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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pubmed:22659295Le document en format XML
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<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>
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<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>
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