Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition.
Identifieur interne : 002590 ( PubMed/Checkpoint ); précédent : 002589; suivant : 002591Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition.
Auteurs : Yu-San Han [République populaire de Chine] ; Gu-Gang Chang ; Chiun-Gung Juo ; Hong-Jen Lee ; Shiou-Hwei Yeh ; John Tsu-An Hsu ; Xin ChenSource :
- Biochemistry [ 0006-2960 ] ; 2005.
Descripteurs français
- KwdFr :
- Catalyse, Cinétique, Concentration inhibitrice 50, Coronavirus bovin (enzymologie), Domaine catalytique, Données de séquences moléculaires, Hydrolyse, Inhibiteurs de la cystéine protéinase (pharmacologie), Inhibiteurs de la cystéine protéinase (synthèse chimique), Papaïne (antagonistes et inhibiteurs), Papaïne (biosynthèse), Papaïne (génétique), Papaïne (isolement et purification), Protéines virales (antagonistes et inhibiteurs), Protéines virales (biosynthèse), Protéines virales (génétique), Protéines virales (isolement et purification), Spécificité du substrat, Séquence d'acides aminés, Virus de l'hépatite murine (enzymologie), Virus du SRAS (enzymologie), Virus du SRAS (pathogénicité), Zinc (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Papaïne, Protéines virales.
- biosynthèse : Papaïne, Protéines virales.
- enzymologie : Coronavirus bovin, Virus de l'hépatite murine, Virus du SRAS.
- génétique : Papaïne, Protéines virales.
- isolement et purification : Papaïne, Protéines virales.
- pathogénicité : Virus du SRAS.
- pharmacologie : Inhibiteurs de la cystéine protéinase, Zinc.
- synthèse chimique : Inhibiteurs de la cystéine protéinase.
- Catalyse, Cinétique, Concentration inhibitrice 50, Domaine catalytique, Données de séquences moléculaires, Hydrolyse, Spécificité du substrat, Séquence d'acides aminés.
English descriptors
- KwdEn :
- Amino Acid Sequence, Catalysis, Catalytic Domain, Coronavirus, Bovine (enzymology), Cysteine Proteinase Inhibitors (chemical synthesis), Cysteine Proteinase Inhibitors (pharmacology), Hydrolysis, Inhibitory Concentration 50, Kinetics, Molecular Sequence Data, Murine hepatitis virus (enzymology), Papain (antagonists & inhibitors), Papain (biosynthesis), Papain (genetics), Papain (isolation & purification), SARS Virus (enzymology), SARS Virus (pathogenicity), Substrate Specificity, Viral Proteins (antagonists & inhibitors), Viral Proteins (biosynthesis), Viral Proteins (genetics), Viral Proteins (isolation & purification), Zinc (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Papain, Viral Proteins.
- chemical , biosynthesis : Papain, Viral Proteins.
- chemical , chemical synthesis : Cysteine Proteinase Inhibitors.
- enzymology : Coronavirus, Bovine, Murine hepatitis virus, SARS Virus.
- chemical , genetics : Papain, Viral Proteins.
- chemical , isolation & purification : Papain, Viral Proteins.
- pathogenicity : SARS Virus.
- chemical , pharmacology : Cysteine Proteinase Inhibitors, Zinc.
- Amino Acid Sequence, Catalysis, Catalytic Domain, Hydrolysis, Inhibitory Concentration 50, Kinetics, Molecular Sequence Data, Substrate Specificity.
