease Inhibitors, Zinc.
- enzymology : Coronavirus, Feline.
- chemical , metabolism : Cysteine Endopeptidases, Protease Inhibitors, Zinc.
- Amino Acid Sequence, Crystallography, X-Ray, Models, Molecular, Molecular Sequence Data, Protein Binding, Protein Conformation.

Abstract

Coronaviruses (CoVs) can cause highly prevalent diseases in humans and animals. Feline infectious peritonitis virus (FIPV) belongs to the genus Alphacoronavirus, resulting in a lethal systemic granulomatous disease called feline infectious peritonitis (FIP), which is one of the most important fatal infectious diseases of cats worldwide. No specific vaccines or drugs have been approved to treat FIP. CoV main proteases (M(pro)s) play a pivotal role in viral transcription and replication, making them an ideal target for drug development. Here, we report the crystal structure of FIPV M(pro) in complex with dual inhibitors, a zinc ion and a Michael acceptor. The complex structure elaborates a unique mechanism of two distinct inhibitors synergizing to inactivate the protease, providing a structural basis to design novel antivirals and suggesting the potential to take advantage of zinc as an adjunct therapy against CoV-associated diseases.

DOI: 10.1128/JVI.02685-15
PubMed: 26656689

Affiliations:

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

to stream PubMed, to step Corpus: 000D30
to stream PubMed, to step Curation: 000D30

