Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex.
Identifieur interne : 001352 ( PubMed/Curation ); précédent : 001351; suivant : 001353Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex.
Auteurs : Min Ke [République populaire de Chine] ; Yu Chen ; Andong Wu ; Ying Sun ; Ceyang Su ; Hao Wu ; Xu Jin ; Jiali Tao ; Yi Wang ; Xiao Ma ; Ji-An Pan ; Deyin GuoSource :
- Virus research [ 1872-7492 ] ; 2012.
Descripteurs français
- KwdFr :
- Antienzymes (métabolisme), Cartographie d'interactions entre protéines, Conformation des protéines, Methyltransferases (antagonistes et inhibiteurs), Methyltransferases (métabolisme), Modèles moléculaires, Motifs et domaines d'intéraction protéique, Peptides (métabolisme), Protéines virales non structurales (antagonistes et inhibiteurs), Protéines virales non structurales (métabolisme), Techniques de double hybride, Virus du SRAS (enzymologie).
- MESH :
- antagonistes et inhibiteurs : Methyltransferases, Protéines virales non structurales.
- enzymologie : Virus du SRAS.
- métabolisme : Antienzymes, Methyltransferases, Peptides, Protéines virales non structurales.
- Cartographie d'interactions entre protéines, Conformation des protéines, Modèles moléculaires, Motifs et domaines d'intéraction protéique, Techniques de double hybride.
English descriptors
- KwdEn :
- Enzyme Inhibitors (metabolism), Methyltransferases (antagonists & inhibitors), Methyltransferases (metabolism), Models, Molecular, Peptides (metabolism), Protein Conformation, Protein Interaction Domains and Motifs, Protein Interaction Mapping, SARS Virus (enzymology), Two-Hybrid System Techniques, Viral Nonstructural Proteins (antagonists & inhibitors), Viral Nonstructural Proteins (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Methyltransferases, Viral Nonstructural Proteins.
- chemical , metabolism : Enzyme Inhibitors, Methyltransferases, Peptides, Viral Nonstructural Proteins.
- enzymology : SARS Virus.
- Models, Molecular, Protein Conformation, Protein Interaction Domains and Motifs, Protein Interaction Mapping, Two-Hybrid System Techniques.
Abstract
Coronaviruses are the etiological agents of respiratory and enteric diseases in humans and livestock, exemplified by the life-threatening severe acute respiratory syndrome (SARS) caused by SARS coronavirus (SARS-CoV). However, effective means for combating coronaviruses are still lacking. The interaction between nonstructural protein (nsp) 10 and nsp16 has been demonstrated and the crystal structure of SARS-CoV nsp16/10 complex has been revealed. As nsp10 acts as an essential trigger to activate the 2'-O-methyltransferase activity of nsp16, short peptides derived from nsp10 may have inhibitory effect on viral 2'-O-methyltransferase activity. In this study, we revealed that the domain of aa 65-107 of nsp10 was sufficient for its interaction with nsp16 and the region of aa 42-120 in nsp10, which is larger than the interaction domain, was needed for stimulating the nsp16 2'-O-methyltransferase activity. We further showed that two short peptides derived from the interaction domain of nsp10 could inhibit the 2'-O-methyltransferase activity of SARS-CoV nsp16/10 complex, thus providing a novel strategy and proof-of-principle study for developing peptide inhibitors against SARS-CoV.
DOI: 10.1016/j.virusres.2012.05.017
PubMed: 22659295
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wicri:level="1"><nlm:affiliation>State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, People's Republic of China.</nlm:affiliation><country xml:lang="fr">République populaire de Chine</country><wicri:regionArea>State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072</wicri:regionArea></affiliation></author><author><name sortKey="Chen, Yu" sort="Chen, Yu" uniqKey="Chen Y" first="Yu" last="Chen">Yu Chen</name></author><author><name sortKey="Wu, Andong" sort="Wu, Andong" uniqKey="Wu A" first="Andong" last="Wu">Andong Wu</name></author><author><name sortKey="Sun, Ying" sort="Sun, Ying" uniqKey="Sun Y" first="Ying" last="Sun">Ying Sun</name></author><author><name sortKey="Su, Ceyang" sort="Su, Ceyang" uniqKey="Su C" first="Ceyang" last="Su">Ceyang Su</name></author><author><name sortKey="Wu, Hao" sort="Wu, Hao" uniqKey="Wu H" first="Hao" 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Inhibitors (metabolism)</term><term>Methyltransferases (antagonists & inhibitors)</term><term>Methyltransferases (metabolism)</term><term>Models, Molecular</term><term>Peptides (metabolism)</term><term>Protein Conformation</term><term>Protein Interaction Domains and Motifs</term><term>Protein Interaction Mapping</term><term>SARS Virus (enzymology)</term><term>Two-Hybrid System Techniques</term><term>Viral Nonstructural Proteins (antagonists & inhibitors)</term><term>Viral Nonstructural Proteins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antienzymes (métabolisme)</term><term>Cartographie d'interactions entre protéines</term><term>Conformation des protéines</term><term>Methyltransferases (antagonistes et inhibiteurs)</term><term>Methyltransferases (métabolisme)</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Peptides (métabolisme)</term><term>Protéines virales non structurales (antagonistes et inhibiteurs)</term><term>Protéines virales non structurales (métabolisme)</term><term>Techniques de double hybride</term><term>Virus du SRAS (enzymologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Methyltransferases</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Enzyme Inhibitors</term><term>Methyltransferases</term><term>Peptides</term><term>Viral Nonstructural Proteins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Methyltransferases</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Virus du SRAS</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>SARS Virus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antienzymes</term><term>Methyltransferases</term><term>Peptides</term><term>Protéines virales non structurales</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Models, Molecular</term><term>Protein Conformation</term><term>Protein Interaction Domains and Motifs</term><term>Protein Interaction Mapping</term><term>Two-Hybrid System Techniques</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Cartographie d'interactions entre protéines</term><term>Conformation des protéines</term><term>Modèles moléculaires</term><term>Motifs et domaines d'intéraction protéique</term><term>Techniques de double hybride</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Coronaviruses are the etiological agents of respiratory