Abstract
Viral proteases are essential for pathogenesis and virulence of severe acute respiratory syndrome coronavirus (SARS-CoV). Little information is available on SARS-CoV papain-like protease 2 (PLP2), and development of inhibitors against PLP2 is attractive for antiviral therapy. Here, we report the characterization of SARS-CoV PLP2 (from residues 1414 to 1858) purified from baculovirus-infected insect cells. We demonstrate that SARS-CoV PLP2 by itself differentially cleaves between the amino acids Gly180 and Ala181, Gly818 and Ala819, and Gly2740 and Lys2741 of the viral polypeptide pp1a, as determined by reversed-phase high-performance liquid chromatography analysis coupled with mass spectrometry. This protease is especially selective for the P1, P4, and P6 sites of the substrate. The study demonstrates, for the first time among coronaviral PLPs, that the reaction mechanism of SARS-CoV PLP2 is characteristic of papain and compatible with the involvement of the catalytic dyad (Cys)-S(-)/(His)-Im(+)H ion pair. With a fluorogenic inhibitor-screening platform, we show that zinc ion and its conjugates potently inhibit the enzymatic activity of SARS-CoV PLP2. In addition, we provided evidence for evolutionary reclassification of SARS-CoV. The results provide important insights into the biochemical properties of the coronaviral PLP family and a promising therapeutic way to fight SARS-CoV.
DOI: 10.1021/bi0504761
PubMed: 16042412
Affiliations:
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aminés</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Viral proteases are essential for pathogenesis and virulence of severe acute respiratory syndrome coronavirus (SARS-CoV). Little information is available on SARS-CoV papain-like protease 2 (PLP2), and development of inhibitors against PLP2 is attractive for antiviral therapy. Here, we report the characterization of SARS-CoV PLP2 (from residues 1414 to 1858) purified from baculovirus-infected insect cells. We demonstrate that SARS-CoV PLP2 by itself differentially cleaves between the amino acids Gly180 and Ala181, Gly818 and Ala819, and Gly2740 and Lys2741 of the viral polypeptide pp1a, as determined by reversed-phase high-performance liquid chromatography analysis coupled with mass spectrometry. This protease is especially selective for the P1, P4, and P6 sites of the substrate. The study demonstrates, for the first time among coronaviral PLPs, that the reaction mechanism of SARS-CoV PLP2 is characteristic of papain and compatible with the involvement of the catalytic dyad (Cys)-S(-)/(His)-Im(+)H ion pair. With a fluorogenic inhibitor-screening platform, we show that zinc ion and its conjugates potently inhibit the enzymatic activity of SARS-CoV PLP2. In addition, we provided evidence for evolutionary reclassification of SARS-CoV. The results provide important insights into the biochemical properties of the coronaviral PLP family and a promising therapeutic way to fight SARS-CoV.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">16042412</PMID><DateCompleted><Year>2005</Year><Month>11</Month><Day>07</Day></DateCompleted><DateRevised><Year>2020</Year><Month>03</Month><Day>25</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-2960</ISSN><JournalIssue CitedMedium="Print"><Volume>44</Volume><Issue>30</Issue><PubDate><Year>2005</Year><Month>Aug</Month><Day>02</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Papain-like protease 2 (PLP2) from severe acute respiratory syndrome coronavirus (SARS-CoV): expression, purification, characterization, and inhibition.</ArticleTitle><Pagination><MedlinePgn>10349-59</MedlinePgn></Pagination><Abstract><AbstractText>Viral proteases are essential for pathogenesis and virulence of severe acute respiratory syndrome coronavirus (SARS-CoV). Little information is available on SARS-CoV papain-like protease 2 (PLP2), and development of inhibitors against PLP2 is attractive for antiviral therapy. Here, we report the characterization of SARS-CoV PLP2 (from residues 1414 to 1858) purified from baculovirus-infected insect cells. We demonstrate that SARS-CoV PLP2 by itself differentially cleaves between the amino acids Gly180 and Ala181, Gly818 and Ala819, and Gly2740 and Lys2741 of the viral polypeptide pp1a, as determined by reversed-phase high-performance liquid chromatography analysis coupled with mass spectrometry. This protease is especially selective for the P1, P4, and P6 sites of the substrate. The study demonstrates, for the first time among coronaviral PLPs, that the reaction mechanism of SARS-CoV PLP2 is characteristic of papain and compatible with the involvement of the catalytic dyad (Cys)-S(-)/(His)-Im(+)H ion pair. With a fluorogenic inhibitor-screening platform, we show that zinc ion and its conjugates potently inhibit the enzymatic activity of SARS-CoV PLP2. In addition, we provided evidence for evolutionary reclassification of SARS-CoV. The results provide important insights into the biochemical properties of the coronaviral PLP family and a promising therapeutic way to fight SARS-CoV.