Progress in Anti-SARS Coronavirus Chemistry, Biology and Chemotherapy
Identifieur interne : 003D69 ( Main/Exploration ); précédent : 003D68; suivant : 003D70Progress 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
Affiliations:
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Ghosh</name><affiliation wicri:level="2"><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><placeName><region type="state">Indiana</region></placeName></affiliation></author><author><name sortKey="Xi, Kai" sort="Xi, Kai" uniqKey="Xi K" first="Kai" last="Xi">Kai Xi</name><affiliation wicri:level="2"><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><placeName><region type="state">Indiana</region></placeName></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="4"><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><placeName><region type="state">Illinois</region><settlement type="city">Chicago</settlement></placeName><orgName type="university">Université de l'Illinois à Chicago</orgName></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="2"><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><placeName><region type="state">Illinois</region></placeName></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="4"><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><placeName><region type="state">Illinois</region><settlement type="city">Chicago</settlement></placeName><orgName type="university">Université de l'Illinois à Chicago</orgName></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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Wu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Ranst, M V" uniqKey="Ranst M">M.V. Ranst</name></author><author><name sortKey="Keyaerts, E" uniqKey="Keyaerts E">E. Keyaerts</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Tan, E L" uniqKey="Tan E">E.L. Tan</name></author><author><name sortKey="Stanton, L W" uniqKey="Stanton L">L.W. Stanton</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Liu, Y" uniqKey="Liu Y">Y. Liu</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Koren, G" uniqKey="Koren G">G. Koren</name></author><author><name sortKey="King, S" uniqKey="King S">S. King</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Feldmann, H" uniqKey="Feldmann H">H. Feldmann</name></author><author><name sortKey="Li, Y" uniqKey="Li Y">Y. Li</name></author></analytic></biblStruct><biblStruct><analytic><author><name sortKey="Cinati, J" uniqKey="Cinati J">J. Cinati</name></author><author><name sortKey="Morgenstern, B" uniqKey="Morgenstern B">B. Morgenstern</name></author></analytic></biblStruct></listBibl></div1></back></TEI><affiliations><list><country><li>États-Unis</li></country><region><li>Illinois</li><li>Indiana</li></region><settlement><li>Chicago</li></settlement><orgName><li>Université de l'Illinois à Chicago</li></orgName></list><tree><country name="États-Unis"><region name="Indiana"><name sortKey="Ghosh, Arun K" sort="Ghosh, Arun K" uniqKey="Ghosh A" first="Arun K." last="Ghosh">Arun K. Ghosh</name></region><name sortKey="Baker, Susan C" sort="Baker, Susan C" uniqKey="Baker S" first="Susan C." last="Baker">Susan C. Baker</name><name sortKey="Johnson, Michael E" sort="Johnson, Michael E" uniqKey="Johnson M" first="Michael E." last="Johnson">Michael E. Johnson</name><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><name sortKey="Xi, Kai" sort="Xi, Kai" uniqKey="Xi K" first="Kai" last="Xi">Kai Xi</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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