The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds
Identifieur interne : 000842 ( Pmc/Checkpoint ); précédent : 000841; suivant : 000843The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds
Auteurs : Yahira M. Báez-Santos ; Sarah E. St. John ; Andrew D. MesecarSource :
- Antiviral Research [ 0166-3542 ] ; 2014.
Abstract
HTS and structure-based design produced naphthalene-based lead compounds with inhibition of SARS-CoV PLpro in the nM range. These naphthalene-based lead compounds have antiviral potency against SARS-CoV in cell culture. SARS-CoV PLpro naphthalene-based inhibitors are non-toxic and highly selective for SARS-CoV PLpro. Designed SARS-CoV PLpro inhibitors act through a non-covalent, competitive mechanism of inhibition. Lessons from design of SARS-CoV PLpro inhibitors have profound implications for other USPs implicated in disease processes.
Url:
DOI: 10.1016/j.antiviral.2014.12.015
PubMed: 25554382
PubMed Central: 5896749
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds</title><author><name sortKey="Baez Santos, Yahira M" sort="Baez Santos, Yahira M" uniqKey="Baez Santos Y" first="Yahira M." last="Báez-Santos">Yahira M. Báez-Santos</name></author><author><name sortKey="St John, Sarah E" sort="St John, Sarah E" uniqKey="St John S" first="Sarah E." last="St. John">Sarah E. St. John</name></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name></author></titleStmt><publicationStmt><idno type="wicri:source">PMC</idno><idno type="pmid">25554382</idno><idno type="pmc">5896749</idno><idno type="url">http://www.ncbi.nlm.nih.gov/pmc/articles/PMC5896749</idno><idno type="RBID">PMC:5896749</idno><idno type="doi">10.1016/j.antiviral.2014.12.015</idno><date when="2014">2014</date><idno type="wicri:Area/Pmc/Corpus">001691</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Corpus" wicri:corpus="PMC">001691</idno><idno type="wicri:Area/Pmc/Curation">001691</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Curation">001691</idno><idno type="wicri:Area/Pmc/Checkpoint">000842</idno><idno type="wicri:explorRef" wicri:stream="Pmc" wicri:step="Checkpoint">000842</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en" level="a" type="main">The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds</title><author><name sortKey="Baez Santos, Yahira M" sort="Baez Santos, Yahira M" uniqKey="Baez Santos Y" first="Yahira M." last="Báez-Santos">Yahira M. Báez-Santos</name></author><author><name sortKey="St John, Sarah E" sort="St John, Sarah E" uniqKey="St John S" first="Sarah E." last="St. John">Sarah E. St. John</name></author><author><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name></author></analytic><series><title level="j">Antiviral Research</title><idno type="ISSN">0166-3542</idno><idno type="eISSN">1872-9096</idno><imprint><date when="2014">2014</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><title>Highlights</title><p><list list-type="simple" id="l0005"><list-item id="o0005"><label>•</label><p id="p0235">HTS and structure-based design produced naphthalene-based lead compounds with inhibition of SARS-CoV PLpro in the nM range.</p></list-item><list-item id="o0010"><label>•</label><p id="p0240">These naphthalene-based lead compounds have antiviral potency against SARS-CoV in cell culture.</p></list-item><list-item id="o0015"><label>•</label><p id="p0245">SARS-CoV PLpro naphthalene-based inhibitors are non-toxic and highly selective for SARS-CoV PLpro.</p></list-item><list-item id="o0020"><label>•</label><p id="p0250">Designed SARS-CoV PLpro inhibitors act through a non-covalent, competitive mechanism of inhibition.</p></list-item><list-item id="o0025"><label>•</label><p id="p0255">Lessons from design of SARS-CoV PLpro inhibitors have profound implications for other USPs implicated in disease processes.</p></list-item></list></p></div></front><back><div1 type="bibliography"><listBibl><biblStruct><analytic><author><name sortKey="Angelini, M M" uniqKey="Angelini M">M.M. 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<front><journal-meta><journal-id journal-id-type="nlm-ta">Antiviral Res</journal-id><journal-id journal-id-type="iso-abbrev">Antiviral Res</journal-id><journal-title-group><journal-title>Antiviral Research</journal-title></journal-title-group><issn pub-type="ppub">0166-3542</issn><issn pub-type="epub">1872-9096</issn><publisher><publisher-name>Elsevier B.V.</publisher-name></publisher></journal-meta><article-meta><article-id pub-id-type="pmid">25554382</article-id><article-id pub-id-type="pmc">5896749</article-id><article-id pub-id-type="publisher-id">S0166-3542(14)00366-0</article-id><article-id pub-id-type="doi">10.1016/j.antiviral.2014.12.015</article-id><article-categories><subj-group subj-group-type="heading"><subject>Article</subject></subj-group></article-categories><title-group><article-title>The SARS-coronavirus papain-like protease: Structure, function and inhibition by designed antiviral compounds</article-title></title-group><contrib-group><contrib contrib-type="author" id="au005"><name><surname>Báez-Santos</surname><given-names>Yahira M.</given-names></name><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="au010"><name><surname>St. John</surname><given-names>Sarah E.</given-names></name><xref rid="fn1" ref-type="fn">1</xref></contrib><contrib contrib-type="author" id="au015"><name><surname>Mesecar</surname><given-names>Andrew D.