and enteric diseases in humans and livestock, exemplified by the life-threatening severe acute respiratory syndrome (SARS) caused by SARS coronavirus (SARS-CoV). However, effective means for combating coronaviruses are still lacking. The interaction between nonstructural protein (nsp) 10 and nsp16 has been demonstrated and the crystal structure of SARS-CoV nsp16/10 complex has been revealed. As nsp10 acts as an essential trigger to activate the 2'-O-methyltransferase activity of nsp16, short peptides derived from nsp10 may have inhibitory effect on viral 2'-O-methyltransferase activity. In this study, we revealed that the domain of aa 65-107 of nsp10 was sufficient for its interaction with nsp16 and the region of aa 42-120 in nsp10, which is larger than the interaction domain, was needed for stimulating the nsp16 2'-O-methyltransferase activity. We further showed that two short peptides derived from the interaction domain of nsp10 could inhibit the 2'-O-methyltransferase activity of SARS-CoV nsp16/10 complex, thus providing a novel strategy and proof-of-principle study for developing peptide inhibitors against SARS-CoV.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">22659295</PMID><DateCompleted><Year>2012</Year><Month>11</Month><Day>08</Day></DateCompleted><DateRevised><Year>2020</Year><Month>04</Month><Day>07</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-7492</ISSN><JournalIssue CitedMedium="Internet"><Volume>167</Volume><Issue>2</Issue><PubDate><Year>2012</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Virus research</Title><ISOAbbreviation>Virus Res.</ISOAbbreviation></Journal><ArticleTitle>Short peptides derived from the interaction domain of SARS coronavirus nonstructural protein nsp10 can suppress the 2'-O-methyltransferase activity of nsp10/nsp16 complex.</ArticleTitle><Pagination><MedlinePgn>322-8</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virusres.2012.05.017</ELocationID><Abstract><AbstractText>Coronaviruses are the etiological agents of respiratory and enteric diseases in humans and livestock, exemplified by the life-threatening severe acute respiratory syndrome (SARS) caused by SARS coronavirus (SARS-CoV). However, effective means for combating coronaviruses are still lacking. The interaction between nonstructural protein (nsp) 10 and nsp16 has been demonstrated and the crystal structure of SARS-CoV nsp16/10 complex has been revealed. As nsp10 acts as an essential trigger to activate the 2'-O-methyltransferase activity of nsp16, short peptides derived from nsp10 may have inhibitory effect on viral 2'-O-methyltransferase activity. In this study, we revealed that the domain of aa 65-107 of nsp10 was sufficient for its interaction with nsp16 and the region of aa 42-120 in nsp10, which is larger than the interaction domain, was needed for stimulating the nsp16 2'-O-methyltransferase activity. We further showed that two short peptides derived from the interaction domain of nsp10 could inhibit the 2'-O-methyltransferase activity of SARS-CoV nsp16/10 complex, thus providing a novel strategy and proof-of-principle study for developing peptide inhibitors against SARS-CoV.</AbstractText><CopyrightInformation>Copyright © 2012 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ke</LastName><ForeName>Min</ForeName><Initials>M</Initials><AffiliationInfo><Affiliation>State Key Laboratory of Virology and Modern Virology Research Center, College of Life Sciences, Wuhan University, Wuhan 430072, People's Republic of China.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Chen</LastName><ForeName>Yu</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Andong</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Sun</LastName><ForeName>Ying</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Su</LastName><ForeName>Ceyang</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Wu</LastName><ForeName>Hao</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Jin</LastName><ForeName>Xu</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Tao</LastName><ForeName>Jiali</ForeName><Initials>J</Initials></Author><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>Yi</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Ma</LastName><ForeName>Xiao</ForeName><Initials>X</Initials></Author><Author ValidYN="Y"><LastName>Pan</LastName><ForeName>Ji-An</ForeName><Initials>JA</Initials></Author><Author ValidYN="Y"><LastName>Guo</LastName><ForeName>Deyin</ForeName><Initials>D</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>2012</Year><Month>05</Month><Day>29</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Virus Res</MedlineTA><NlmUniqueID>8410979</NlmUniqueID><ISSNLinking>0168-1702</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004791">Enzyme Inhibitors</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C558878">Nsp10 protein, SARS virus</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D010455">Peptides</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D017361">Viral Nonstructural Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="D008780">Methyltransferases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.1.1.-</RegistryNumber><NameOfSubstance UI="C558879">Nsp16 protein, SARS virus</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D004791" MajorTopicYN="N">Enzyme Inhibitors</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008958" MajorTopicYN="N">Models, Molecular</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010455" MajorTopicYN="N">Peptides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011487" MajorTopicYN="N">Protein Conformation</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054730" MajorTopicYN="N">Protein Interaction Domains and Motifs</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D025941" MajorTopicYN="Y">Protein Interaction Mapping</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D045473" MajorTopicYN="N">SARS Virus</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D020798" MajorTopicYN="N">Two-Hybrid System Techniques</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017361" MajorTopicYN="N">Viral Nonstructural Proteins</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="N">antagonists & inhibitors</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2012</Year><Month>04</Month><Day>02</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2012</Year><Month>05</Month><Day>20</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2012</Year><Month>05</Month><Day>22</Day></PubMedPubDate><PubMedPubDate 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