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Han</LastName><ForeName>Yu-San</ForeName><Initials>YS</Initials><AffiliationInfo><Affiliation>Division of Biotechnology and Pharmaceutical Research, National Health Research Institutes, Miaoli County, Taiwan 350, Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chang</LastName><ForeName>Gu-Gang</ForeName><Initials>GG</Initials></Author><Author ValidYN="Y"><LastName>Juo</LastName><ForeName>Chiun-Gung</ForeName><Initials>CG</Initials></Author><Author ValidYN="Y"><LastName>Lee</LastName><ForeName>Hong-Jen</ForeName><Initials>HJ</Initials></Author><Author ValidYN="Y"><LastName>Yeh</LastName><ForeName>Shiou-Hwei</ForeName><Initials>SH</Initials></Author><Author ValidYN="Y"><LastName>Hsu</LastName><ForeName>John Tsu-An</ForeName><Initials>JT</Initials></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Xin</ForeName><Initials>X</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D003160">Comparative Study</PublicationType><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D015853">Cysteine Proteinase Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D014764">Viral Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="D010206">Papain</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.4.22.2</RegistryNumber><NameOfSubstance UI="C000657884">papain-like protease, Coronavirus</NameOfSubstance></Chemical><Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber><NameOfSubstance UI="D015032">Zinc</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002384" MajorTopicYN="N">Catalysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020134" MajorTopicYN="N">Catalytic Domain</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017938" MajorTopicYN="N">Coronavirus, Bovine</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015853" MajorTopicYN="N">Cysteine Proteinase Inhibitors</DescriptorName><QualifierName UI="Q000138" MajorTopicYN="N">chemical synthesis</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006868" MajorTopicYN="N">Hydrolysis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020128" MajorTopicYN="N">Inhibitory Concentration 50</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008969" MajorTopicYN="N">Molecular Sequence Data</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006517" MajorTopicYN="N">Murine hepatitis virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010206" MajorTopicYN="N">Papain</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D014764" MajorTopicYN="N">Viral Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000096" MajorTopicYN="N">biosynthesis</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000302" MajorTopicYN="Y">isolation & purification</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D015032" MajorTopicYN="N">Zinc</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2005</Year><Month>7</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2005</Year><Month>11</Month><Day>8</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2005</Year><Month>7</Month><Day>27</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">16042412</ArticleId><ArticleId IdType="doi">10.1021/bi0504761</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>République populaire de Chine</li></country></list><tree><noCountry><name sortKey="Chang, Gu Gang" sort="Chang, Gu Gang" uniqKey="Chang G" first="Gu-Gang" last="Chang">Gu-Gang Chang</name><name sortKey="Chen, Xin" sort="Chen, Xin" uniqKey="Chen X" first="Xin" last="Chen">Xin Chen</name><name sortKey="Hsu, John Tsu An" sort="Hsu, John Tsu An" uniqKey="Hsu J" first="John Tsu-An" last="Hsu">John Tsu-An Hsu</name><name sortKey="Juo, Chiun Gung" sort="Juo, Chiun Gung" uniqKey="Juo C" first="Chiun-Gung" last="Juo">Chiun-Gung Juo</name><name sortKey="Lee, Hong Jen" sort="Lee, Hong Jen" uniqKey="Lee H" first="Hong-Jen" last="Lee">Hong-Jen Lee</name><name sortKey="Yeh, Shiou Hwei" sort="Yeh, Shiou Hwei" uniqKey="Yeh S" first="Shiou-Hwei" last="Yeh">Shiou-Hwei Yeh</name></noCountry><country name="République populaire de Chine"><noRegion><name sortKey="Han, Yu San" sort="Han, Yu San" uniqKey="Han Y" first="Yu-San" last="Han">Yu-San Han</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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