Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy
Identifieur interne : 001683 ( Pmc/Curation ); précédent : 001682; suivant : 001684Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy
Auteurs : Arun K. Ghosh [États-Unis] ; Kai Xi [États-Unis] ; Michael E. Johnson [États-Unis] ; Susan C. Baker [États-Unis] ; Andrew D. Mesecar [États-Unis]Source :
- Annual Reports in Medicinal Chemistry [ 0065-7743 ] ; 2006.
Abstract
Proteolytic processing of the coronavirus replicase polyproteins is essential for ongoing viral ribonucleic acid (RNA) synthesis. Therefore, the severe acute respiratory syndrome (SARS)-coronaviruses (SARS-CoV) proteases are attractive targets for the development of antiviral drugs to reduce viral replication and pathogenicity. The structure and activity of the coronavirus 3C-like protease (3CLpro) has already been elucidated, and the design of inhibitors to 3CLpro as therapeutics has been proposed. The chapter discusses SARS-CoV 3CLpro inhibitors that include covalent inhibitors, noncovalent inhibitors, and inhibitors from screening. SARS-CoV papain-like protease (PLpro) is considered an equally viable target to 3CLpro for drug design because both are essential for viral replication. However, PLpro has likely not been pursued because of the paucity of structural information. Several compounds have been identified that have shown inhibitory activity against SARS-CoV. However, no information regarding their mechanism of action or the corresponding target is known. Glycyrrhizin showed inhibitory activity for SARS-CoV replication with EC50 = 300 mg/L after virus absorption in Vero cells. Some glycyrrhizin acid derivatives were found to inhibit SARS-CoV replication
Url:
DOI: 10.1016/S0065-7743(06)41011-3
PubMed: 19649165
PubMed Central: 2718771
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy</title><author><name sortKey="Ghosh, Arun K" sort="Ghosh, Arun K" uniqKey="Ghosh A" first="Arun K." last="Ghosh">Arun K. Ghosh</name><affiliation wicri:level="1"><nlm:aff id="aff1">Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN</wicri:regionArea></affiliation></author><author><name sortKey="Xi, Kai" sort="Xi, Kai" uniqKey="Xi K" first="Kai" last="Xi">Kai Xi</name><affiliation wicri:level="1"><nlm:aff id="aff1">Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN</wicri:regionArea></affiliation></author><author><name sortKey="Johnson, Michael E" sort="Johnson, Michael E" uniqKey="Johnson M" first="Michael E." last="Johnson">Michael E. Johnson</name><affiliation wicri:level="1"><nlm:aff id="aff2">Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL</wicri:regionArea></affiliation></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><affiliation wicri:level="1"><nlm:aff id="aff3">Department of Microbiology and Immunology, Loyola University Medical Center, IL, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Loyola University Medical Center, IL</wicri:regionArea></affiliation></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><affiliation wicri:level="1"><nlm:aff id="aff2">Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL</wicri:regionArea></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">19649165</idno><idno type="pmc">2718771</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC2718771</idno><idno type="RBID">PMC:2718771</idno><idno type="doi">10.1016/S0065-7743(06)41011-3</idno><date when="2006">2006</date><idno type="wicri:Area/Pmc/Corpus">001683</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001683</idno><idno type="wicri:Area/Pmc/Curation">001683</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001683</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy</title><author><name sortKey="Ghosh, Arun K" sort="Ghosh, Arun K" uniqKey="Ghosh A" first="Arun K." last="Ghosh">Arun K. Ghosh</name><affiliation wicri:level="1"><nlm:aff id="aff1">Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN</wicri:regionArea></affiliation></author><author><name sortKey="Xi, Kai" sort="Xi, Kai" uniqKey="Xi K" first="Kai" last="Xi">Kai Xi</name><affiliation wicri:level="1"><nlm:aff id="aff1">Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN</wicri:regionArea></affiliation></author><author><name sortKey="Johnson, Michael E" sort="Johnson, Michael E" uniqKey="Johnson M" first="Michael E." last="Johnson">Michael E. Johnson</name><affiliation wicri:level="1"><nlm:aff id="aff2">Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL</wicri:regionArea></affiliation></author><author><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><affiliation wicri:level="1"><nlm:aff id="aff3">Department of Microbiology and Immunology, Loyola University Medical Center, IL, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Microbiology and Immunology, Loyola University Medical Center, IL</wicri:regionArea></affiliation></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><affiliation wicri:level="1"><nlm:aff id="aff2">Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL, USA</nlm:aff><country xml:lang="fr">États-Unis</country><wicri:regionArea>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL</wicri:regionArea></affiliation></author></analytic><series><title level="j">Annual Reports in Medicinal Chemistry</title><idno type="ISSN">0065-7743</idno><idno type="eISSN">1557-8437</idno><imprint><date when="2006">2006</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Publisher Summary</title><p>Proteolytic processing of the coronavirus replicase polyproteins is essential for ongoing viral ribonucleic acid (RNA) synthesis. Therefore, the severe acute respiratory syndrome (SARS)-coronaviruses (SARS-CoV) proteases are attractive targets for the development of antiviral drugs to reduce viral replication and pathogenicity. The structure and activity of the coronavirus 3C-like protease (3CLpro) has already been elucidated, and the design of inhibitors to 3CLpro as therapeutics has been proposed. The chapter discusses SARS-CoV 3CLpro inhibitors that include covalent inhibitors, noncovalent inhibitors, and inhibitors from screening. SARS-CoV papain-like protease (PLpro) is considered an equally viable target to 3CLpro for drug design because both are essential for viral replication. However, PLpro has likely not been pursued because of the paucity of structural information. Several compounds have been identified that have shown inhibitory activity against SARS-CoV. However, no information regarding their mechanism of action or the corresponding target is known. Glycyrrhizin showed inhibitory activity for SARS-CoV replication with EC<sub>50</sub> = 300 mg/L after virus absorption in Vero cells. Some glycyrrhizin acid derivatives were found to inhibit SARS-CoV replication <italic>in vitro</italic> with EC<sub>50</sub> values ranging from 5 to 50 <italic>μ</italic>M. Unfortunately, these compounds show high cytotoxity.