</given-names></name><email>amesecar@purdue.edu</email><xref rid="cor1" ref-type="corresp">⁎</xref></contrib></contrib-group><aff id="af005">Department of Biological Sciences, Purdue University, West Lafayette, IN, USA</aff><aff id="af010">Department of Chemistry, Purdue University, West Lafayette, IN, USA</aff><aff id="af015">Center for Drug Discovery, Purdue University, West Lafayette, IN, USA</aff><aff id="af020">Center for Cancer Research, Purdue University, West Lafayette, IN, USA</aff><author-notes><corresp id="cor1"><label>⁎</label>Corresponding author at: Department of Biological Sciences, Purdue University, West Lafayette, IN, USA. Tel.: +1 765 494 1924. <email>amesecar@purdue.edu</email></corresp><fn id="fn1"><label>1</label><p id="np005">These authors contributed equally to this work.</p></fn></author-notes><pub-date pub-type="pmc-release"><day>29</day><month>12</month><year>2014</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"><month>3</month><year>2015</year></pub-date><pub-date pub-type="epub"><day>29</day><month>12</month><year>2014</year></pub-date><volume>115</volume><fpage>21</fpage><lpage>38</lpage><history><date date-type="received"><day>29</day><month>8</month><year>2014</year></date><date date-type="rev-recd"><day>17</day><month>12</month><year>2014</year></date><date date-type="accepted"><day>19</day><month>12</month><year>2014</year></date></history><permissions><copyright-statement>Copyright © 2014 Elsevier B.V. All rights reserved.</copyright-statement><copyright-year>2014</copyright-year><copyright-holder>Elsevier B.V.</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 abstract-type="author-highlights" id="ab005"><title>Highlights</title><p><list list-type="simple" id="l0005"><list-item id="o0005"><label>•</label><p id="p0235">HTS and structure-based design produced naphthalene-based lead compounds with inhibition of SARS-CoV PLpro in the nM range.</p></list-item><list-item id="o0010"><label>•</label><p id="p0240">These naphthalene-based lead compounds have antiviral potency against SARS-CoV in cell culture.</p></list-item><list-item id="o0015"><label>•</label><p id="p0245">SARS-CoV PLpro naphthalene-based inhibitors are non-toxic and highly selective for SARS-CoV PLpro.</p></list-item><list-item id="o0020"><label>•</label><p id="p0250">Designed SARS-CoV PLpro inhibitors act through a non-covalent, competitive mechanism of inhibition.</p></list-item><list-item id="o0025"><label>•</label><p id="p0255">Lessons from design of SARS-CoV PLpro inhibitors have profound implications for other USPs implicated in disease processes.</p></list-item></list></p></abstract><abstract id="ab010"><p>Over 10 years have passed since the deadly human coronavirus that causes severe acute respiratory syndrome (SARS-CoV) emerged from the Guangdong Province of China. Despite the fact that the SARS-CoV pandemic infected over 8500 individuals, claimed over 800 lives and cost billions of dollars in economic loss worldwide, there still are no clinically approved antiviral drugs, vaccines or monoclonal antibody therapies to treat SARS-CoV infections. The recent emergence of the deadly human coronavirus that causes Middle East respiratory syndrome (MERS-CoV) is a sobering reminder that new and deadly coronaviruses can emerge at any time with the potential to become pandemics. Therefore, the continued development of therapeutic and prophylactic countermeasures to potentially deadly coronaviruses is warranted. The coronaviral proteases, papain-like protease (PLpro) and 3C-like protease (3CLpro), are attractive antiviral drug targets because they are essential for coronaviral replication. Although the primary function of PLpro and 3CLpro are to process the viral polyprotein in a coordinated manner, PLpro has the additional function of stripping ubiquitin and ISG15 from host-cell proteins to aid coronaviruses in their evasion of the host innate immune responses. Therefore, targeting PLpro with antiviral drugs may have an advantage in not only inhibiting viral replication but also inhibiting the dysregulation of signaling cascades in infected cells that may lead to cell death in surrounding, uninfected cells. This review provides an up-to-date discussion on the SARS-CoV papain-like protease including a brief overview of the SARS-CoV genome and replication followed by a more in-depth discussion on the structure and catalytic mechanism of SARS-CoV PLpro, the multiple cellular functions of SARS-CoV PLpro, the inhibition of SARS-CoV PLpro by small molecule inhibitors, and the prospect of inhibiting papain-like protease from other coronaviruses. This paper forms part of a series of invited articles in <italic>Antiviral Research</italic> on “From SARS to MERS: 10 years of research on highly pathogenic human coronaviruses.”</p></abstract><kwd-group id="kg005"><title>Abbreviations</title><kwd>PLpro, papain-like protease</kwd><kwd>CoV, coronavirus</kwd><kwd>nsp, nonstructural protein</kwd><kwd>USP, ubiquitin-specific protease</kwd><kwd>DUB, de-ubiquitinating enzyme</kwd></kwd-group><kwd-group id="kg010"><title>Keywords</title><kwd>Papain-like protease</kwd><kwd>3C-like protease</kwd><kwd>Nsp3</kwd><kwd>SARS-CoV</kwd><kwd>MERS-CoV</kwd><kwd>Ubiquitin</kwd></kwd-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Baez Santos, Yahira M" sort="Baez Santos, Yahira M" uniqKey="Baez Santos Y" first="Yahira M." last="Báez-Santos">Yahira M. Báez-Santos</name><name sortKey="Mesecar, Andrew D" sort="Mesecar, Andrew D" uniqKey="Mesecar A" first="Andrew D." last="Mesecar">Andrew D. Mesecar</name><name sortKey="St John, Sarah E" sort="St John, Sarah E" uniqKey="St John S" first="Sarah E." last="St. John">Sarah E. St. John</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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