Profiling of substrate specificity of SARS-CoV 3CL.
Identifieur interne : 001608 ( PubMed/Corpus ); précédent : 001607; suivant : 001609Profiling of substrate specificity of SARS-CoV 3CL.
Auteurs : Chi-Pang Chuck ; Lin-Tat Chong ; Chao Chen ; Hak-Fun Chow ; David Chi-Cheong Wan ; Kam-Bo WongSource :
- PloS one [ 1932-6203 ] ; 2010.
English descriptors
- KwdEn :
- MESH :
- chemical , metabolism : Cysteine Endopeptidases, Viral Proteins.
- enzymology : SARS Virus.
- Fluorescence Resonance Energy Transfer, Hydrolysis, Substrate Specificity.
Abstract
The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome-coronavirus is required for autoprocessing of the polyprotein, and is a potential target for treating coronaviral infection.
DOI: 10.1371/journal.pone.0013197
PubMed: 20949131
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pubmed:20949131Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Profiling of substrate specificity of SARS-CoV 3CL.</title><author><name sortKey="Chuck, Chi Pang" sort="Chuck, Chi Pang" uniqKey="Chuck C" first="Chi-Pang" last="Chuck">Chi-Pang Chuck</name><affiliation><nlm:affiliation>School of Biochemical Sciences, The Chinese University of Hong Kong, Sha Tin, Hong Kong, China.</nlm:affiliation></affiliation></author><author><name sortKey="Chong, Lin Tat" sort="Chong, Lin Tat" uniqKey="Chong L" first="Lin-Tat" last="Chong">Lin-Tat Chong</name></author><author><name sortKey="Chen, Chao" sort="Chen, Chao" uniqKey="Chen C" first="Chao" last="Chen">Chao Chen</name></author><author><name sortKey="Chow, Hak Fun" sort="Chow, Hak Fun" uniqKey="Chow H" first="Hak-Fun" last="Chow">Hak-Fun Chow</name></author><author><name sortKey="Wan, David Chi Cheong" sort="Wan, David Chi Cheong" uniqKey="Wan D" first="David Chi-Cheong" last="Wan">David Chi-Cheong Wan</name></author><author><name sortKey="Wong, Kam Bo" sort="Wong, Kam Bo" uniqKey="Wong K" first="Kam-Bo" last="Wong">Kam-Bo Wong</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2010">2010</date><idno type="RBID">pubmed:20949131</idno><idno type="pmid">20949131</idno><idno type="doi">10.1371/journal.pone.0013197</idno><idno type="wicri:Area/PubMed/Corpus">001608</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">001608</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Profiling of substrate specificity of SARS-CoV 3CL.</title><author><name sortKey="Chuck, Chi Pang" sort="Chuck, Chi Pang" uniqKey="Chuck C" first="Chi-Pang" last="Chuck">Chi-Pang Chuck</name><affiliation><nlm:affiliation>School of Biochemical Sciences, The Chinese University of Hong Kong, Sha Tin, Hong Kong, China.</nlm:affiliation></affiliation></author><author><name sortKey="Chong, Lin Tat" sort="Chong, Lin Tat" uniqKey="Chong L" first="Lin-Tat" last="Chong">Lin-Tat Chong</name></author><author><name sortKey="Chen, Chao" sort="Chen, Chao" uniqKey="Chen C" first="Chao" last="Chen">Chao Chen</name></author><author><name sortKey="Chow, Hak Fun" sort="Chow, Hak Fun" uniqKey="Chow H" first="Hak-Fun" last="Chow">Hak-Fun Chow</name></author><author><name sortKey="Wan, David Chi Cheong" sort="Wan, David Chi Cheong" uniqKey="Wan D" first="David Chi-Cheong" last="Wan">David Chi-Cheong Wan</name></author><author><name sortKey="Wong, Kam Bo" sort="Wong, Kam Bo" uniqKey="Wong K" first="Kam-Bo" last="Wong">Kam-Bo Wong</name></author></analytic><series><title level="j">PloS one</title><idno type="eISSN">1932-6203</idno><imprint><date when="2010" type="published">2010</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Cysteine Endopeptidases (metabolism)</term><term>Fluorescence Resonance Energy Transfer</term><term>Hydrolysis</term><term>SARS Virus (enzymology)</term><term>Substrate Specificity</term><term>Viral Proteins (metabolism)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cysteine Endopeptidases</term><term>Viral Proteins</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Fluorescence Resonance Energy Transfer</term><term>Hydrolysis</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome-coronavirus is required for autoprocessing of the polyprotein, and is a potential target for treating coronaviral infection.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">20949131</PMID><DateCompleted><Year>2011</Year><Month>03</Month><Day>07</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>13</Day></DateRevised><Article PubModel="Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN><JournalIssue CitedMedium="Internet"><Volume>5</Volume><Issue>10</Issue><PubDate><Year>2010</Year><Month>Oct</Month><Day>06</Day></PubDate></JournalIssue><Title>PloS one</Title><ISOAbbreviation>PLoS ONE</ISOAbbreviation></Journal><ArticleTitle>Profiling of substrate specificity of SARS-CoV 3CL.