Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay.
Identifieur interne : 000C34 ( PubMed/Corpus ); précédent : 000C33; suivant : 000C35Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay.
Auteurs : Wahiba Aouadi ; Cécilia Eydoux ; Bruno Coutard ; Baptiste Martin ; Françoise Debart ; Jean Jacques Vasseur ; Jean Marie Contreras ; Christophe Morice ; Gilles Quérat ; Marie-Louise Jung ; Bruno Canard ; Jean-Claude Guillemot ; Etienne DecrolySource :
- Antiviral research [ 1872-9096 ] ; 2017.
English descriptors
- KwdEn :
- Antiviral Agents (isolation & purification), Drug Evaluation, Preclinical (methods), Exoribonucleases (antagonists & inhibitors), Fluorometry, Humans, Inhibitory Concentration 50, Methyltransferases (antagonists & inhibitors), Microbial Sensitivity Tests, SARS Virus (enzymology), Viral Nonstructural Proteins (antagonists & inhibitors).
- MESH :
- chemical , antagonists & inhibitors : Exoribonucleases, Methyltransferases, Viral Nonstructural Proteins.
- chemical , isolation & purification : Antiviral Agents.
- enzymology : SARS Virus.
- methods : Drug Evaluation, Preclinical.
- Fluorometry, Humans, Inhibitory Concentration 50, Microbial Sensitivity Tests.
Abstract
Two highly pathogenic human coronaviruses associated with severe respiratory syndromes emerged since the beginning of the century. The severe acute respiratory syndrome SARS-coronavirus (CoV) spread first in southern China in 2003 with about 8000 infected cases in few months. Then in 2012, the Middle East respiratory syndrome (MERS-CoV) emerged from the Arabian Peninsula giving a still on-going epidemic associated to a high fatality rate. CoVs are thus considered a major health threat. This is especially true as no vaccine nor specific therapeutic are available against either SARS- or MERS-CoV. Therefore, new drugs need to be identified in order to develop antiviral treatments limiting CoV replication. In this study, we focus on the nsp14 protein, which plays a key role in virus replication as it methylates the RNA cap structure at the N7 position of the guanine. We developed a high-throughput N7-MTase assay based on Homogenous Time Resolved Fluorescence (HTRF®) and screened chemical libraries (2000 compounds) on the SARS-CoV nsp14. 20 compounds inhibiting the SARS-CoV nsp14 were further evaluated by IC50 determination and their specificity was assessed toward flavivirus- and human cap N7-MTases. Our results reveal three classes of compounds: 1) molecules inhibiting several MTases as well as the dengue virus polymerase activity unspecifically, 2) pan MTases inhibitors targeting both viral and cellular MTases, and 3) inhibitors targeting one viral MTase more specifically showing however activity against the human cap N7-MTase. These compounds provide a first basis towards the development of more specific inhibitors of viral methyltransferases.
DOI: 10.1016/j.antiviral.2017.06.021
PubMed: 28676301
Links to Exploration step
pubmed:28676301Le document en format XML
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Electronic address: etienne.decroly@afmb.univ-mrs.fr.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2017">2017</date><idno type="RBID">pubmed:28676301</idno><idno type="pmid">28676301</idno><idno type="doi">10.1016/j.antiviral.2017.06.021</idno><idno type="wicri:Area/PubMed/Corpus">000C34</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000C34</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay.</title><author><name sortKey="Aouadi, Wahiba" sort="Aouadi, Wahiba" uniqKey="Aouadi W" first="Wahiba" last="Aouadi">Wahiba Aouadi</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Eydoux, Cecilia" sort="Eydoux, Cecilia" uniqKey="Eydoux C" first="Cécilia" last="Eydoux">Cécilia Eydoux</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Coutard, Bruno" sort="Coutard, Bruno" uniqKey="Coutard B" first="Bruno" last="Coutard">Bruno Coutard</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Martin, Baptiste" sort="Martin, Baptiste" uniqKey="Martin B" first="Baptiste" last="Martin">Baptiste Martin</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Debart, Francoise" sort="Debart, Francoise" uniqKey="Debart F" first="Françoise" last="Debart">Françoise Debart</name><affiliation><nlm:affiliation>IBMM, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095, Montpellier Cedex 05, France.</nlm:affiliation></affiliation></author><author><name sortKey="Vasseur, Jean Jacques" sort="Vasseur, Jean Jacques" uniqKey="Vasseur J" first="Jean Jacques" last="Vasseur">Jean Jacques Vasseur</name><affiliation><nlm:affiliation>IBMM, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095, Montpellier Cedex 05, France.</nlm:affiliation></affiliation></author><author><name sortKey="Contreras, Jean Marie" sort="Contreras, Jean Marie" uniqKey="Contreras J" first="Jean Marie" last="Contreras">Jean Marie Contreras</name><affiliation><nlm:affiliation>Prestwick Chemical, 67400, Illkirch, Strasbourg, France.</nlm:affiliation></affiliation></author><author><name sortKey="Morice, Christophe" sort="Morice, Christophe" uniqKey="Morice C" first="Christophe" last="Morice">Christophe Morice</name><affiliation><nlm:affiliation>Prestwick Chemical, 67400, Illkirch, Strasbourg, France.