Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.
Identifieur interne : 000D30 ( PubMed/Corpus ); précédent : 000D29; suivant : 000D31Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.
Auteurs : Fenghua Wang ; Cheng Chen ; Xuemeng Liu ; Kailin Yang ; Xiaoling Xu ; Haitao YangSource :
- Journal of virology [ 1098-5514 ] ; 2016.
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
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Research, School of Medicine, Hangzhou Normal University, Hangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Kailin" sort="Yang, Kailin" uniqKey="Yang K" first="Kailin" last="Yang">Kailin Yang</name><affiliation><nlm:affiliation>Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland, Ohio, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Xu, Xiaoling" sort="Xu, Xiaoling" uniqKey="Xu X" first="Xiaoling" last="Xu">Xiaoling Xu</name><affiliation><nlm:affiliation>Institute of Ageing Research, School of Medicine, Hangzhou Normal University, Hangzhou, China xuxl@hznu.edu.cn yanght@tju.edu.cn.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Haitao" sort="Yang, Haitao" uniqKey="Yang H" first="Haitao" last="Yang">Haitao Yang</name><affiliation><nlm: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.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2016">2016</date><idno type="RBID">pubmed:26656689</idno><idno type="pmid">26656689</idno><idno type="doi">10.1128/JVI.02685-15</idno><idno type="wicri:Area/PubMed/Corpus">000D30</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000D30</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Crystal Structure of Feline Infectious Peritonitis Virus Main Protease in Complex with Synergetic Dual Inhibitors.</title><author><name sortKey="Wang, Fenghua" sort="Wang, Fenghua" uniqKey="Wang F" first="Fenghua" last="Wang">Fenghua Wang</name><affiliation><nlm:affiliation>School of Life Sciences, Tianjin University, Tianjin, People's Republic of China.</nlm:affiliation></affiliation></author><author><name sortKey="Chen, Cheng" sort="Chen, Cheng" uniqKey="Chen C" first="Cheng" last="Chen">Cheng Chen</name><affiliation><nlm: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.</nlm:affiliation></affiliation></author><author><name sortKey="Liu, Xuemeng" sort="Liu, Xuemeng" uniqKey="Liu X" first="Xuemeng" last="Liu">Xuemeng Liu</name><affiliation><nlm:affiliation>Institute of Ageing Research, School of Medicine, Hangzhou Normal University, Hangzhou, China.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Kailin" sort="Yang, Kailin" uniqKey="Yang K" first="Kailin" last="Yang">Kailin Yang</name><affiliation><nlm:affiliation>Cleveland Clinic Lerner College of Medicine of Case Western Reserve University, Cleveland, Ohio, USA.</nlm:affiliation></affiliation></author><author><name sortKey="Xu, Xiaoling" sort="Xu, Xiaoling" uniqKey="Xu X" first="Xiaoling" last="Xu">Xiaoling Xu</name><affiliation><nlm:affiliation>Institute of Ageing Research, School of Medicine, Hangzhou Normal University, Hangzhou, China xuxl@hznu.edu.cn yanght@tju.edu.cn.</nlm:affiliation></affiliation></author><author><name sortKey="Yang, Haitao" sort="Yang, Haitao" uniqKey="Yang H" first="Haitao" last="Yang">Haitao Yang</name><affiliation><nlm: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.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Journal of virology</title><idno type="eISSN">1098-5514</idno><imprint><date when="2016" type="published">2016</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence</term><term>Coronavirus, Feline (enzymology)</term><term>Crystallography, X-Ray</term><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></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Protease Inhibitors</term><term>Zinc</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Coronavirus, Feline</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Protease Inhibitors</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></textClass></profileDesc></teiHeader><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></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">26656689</PMID><DateCompleted><Year>2016</Year><Month>06</Month><Day>09</Day></DateCompleted><DateRevised><Year>2019</Year><Month>01</Month><Day>09</Day></DateRevised><Article PubModel="Electronic-Print"><Journal><ISSN IssnType="Electronic">1098-5514</ISSN><JournalIssue CitedMedium="Internet"><Volume>90</Volume><Issue>4</Issue><PubDate><Year>2016</Year><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></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1128/JVI.02685-15</ELocationID><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><DataBankList 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