</ArticleTitle><Pagination><MedlinePgn>e13197</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0013197</ELocationID><ELocationID EIdType="pii" ValidYN="Y">e13197</ELocationID><Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">The 3C-like protease (3CL(pro)) of severe acute respiratory syndrome-coronavirus is required for autoprocessing of the polyprotein, and is a potential target for treating coronaviral infection.</AbstractText><AbstractText Label="METHODOLOGY/PRINCIPAL FINDINGS" NlmCategory="RESULTS">To obtain a thorough understanding of substrate specificity of the protease, a substrate library of 198 variants was created by performing saturation mutagenesis on the autocleavage sequence at P5 to P3' positions. The substrate sequences were inserted between cyan and yellow fluorescent proteins so that the cleavage rates were monitored by in vitro fluorescence resonance energy transfer. The relative cleavage rate for different substrate sequences was correlated with various structural properties. P5 and P3 positions prefer residues with high β-sheet propensity; P4 prefers small hydrophobic residues; P2 prefers hydrophobic residues without β-branch. Gln is the best residue at P1 position, but observable cleavage can be detected with His and Met substitutions. P1' position prefers small residues, while P2' and P3' positions have no strong preference on residue substitutions. Noteworthy, solvent exposed sites such as P5, P3 and P3' positions favour positively charged residues over negatively charged one, suggesting that electrostatic interactions may play a role in catalysis. A super-active substrate, which combined the preferred residues at P5 to P1 positions, was found to have 2.8 fold higher activity than the wild-type sequence.</AbstractText><AbstractText Label="CONCLUSIONS/SIGNIFICANCE" NlmCategory="CONCLUSIONS">Our results demonstrated a strong structure-activity relationship between the 3CL(pro) and its substrate. The substrate specificity profiled in this study may provide insights into a rational design of peptidomimetic inhibitors.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Chuck</LastName><ForeName>Chi-Pang</ForeName><Initials>CP</Initials><AffiliationInfo><Affiliation>School of Biochemical Sciences, The Chinese University of Hong Kong, Sha Tin, Hong Kong, China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chong</LastName><ForeName>Lin-Tat</ForeName><Initials>LT</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Chao</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Chow</LastName><ForeName>Hak-Fun</ForeName><Initials>HF</Initials></Author><Author ValidYN="Y"><LastName>Wan</LastName><ForeName>David Chi-Cheong</ForeName><Initials>DC</Initials></Author><Author ValidYN="Y"><LastName>Wong</LastName><ForeName>Kam-Bo</ForeName><Initials>KB</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2010</Year><Month>10</Month><Day>06</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>PLoS One</MedlineTA><NlmUniqueID>101285081</NlmUniqueID><ISSNLinking>1932-6203</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber><NameOfSubstance UI="D003546">Cysteine Endopeptidases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.28</RegistryNumber><NameOfSubstance UI="C052731">3C proteases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D003546" MajorTopicYN="N">Cysteine Endopeptidases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D031541" MajorTopicYN="N">Fluorescence Resonance Energy Transfer</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year><Month>07</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2010</Year><Month>09</Month><Day>13</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2010</Year><Month>10</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2010</Year><Month>10</Month><Day>16</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2011</Year><Month>3</Month><Day>8</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>epublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">20949131</ArticleId><ArticleId IdType="doi">10.1371/journal.pone.0013197</ArticleId><ArticleId IdType="pmc">PMC2950840</ArticleId></ArticleIdList><ReferenceList><Reference><Citation>J Gen Virol. 2002 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