</nlm:affiliation></affiliation></author><author><name sortKey="Querat, Gilles" sort="Querat, Gilles" uniqKey="Querat G" first="Gilles" last="Quérat">Gilles Quérat</name><affiliation><nlm:affiliation>UMR "Emergence des Pathologies Virales" (EPV: Aix-Marseille Université - IRD 190 - Inserm 1207 - EHESP), Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Jung, Marie Louise" sort="Jung, Marie Louise" uniqKey="Jung M" first="Marie-Louise" last="Jung">Marie-Louise Jung</name><affiliation><nlm:affiliation>Prestwick Chemical, 67400, Illkirch, Strasbourg, France.</nlm:affiliation></affiliation></author><author><name sortKey="Canard, Bruno" sort="Canard, Bruno" uniqKey="Canard B" first="Bruno" last="Canard">Bruno Canard</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Guillemot, Jean Claude" sort="Guillemot, Jean Claude" uniqKey="Guillemot J" first="Jean-Claude" last="Guillemot">Jean-Claude Guillemot</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</nlm:affiliation></affiliation></author><author><name sortKey="Decroly, Etienne" sort="Decroly, Etienne" uniqKey="Decroly E" first="Etienne" last="Decroly">Etienne Decroly</name><affiliation><nlm:affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France. Electronic address: etienne.decroly@afmb.univ-mrs.fr.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Antiviral research</title><idno type="eISSN">1872-9096</idno><imprint><date when="2017" type="published">2017</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antiviral Agents (isolation & purification)</term><term>Drug Evaluation, Preclinical (methods)</term><term>Exoribonucleases (antagonists & inhibitors)</term><term>Fluorometry</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Methyltransferases (antagonists & inhibitors)</term><term>Microbial Sensitivity Tests</term><term>SARS Virus (enzymology)</term><term>Viral Nonstructural Proteins (antagonists & inhibitors)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Exoribonucleases</term><term>Methyltransferases</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Antiviral Agents</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="methods" xml:lang="en"><term>Drug Evaluation, Preclinical</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Fluorometry</term><term>Humans</term><term>Inhibitory Concentration 50</term><term>Microbial Sensitivity Tests</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Two highly pathogenic human coronaviruses associated with severe respiratory syndromes emerged since the beginning of the century. The severe acute respiratory syndrome SARS-coronavirus (CoV) spread first in southern China in 2003 with about 8000 infected cases in few months. Then in 2012, the Middle East respiratory syndrome (MERS-CoV) emerged from the Arabian Peninsula giving a still on-going epidemic associated to a high fatality rate. CoVs are thus considered a major health threat. This is especially true as no vaccine nor specific therapeutic are available against either SARS- or MERS-CoV. Therefore, new drugs need to be identified in order to develop antiviral treatments limiting CoV replication. In this study, we focus on the nsp14 protein, which plays a key role in virus replication as it methylates the RNA cap structure at the N7 position of the guanine. We developed a high-throughput N7-MTase assay based on Homogenous Time Resolved Fluorescence (HTRF<sup>®</sup>) and screened chemical libraries (2000 compounds) on the SARS-CoV nsp14. 20 compounds inhibiting the SARS-CoV nsp14 were further evaluated by IC<sub>50</sub> determination and their specificity was assessed toward flavivirus- and human cap N7-MTases. Our results reveal three classes of compounds: 1) molecules inhibiting several MTases as well as the dengue virus polymerase activity unspecifically, 2) pan MTases inhibitors targeting both viral and cellular MTases, and 3) inhibitors targeting one viral MTase more specifically showing however activity against the human cap N7-MTase. These compounds provide a first basis towards the development of more specific inhibitors of viral methyltransferases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">28676301</PMID><DateCompleted><Year>2018</Year><Month>03</Month><Day>29</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9096</ISSN><JournalIssue CitedMedium="Internet"><Volume>144</Volume><PubDate><Year>2017</Year><Month>08</Month></PubDate></JournalIssue><Title>Antiviral research</Title><ISOAbbreviation>Antiviral Res.</ISOAbbreviation></Journal><ArticleTitle>Toward the identification of viral cap-methyltransferase inhibitors by fluorescence screening assay.</ArticleTitle><Pagination><MedlinePgn>330-339</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0166-3542(17)30391-1</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.antiviral.2017.06.021</ELocationID><Abstract><AbstractText>Two highly pathogenic human coronaviruses associated with severe respiratory syndromes emerged since the beginning of the century. The severe acute respiratory syndrome SARS-coronavirus (CoV) spread first in southern China in 2003 with about 8000 infected cases in few months. Then in 2012, the Middle East respiratory syndrome (MERS-CoV) emerged from the Arabian Peninsula giving a still on-going epidemic associated to a high fatality rate. CoVs are thus considered a major health threat. This is especially true as no vaccine nor specific therapeutic are available against either SARS- or MERS-CoV. Therefore, new drugs need to be identified in order to develop antiviral treatments limiting CoV replication. In this study, we focus on the nsp14 protein, which plays a key role in virus replication as it methylates the RNA cap structure at the N7 position of the guanine. We developed a high-throughput N7-MTase assay based on Homogenous Time Resolved Fluorescence (HTRF<sup>®</sup>) and screened chemical libraries (2000 compounds) on the SARS-CoV nsp14. 