SrasV1, Ncbi, Merge, bibRecord, 002832

Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.

Identifieur interne : 002832 ( Ncbi/Merge ); précédent : 002831; suivant : 002833

Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.

Auteurs : Ying Sun [République populaire de Chine] ; Zidao Wang [République populaire de Chine] ; Jiali Tao [République populaire de Chine] ; Yi Wang [République populaire de Chine] ; Andong Wu [République populaire de Chine] ; Ziwen Yang [République populaire de Chine] ; Kaimei Wang [République populaire de Chine] ; Liqiao Shi [République populaire de Chine] ; Yu Chen [République populaire de Chine] ; Deyin Guo [République populaire de Chine]

Source :

Antiviral research [ 1872-9096 ] ; 2014.

RBID : pubmed:24530452

Descripteurs français

KwdFr :
- Activation enzymatique (), Antienzymes (pharmacologie), Antiviraux (pharmacologie), Coiffes des ARN (métabolisme), Concentration inhibitrice 50, Coronavirus (), Coronavirus (enzymologie), Guanine (métabolisme), Levures (), Levures (génétique), Levures (métabolisme), Methyltransferases (antagonistes et inhibiteurs), Produits biologiques (pharmacologie), Relation dose-effet des médicaments, Tests de criblage à haut débit, Virus du SRAS (), Virus du SRAS (enzymologie).
MESH :
- antagonistes et inhibiteurs : Methyltransferases.
- enzymologie : Coronavirus, Virus du SRAS.
- génétique : Levures.
- métabolisme : Coiffes des ARN, Guanine, Levures.
- pharmacologie : Antienzymes, Antiviraux, Produits biologiques.
- Activation enzymatique, Concentration inhibitrice 50, Coronavirus, Levures, Relation dose-effet des médicaments, Tests de criblage à haut débit, Virus du SRAS.

English descriptors

KwdEn :
- Antiviral Agents (pharmacology), Biological Products (pharmacology), Coronavirus (drug effects), Coronavirus (enzymology), Dose-Response Relationship, Drug, Enzyme Activation (drug effects), Enzyme Inhibitors (pharmacology), Guanine (metabolism), High-Throughput Screening Assays, Inhibitory Concentration 50, Methyltransferases (antagonists & inhibitors), RNA Caps (metabolism), SARS Virus (drug effects), SARS Virus (enzymology), Yeasts (drug effects), Yeasts (genetics), Yeasts (metabolism).
MESH :
- chemical , antagonists & inhibitors : Methyltransferases.
- chemical , metabolism : Guanine, RNA Caps.
- chemical , pharmacology : Antiviral Agents, Biological Products, Enzyme Inhibitors.
- drug effects : Coronavirus, Enzyme Activation, SARS Virus, Yeasts.
- enzymology : Coronavirus, SARS Virus.
- genetics : Yeasts.
- metabolism : Yeasts.
- Dose-Response Relationship, Drug, High-Throughput Screening Assays, Inhibitory Concentration 50.

Abstract

The 5'-cap structure is a distinct feature of eukaryotic mRNAs and is important for RNA stability and protein translation by providing a molecular signature for the distinction of self or non-self mRNA. Eukaryotic viruses generally modify the 5'-end of their RNAs to mimic the cellular mRNA structure, thereby facilitating viral replication in host cells. However, the molecular organization and biochemical mechanisms of the viral capping apparatus typically differ from its cellular counterpart, which makes viral capping enzymes attractive targets for drug discovery. Our previous work showed that SARS coronavirus (SARS-CoV) non-structural protein 14 represents a structurally novel and unique guanine-N7-methyltransferase (N7-MTase) that is able to functionally complement yeast cellular N7-MTase. In the present study, we developed a yeast-based system for identifying and screening inhibitors against coronavirus N7-MTase using both 96-well and 384-well microtiter plates. The MTase inhibitors previously identified by in vitro biochemical assays were tested, and some, such as sinefungin, effectively suppressed N7-MTase in the yeast system. However, other compounds, such as ATA and AdoHcy, did not exert an inhibitory effect within a cellular context. These results validated the yeast assay system for inhibitor screening yet also demonstrated the difference between cell-based and in vitro biochemical assays. The yeast system was applied to the screening of 3000 natural product extracts, and three were observed to more potently inhibit the activity of coronavirus than human N7-MTase.

