Characterization and Inhibition of the Main Protease of Severe Acute Respiratory Syndrome Coronavirus
Identifieur interne : 000816 ( Pmc/Checkpoint ); précédent : 000815; suivant : 000817Characterization and Inhibition of the Main Protease of Severe Acute Respiratory Syndrome Coronavirus
Auteurs : Chih-Jung Kuo ; Po-Huang LiangSource :
- ChemBioEng Reviews [ 2196-9744 ] ; 2015.
Abstract
The main protease of SARS‐associated coronavirus (SARS‐CoV), also called 3C‐like protease (3CLpro), is vital for the viral replication. It cleaves the replicase polyproteins at 11 sites and is a promising drug target. Several groups of inhibitors have been identified through high‐throughput screening and rational drug design. In addition to the pharmaceutical applications, a mutant 3CLpro (T25G) with an expanded S1′ space has been demonstrated to tolerate larger residues at P1′, facilitating the cleavage behind the recognition sequence. This review summarizes current developments in anti‐SARS agents targeting 3CLpro and the application of the mutant protease as a tag‐cleavage endopeptidase.
Url:
DOI: 10.1002/cben.201400031
PubMed: NONE
PubMed Central: 7159133
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It cleaves the replicase polyproteins at 11 sites and is a promising drug target. Several groups of inhibitors have been identified through high‐throughput screening and rational drug design. In addition to the pharmaceutical applications, a mutant 3CL<sup>pro</sup> (T25G) with an expanded S1′ space has been demonstrated to tolerate larger residues at P1′, facilitating the cleavage behind the recognition sequence. 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<front><journal-meta><journal-id journal-id-type="doi">10.1002/(ISSN)2196-9744</journal-id><journal-id journal-id-type="publisher-id">CBEN</journal-id><journal-title-group><journal-title>ChemBioEng Reviews</journal-title></journal-title-group><issn pub-type="epub">2196-9744</issn><publisher><publisher-name>WILEY‐VCH Verlag</publisher-name><publisher-loc>Weinheim</publisher-loc></publisher></journal-meta><article-meta><article-id pub-id-type="pmc">7159133</article-id><article-id pub-id-type="doi">10.1002/cben.201400031</article-id><article-id pub-id-type="publisher-id">CBEN201400031</article-id><article-categories><subj-group subj-group-type="overline"><subject>Review</subject></subj-group><subj-group subj-group-type="heading"><subject>Reviews</subject></subj-group></article-categories><title-group><article-title>Characterization and Inhibition of the Main Protease of Severe Acute Respiratory Syndrome Coronavirus</article-title></title-group><contrib-group><contrib id="au1" contrib-type="author" corresp="yes"><name><surname>Kuo</surname><given-names>Chih‐Jung</given-names></name><xref ref-type="aff" rid="a1"><sup>1</sup></xref><address><email>ck476@nchu.edu.tw</email></address></contrib><contrib id="au2" contrib-type="author" corresp="yes"><name><surname>Liang</surname><given-names>Po‐Huang</given-names></name><xref ref-type="aff" rid="a1"><sup>1</sup></xref><address><email>phliang@gate.sinica.edu.tw</email></address></contrib></contrib-group><aff id="a1"><label><sup>1</sup></label>National Chung Hsing University, College of Veterinary Medicine, Department of Veterinary Medicine, Taichung 402, Taiwan.</aff><aff id="a2"><label><sup>2</sup></label>Institute of Biological Chemistry, Academia Sinica, Taipei 115, Taiwan</aff><author-notes><corresp id="correspondenceTo"><label>*</label>National Chung Hsing University, College of Veterinary Medicine, Department of Veterinary Medicine, Taichung 402, Taiwan.