20 compounds inhibiting the SARS-CoV nsp14 were further evaluated by IC<sub>50</sub> determination and their specificity was assessed toward flavivirus- and human cap N7-MTases. Our results reveal three classes of compounds: 1) molecules inhibiting several MTases as well as the dengue virus polymerase activity unspecifically, 2) pan MTases inhibitors targeting both viral and cellular MTases, and 3) inhibitors targeting one viral MTase more specifically showing however activity against the human cap N7-MTase. These compounds provide a first basis towards the development of more specific inhibitors of viral methyltransferases.</AbstractText><CopyrightInformation>Copyright © 2017. Published by Elsevier B.V.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Aouadi</LastName><ForeName>Wahiba</ForeName><Initials>W</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Eydoux</LastName><ForeName>Cécilia</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Coutard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Martin</LastName><ForeName>Baptiste</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Debart</LastName><ForeName>Françoise</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>IBMM, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095, Montpellier Cedex 05, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Vasseur</LastName><ForeName>Jean Jacques</ForeName><Initials>JJ</Initials><AffiliationInfo><Affiliation>IBMM, CNRS, Université Montpellier, ENSCM, Campus Triolet, Place E. Bataillon, 34095, Montpellier Cedex 05, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Contreras</LastName><ForeName>Jean Marie</ForeName><Initials>JM</Initials><AffiliationInfo><Affiliation>Prestwick Chemical, 67400, Illkirch, Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Morice</LastName><ForeName>Christophe</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Prestwick Chemical, 67400, Illkirch, Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Quérat</LastName><ForeName>Gilles</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>UMR "Emergence des Pathologies Virales" (EPV: Aix-Marseille Université - IRD 190 - Inserm 1207 - EHESP), Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Jung</LastName><ForeName>Marie-Louise</ForeName><Initials>ML</Initials><AffiliationInfo><Affiliation>Prestwick Chemical, 67400, Illkirch, Strasbourg, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Canard</LastName><ForeName>Bruno</ForeName><Initials>B</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Guillemot</LastName><ForeName>Jean-Claude</ForeName><Initials>JC</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Decroly</LastName><ForeName>Etienne</ForeName><Initials>E</Initials><AffiliationInfo><Affiliation>Aix Marseille Université, CNRS, AFMB UMR 7257, Marseille, France. Electronic address: etienne.decroly@afmb.univ-mrs.fr.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2017</Year><Month>07</Month><Day>01</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Antiviral Res</MedlineTA><NlmUniqueID>8109699</NlmUniqueID><ISSNLinking>0166-3542</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.56</RegistryNumber><NameOfSubstance UI="C525596">nsp14 protein, SARS coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="D005095">Exoribonucleases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000998" MajorTopicYN="N">Antiviral Agents</DescriptorName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004353" MajorTopicYN="N">Drug Evaluation, Preclinical</DescriptorName><QualifierName UI="Q000379" MajorTopicYN="Y">methods</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005095" MajorTopicYN="N">Exoribonucleases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005470" MajorTopicYN="N">Fluorometry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020128" MajorTopicYN="N">Inhibitory Concentration 50</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008826" MajorTopicYN="N">Microbial Sensitivity Tests</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Antiviral</Keyword><Keyword MajorTopicYN="Y">Coronavirus</Keyword><Keyword MajorTopicYN="Y">Flavivirus</Keyword><Keyword MajorTopicYN="Y">HTRF</Keyword><Keyword MajorTopicYN="Y">Inhibitor</Keyword><Keyword MajorTopicYN="Y">Methyltransferase</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2017</Year><Month>05</Month><Day>22</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2017</Year><Month>06</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2017</Year><Month>06</Month><Day>29</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2017</Year><Month>7</Month><Day>6</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>3</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate 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