</p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Lee, N" uniqKey="Lee N">N. Lee</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ksiazek, T G" uniqKey="Ksiazek T">T.G. Ksiazek</name></author><author><name sortKey="Erdman, D" uniqKey="Erdman D">D. Erdman</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Drosten, C" uniqKey="Drosten C">C. Drosten</name></author><author><name sortKey="Gunther, S" uniqKey="Gunther S">S. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Annu Rep Med Chem</journal-id><journal-id journal-id-type="iso-abbrev">Annu Rep Med Chem</journal-id><journal-title-group><journal-title>Annual Reports in Medicinal Chemistry</journal-title></journal-title-group><issn pub-type="ppub">0065-7743</issn><issn pub-type="epub">1557-8437</issn><publisher><publisher-name>Elsevier Inc.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">19649165</article-id><article-id pub-id-type="pmc">2718771</article-id><article-id pub-id-type="publisher-id">S0065-7743(06)41011-3</article-id><article-id pub-id-type="doi">10.1016/S0065-7743(06)41011-3</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy</article-title></title-group><contrib-group><contrib contrib-type="author"><name><surname>Ghosh</surname><given-names>Arun K.</given-names></name><xref rid="aff1" ref-type="aff">1</xref></contrib><contrib contrib-type="author"><name><surname>Xi</surname><given-names>Kai</given-names></name><xref rid="aff1" ref-type="aff">1</xref></contrib><contrib contrib-type="author"><name><surname>Johnson</surname><given-names>Michael E.</given-names></name><xref rid="aff2" ref-type="aff">2</xref></contrib><contrib contrib-type="author"><name><surname>Baker</surname><given-names>Susan C.</given-names></name><xref rid="aff3" ref-type="aff">3</xref></contrib><contrib contrib-type="author"><name><surname>Mesecar</surname><given-names>Andrew D.</given-names></name><xref rid="aff2" ref-type="aff">2</xref></contrib></contrib-group><aff id="aff1"><label>1</label>Departments of Chemistry and Medicinal Chemistry, Purdue University, West Lafayette, IN, USA</aff><aff id="aff2"><label>2</label>Center for Pharmaceutical Biotechnology and Department of Medicinal Chemistry and Pharmacognosy, University of Illinois at Chicago, IL, USA</aff><aff id="aff3"><label>3</label>Department of Microbiology and Immunology, Loyola University Medical Center, IL, USA</aff><pub-date pub-type="pmc-release"><day>26</day><month>1</month><year>2007</year></pub-date><pmc-comment> PMC Release delay is 0 months and 0 days and was based on .</pmc-comment>
<pub-date pub-type="ppub"><year>2006</year></pub-date><pub-date pub-type="epub"><day>26</day><month>1</month><year>2007</year></pub-date><volume>41</volume><fpage>183</fpage><lpage>196</lpage><permissions><copyright-statement>Copyright © 2006 Elsevier Inc. All rights reserved.</copyright-statement><copyright-year>2006</copyright-year><copyright-holder>Elsevier Inc.</copyright-holder><license><license-p>Since January 2020 Elsevier has created a COVID-19 resource centre with free information in English and Mandarin on the novel coronavirus COVID-19. The COVID-19 resource centre is hosted on Elsevier Connect, the company's public news and information website. Elsevier hereby grants permission to make all its COVID-19-related research that is available on the COVID-19 resource centre - including this research content - immediately available in PubMed Central and other publicly funded repositories, such as the WHO COVID database with rights for unrestricted research re-use and analyses in any form or by any means with acknowledgement of the original source. These permissions are granted for free by Elsevier for as long as the COVID-19 resource centre remains active.</license-p></license></permissions><abstract><title>Publisher Summary</title><p>Proteolytic processing of the coronavirus replicase polyproteins is essential for ongoing viral ribonucleic acid (RNA) synthesis. Therefore, the severe acute respiratory syndrome (SARS)-coronaviruses (SARS-CoV) proteases are attractive targets for the development of antiviral drugs to reduce viral replication and pathogenicity. The structure and activity of the coronavirus 3C-like protease (3CLpro) has already been elucidated, and the design of inhibitors to 3CLpro as therapeutics has been proposed. The chapter discusses SARS-CoV 3CLpro inhibitors that include covalent inhibitors, noncovalent inhibitors, and inhibitors from screening. SARS-CoV papain-like protease (PLpro) is considered an equally viable target to 3CLpro for drug design because both are essential for viral replication. However, PLpro has likely not been pursued because of the paucity of structural information. Several compounds have been identified that have shown inhibitory activity against SARS-CoV. However, no information regarding their mechanism of action or the corresponding target is known. Glycyrrhizin showed inhibitory activity for SARS-CoV replication with EC<sub>50</sub> = 300 mg/L after virus absorption in Vero cells. Some glycyrrhizin acid derivatives were found to inhibit SARS-CoV replication <italic>in vitro</italic> with EC<sub>50</sub> values ranging from 5 to 50 <italic>μ</italic>M. Unfortunately, these compounds show high cytotoxity.</p></abstract></article-meta></front></pmc></record>Pour manipuler ce document sous Unix (Dilib)
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