</corresp></author-notes><pub-date pub-type="epub"><day>25</day><month>2</month><year>2015</year></pub-date><pub-date pub-type="ppub"><month>4</month><year>2015</year></pub-date><volume>2</volume><issue>2</issue><issue-id pub-id-type="doi">10.1002/cben.v2.2</issue-id><issue-title content-type="special-issue-title">Enzymes</issue-title><fpage>118</fpage><lpage>132</lpage><history><date date-type="accepted"><day>09</day><month>1</month><year>2014</year></date><date date-type="received"><day>07</day><month>11</month><year>2014</year></date><date date-type="rev-recd"><day>04</day><month>1</month><year>2015</year></date></history><permissions><copyright-statement content-type="article-copyright">Copyright © 2015 WILEY‐VCH Verlag GmbH & Co. KGaA, Weinheim</copyright-statement><license><license-p>This article is being made freely available through PubMed Central as part of the COVID-19 public health emergency response. It can be used for unrestricted research re-use and analysis in any form or by any means with acknowledgement of the original source, for the duration of the public health emergency.</license-p></license></permissions><self-uri content-type="pdf" xlink:href="file:CBEN-2-118.pdf"></self-uri><abstract><title>Abstract</title><p>The main protease of SARS‐associated coronavirus (SARS‐CoV), also called 3C‐like protease (3CL<sup>pro</sup>), is vital for the viral replication. It cleaves the replicase polyproteins at 11 sites and is a promising drug target. Several groups of inhibitors have been identified through high‐throughput screening and rational drug design. In addition to the pharmaceutical applications, a mutant 3CL<sup>pro</sup> (T25G) with an expanded S1′ space has been demonstrated to tolerate larger residues at P1′, facilitating the cleavage behind the recognition sequence. This review summarizes current developments in anti‐SARS agents targeting 3CL<sup>pro</sup> and the application of the mutant protease as a tag‐cleavage endopeptidase.</p></abstract><abstract abstract-type="graphical"><p>Severe acute respiratory syndrome (SARS)‐associated coronavirus (CoV) has disappeared, but might re‐emerge in the future, together with other new and existing CoV. The 3CL protease of SARS‐CoV, a key enzyme for viral replication, is a promising drug target for inhibitor molecules in order to combat CoVs. This review summarizes current developments and research on inhibitors against proteases and the engineering of the mutant protease as an endopeptidase. <boxed-text position="anchor" content-type="graphic" orientation="portrait"><graphic xlink:href="CBEN-2-118-g003.jpg" position="anchor" id="nlm-graphic-1" orientation="portrait"><permissions><copyright-holder>WILEY-VCH</copyright-holder></permissions></graphic></boxed-text></p></abstract><kwd-group kwd-group-type="author-generated"><kwd id="kwd1">Coronavirus</kwd><kwd id="kwd2">Enzymatic hydrolysis</kwd><kwd id="kwd3">Protease</kwd><kwd id="kwd4">Protein engineering</kwd><kwd id="kwd5">Proteins</kwd></kwd-group><counts><fig-count count="8"></fig-count><table-count count="0"></table-count><ref-count count="90"></ref-count><page-count count="15"></page-count></counts><custom-meta-group><custom-meta><meta-name>source-schema-version-number</meta-name><meta-value>2.0</meta-value></custom-meta><custom-meta><meta-name>cover-date</meta-name><meta-value>April, 2015</meta-value></custom-meta><custom-meta><meta-name>details-of-publishers-convertor</meta-name><meta-value>Converter:WILEY_ML3GV2_TO_JATSPMC version:5.8.0 mode:remove_FC converted:15.04.2020</meta-value></custom-meta></custom-meta-group></article-meta></front></pmc><affiliations><list></list><tree><noCountry><name sortKey="Kuo, Chih Ung" sort="Kuo, Chih Ung" uniqKey="Kuo C" first="Chih-Jung" last="Kuo">Chih-Jung Kuo</name><name sortKey="Liang, Po Uang" sort="Liang, Po Uang" uniqKey="Liang P" first="Po-Huang" last="Liang">Po-Huang Liang</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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