DOI: 10.1016/j.antiviral.2014.02.002
PubMed: 24530452

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pubmed:24530452

Le document en format XML

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<front><div type="abstract" xml:lang="en">The 5'-cap structure is a distinct feature of eukaryotic mRNAs and is important for RNA stability and protein translation by providing a molecular signature for the distinction of self or non-self mRNA. Eukaryotic viruses generally modify the 5'-end of their RNAs to mimic the cellular mRNA structure, thereby facilitating viral replication in host cells. However, the molecular organization and biochemical mechanisms of the viral capping apparatus typically differ from its cellular counterpart, which makes viral capping enzymes attractive targets for drug discovery. Our previous work showed that SARS coronavirus (SARS-CoV) non-structural protein 14 represents a structurally novel and unique guanine-N7-methyltransferase (N7-MTase) that is able to functionally complement yeast cellular N7-MTase. In the present study, we developed a yeast-based system for identifying and screening inhibitors against coronavirus N7-MTase using both 96-well and 384-well microtiter plates. The MTase inhibitors previously identified by in vitro biochemical assays were tested, and some, such as sinefungin, effectively suppressed N7-MTase in the yeast system. However, other compounds, such as ATA and AdoHcy, did not exert an inhibitory effect within a cellular context. These results validated the yeast assay system for inhibitor screening yet also demonstrated the difference between cell-based and in vitro biochemical assays. The yeast system was applied to the screening of 3000 natural product extracts, and three were observed to more potently inhibit the activity of coronavirus than human N7-MTase. </div>
</front>
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<DateCompleted><Year>2014</Year>
<Month>11</Month>
<Day>04</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>04</Month>
<Day>04</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1872-9096</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>104</Volume>
<PubDate><Year>2014</Year>
<Month>Apr</Month>
</PubDate>
</JournalIssue>
<Title>Antiviral research</Title>
<ISOAbbreviation>Antiviral Res.</ISOAbbreviation>
</Journal>
<ArticleTitle>Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.</ArticleTitle>
<Pagination><MedlinePgn>156-64</MedlinePgn>
</Pagination>
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<ELocationID EIdType="pii" ValidYN="Y">S0166-3542(14)00036-9</ELocationID>
<Abstract><AbstractText>The 5'-cap structure is a distinct feature of eukaryotic mRNAs and is important for RNA stability and protein translation by providing a molecular signature for the distinction of self or non-self mRNA. Eukaryotic viruses generally modify the 5'-end of their RNAs to mimic the cellular mRNA structure, thereby facilitating viral replication in host cells. However, the molecular organization and biochemical mechanisms of the viral capping apparatus typically differ from its cellular counterpart, which makes viral capping enzymes attractive targets for drug discovery. Our previous work showed that SARS coronavirus (SARS-CoV) non-structural protein 14 represents a structurally novel and unique guanine-N7-methyltransferase (N7-MTase) that is able to functionally complement yeast cellular N7-MTase. In the present study, we developed a yeast-based system for identifying and screening inhibitors against coronavirus N7-MTase using both 96-well and 384-well microtiter plates. The MTase inhibitors previously identified by in vitro biochemical assays were tested, and some, such as sinefungin, effectively suppressed N7-MTase in the yeast system. However, other compounds, such as ATA and AdoHcy, did not exert an inhibitory effect within a cellular context. These results validated the yeast assay system for inhibitor screening yet also demonstrated the difference between cell-based and in vitro biochemical assays. The yeast system was applied to the screening of 3000 natural product extracts, and three were observed to more potently inhibit the activity of coronavirus than human N7-MTase. </AbstractText>
<CopyrightInformation>Copyright © 2014 Elsevier B.V. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Sun</LastName>
<ForeName>Ying</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Zidao</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Tao</LastName>
<ForeName>Jiali</ForeName>
<Initials>J</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Yi</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wu</LastName>
<ForeName>Andong</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Yang</LastName>
<ForeName>Ziwen</ForeName>
<Initials>Z</Initials>
<AffiliationInfo><Affiliation>Biological Pesticide Engineering Research Center, Hubei Academy of Agricultural Science, Hubei 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Wang</LastName>
<ForeName>Kaimei</ForeName>
<Initials>K</Initials>
<AffiliationInfo><Affiliation>Biological Pesticide Engineering Research Center, Hubei Academy of Agricultural Science, Hubei 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Shi</LastName>
<ForeName>Liqiao</ForeName>
<Initials>L</Initials>
<AffiliationInfo><Affiliation>Biological Pesticide Engineering Research Center, Hubei Academy of Agricultural Science, Hubei 430072, PR China.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Yu</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China. Electronic address: chenyu@whu.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Guo</LastName>
<ForeName>Deyin</ForeName>
<Initials>D</Initials>
<AffiliationInfo><Affiliation>State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072, PR China. Electronic address: dguo@whu.edu.cn.</Affiliation>
</AffiliationInfo>
</Author>
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<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<Month>02</Month>
<Day>11</Day>
</ArticleDate>
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<MedlineJournalInfo><Country>Netherlands</Country>
<MedlineTA>Antiviral Res</MedlineTA>
<NlmUniqueID>8109699</NlmUniqueID>
<ISSNLinking>0166-3542</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
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<MeshHeading><DescriptorName UI="D004305" MajorTopicYN="N">Dose-Response Relationship, Drug</DescriptorName>
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<MeshHeading><DescriptorName UI="D057166" MajorTopicYN="Y">High-Throughput Screening Assays</DescriptorName>
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<MeshHeading><DescriptorName UI="D020128" MajorTopicYN="N">Inhibitory Concentration 50</DescriptorName>
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<MeshHeading><DescriptorName UI="D008780" MajorTopicYN="N">Methyltransferases</DescriptorName>
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<MeshHeading><DescriptorName UI="D012315" MajorTopicYN="N">RNA Caps</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
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<QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName>
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<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
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<Keyword MajorTopicYN="N">N7-methyltransferase</Keyword>
<Keyword MajorTopicYN="N">Sinefungin</Keyword>
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Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Sante/explor/SrasV1/Data/Ncbi/Merge

HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 002832 | SxmlIndent | more

HfdSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd -nk 002832 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Sante
   |area=    SrasV1
   |flux=    Ncbi
   |étape=   Merge
   |type=    RBID
   |clé=     pubmed:24530452
   |texte=   Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Ncbi/Merge/RBID.i   -Sk "pubmed:24530452" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Ncbi/Merge/biblio.hfd   \
       | NlmPubMed2Wicri -a SrasV1

This area was generated with Dilib version V0.6.33.
Data generation: Tue Apr 28 14:49:16 2020. Site generation: Sat Mar 27 22:06:49 2021

	Serveur d'exploration SRAS
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Serveur d'exploration SRAS

Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.

Yeast-based assays for the high-throughput screening of inhibitors of coronavirus RNA cap guanine-N7-methyltransferase.

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Pour mettre un lien sur cette page dans le réseau Wicri

Pour générer des pages wiki