Links to Exploration step

pubmed:26656689

Le document en format XML

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<term>Cysteine Endopeptidases (chemistry)</term>
<term>Cysteine Endopeptidases (metabolism)</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protease Inhibitors (chemistry)</term>
<term>Protease Inhibitors (metabolism)</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
<term>Zinc (chemistry)</term>
<term>Zinc (metabolism)</term>
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<term>Coronavirus félin (enzymologie)</term>
<term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases ()</term>
<term>Cysteine endopeptidases (métabolisme)</term>
<term>Données de séquences moléculaires</term>
<term>Inhibiteurs de protéases ()</term>
<term>Inhibiteurs de protéases (métabolisme)</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Séquence d'acides aminés</term>
<term>Zinc ()</term>
<term>Zinc (métabolisme)</term>
</keywords>
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<term>Protease Inhibitors</term>
<term>Zinc</term>
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</keywords>
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<term>Protease Inhibitors</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Cysteine endopeptidases</term>
<term>Inhibiteurs de protéases</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Crystallography, X-Ray</term>
<term>Models, Molecular</term>
<term>Molecular Sequence Data</term>
<term>Protein Binding</term>
<term>Protein Conformation</term>
</keywords>
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<term>Cristallographie aux rayons X</term>
<term>Cysteine endopeptidases</term>
<term>Données de séquences moléculaires</term>
<term>Inhibiteurs de protéases</term>
<term>Liaison aux protéines</term>
<term>Modèles moléculaires</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Coronaviruses (CoVs) can cause highly prevalent diseases in humans and animals. Feline infectious peritonitis virus (FIPV) belongs to the genus Alphacoronavirus, resulting in a lethal systemic granulomatous disease called feline infectious peritonitis (FIP), which is one of the most important fatal infectious diseases of cats worldwide. No specific vaccines or drugs have been approved to treat FIP. CoV main proteases (M(pro)s) play a pivotal role in viral transcription and replication, making them an ideal target for drug development. Here, we report the crystal structure of FIPV M(pro) in complex with dual inhibitors, a zinc ion and a Michael acceptor. The complex structure elaborates a unique mechanism of two distinct inhibitors synergizing to inactivate the protease, providing a structural basis to design novel antivirals and suggesting the potential to take advantage of zinc as an adjunct therapy against CoV-associated diseases.</div>
</front>
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<DateCompleted><Year>2016</Year>
<Month>06</Month>
<Day>09</Day>
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<DateRevised><Year>2019</Year>
<Month>01</Month>
<Day>09</Day>
</DateRevised>
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<Issue>4</Issue>
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<Month>02</Month>
<Day>15</Day>
</PubDate>
</JournalIssue>
<Title>Journal of virology</Title>
<ISOAbbreviation>J. Virol.</ISOAbbreviation>
</Journal>
<ArticleTitle>Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.</ArticleTitle>
<Pagination><MedlinePgn>1910-7</MedlinePgn>
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<Abstract><AbstractText Label="UNLABELLED">Coronaviruses (CoVs) can cause highly prevalent diseases in humans and animals. Feline infectious peritonitis virus (FIPV) belongs to the genus Alphacoronavirus, resulting in a lethal systemic granulomatous disease called feline infectious peritonitis (FIP), which is one of the most important fatal infectious diseases of cats worldwide. No specific vaccines or drugs have been approved to treat FIP. CoV main proteases (M(pro)s) play a pivotal role in viral transcription and replication, making them an ideal target for drug development. Here, we report the crystal structure of FIPV M(pro) in complex with dual inhibitors, a zinc ion and a Michael acceptor. The complex structure elaborates a unique mechanism of two distinct inhibitors synergizing to inactivate the protease, providing a structural basis to design novel antivirals and suggesting the potential to take advantage of zinc as an adjunct therapy against CoV-associated diseases.</AbstractText>
<AbstractText Label="IMPORTANCE" NlmCategory="OBJECTIVE">Coronaviruses (CoVs) have the largest genome size among all RNA viruses. CoV infection causes various diseases in humans and animals, including severe acute respiratory syndrome (SARS) and Middle East respiratory syndrome (MERS). No approved specific drugs or vaccinations are available to treat their infections. Here, we report a novel dual inhibition mechanism targeting CoV main protease (M(pro)) from feline infectious peritonitis virus (FIPV), which leads to lethal systemic granulomatous disease in cats. M(pro), conserved across all CoV genomes, is essential for viral replication and transcription. We demonstrated that zinc ion and a Michael acceptor-based peptidomimetic inhibitor synergistically inactivate FIPV M(pro). We also solved the structure of FIPV M(pro) complexed with two inhibitors, delineating the structural view of a dual inhibition mechanism. Our study provides new insight into the pharmaceutical strategy against CoV M(pro) through using zinc as an adjuvant therapy to enhance the efficacy of an irreversible peptidomimetic inhibitor.</AbstractText>
<CopyrightInformation>Copyright © 2016, American Society for Microbiology. All Rights Reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Fenghua</ForeName>
<Initials>F</Initials>
<AffiliationInfo><Affiliation>School of Life Sciences, Tianjin University, Tianjin, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Cheng</ForeName>
<Initials>C</Initials>
<AffiliationInfo><Affiliation>School of Life Sciences, Tianjin University, Tianjin, People's Republic of China Tianjin International Joint Academy of Biotechnology and Medicine, Tianjin, People's Republic of China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Liu</LastName>
<ForeName>Xuemeng</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Institute of Ageing Research, School of Medicine, Hangzhou Normal University, Hangzhou, China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yang</LastName>
<ForeName>Kailin</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland, Ohio, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Xu</LastName>
<ForeName>Xiaoling</ForeName>
<Initials>X</Initials>
<AffiliationInfo><Affiliation>Institute of Ageing Research, School of Medicine, Hangzhou Normal University, Hangzhou, China xuxl@hznu.edu.cn yanght@tju.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yang</LastName>
<ForeName>Haitao</ForeName>
<Initials>H</Initials>
<AffiliationInfo><Affiliation>School of Life Sciences, Tianjin University, Tianjin, People's Republic of China Tianjin International Joint Academy of Biotechnology and Medicine, Tianjin, People's Republic of China xuxl@hznu.edu.cn yanght@tju.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
</AuthorList>
<Language>eng</Language>
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<AccessionNumberList><AccessionNumber>2AMP</AccessionNumber>
</AccessionNumberList>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2015</Year>
<Month>12</Month>
<Day>09</Day>
</ArticleDate>
</Article>
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<MedlineTA>J Virol</MedlineTA>
<NlmUniqueID>0113724</NlmUniqueID>
<ISSNLinking>0022-538X</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D011480">Protease Inhibitors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber>
<NameOfSubstance UI="C099456">3C-like proteinase, Coronavirus</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber>
<NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance>
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<NameOfSubstance UI="D015032">Zinc</NameOfSubstance>
</Chemical>
</ChemicalList>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D016765" MajorTopicYN="N">Coronavirus, Feline</DescriptorName>
<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D018360" MajorTopicYN="N">Crystallography, X-Ray</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011480" MajorTopicYN="N">Protease Inhibitors</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
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<Month>10</Month>
<Day>20</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2015</Year>
<Month>11</Month>
<Day>24</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2015</Year>
<Month>12</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2015</Year>
<Month>12</Month>
<Day>15</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2016</Year>
<Month>6</Month>
<Day>10</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
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Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.

Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.

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