Nitazoxanide, an antiviral thiazolide, depletes ATP-sensitive intracellular Ca(2+) stores.
Identifieur interne : 000666 ( Ncbi/Merge ); précédent : 000665; suivant : 000667Nitazoxanide, an antiviral thiazolide, depletes ATP-sensitive intracellular Ca(2+) stores.
Auteurs : Omodele Ashiru [Royaume-Uni] ; Jonathon D. Howe [Royaume-Uni] ; Terry D. Butters [Royaume-Uni]Source :
- Virology [ 1096-0341 ] ; 2014.
Descripteurs français
- KwdFr :
- Adénosine triphosphate (métabolisme), Animaux, Antiviraux (métabolisme), Calcium (métabolisme), Cytoplasme (), Glycosylation (), Humains, Lignée cellulaire, Réplication virale (), Réticulum endoplasmique (), Thiazoles (métabolisme), Transport de protéines (), Virus de la diarrhée virale bovine de type 1 ().
- MESH :
English descriptors
- KwdEn :
- Adenosine Triphosphate (metabolism), Animals, Antiviral Agents (metabolism), Calcium (metabolism), Cell Line, Cytoplasm (chemistry), Cytoplasm (drug effects), Diarrhea Virus 1, Bovine Viral (drug effects), Endoplasmic Reticulum (drug effects), Glycosylation (drug effects), Humans, Protein Transport (drug effects), Thiazoles (metabolism), Virus Replication (drug effects).
- MESH :
- chemical , metabolism : Adenosine Triphosphate, Antiviral Agents, Calcium, Thiazoles.
- chemistry : Cytoplasm.
- drug effects : Cytoplasm, Diarrhea Virus 1, Bovine Viral, Endoplasmic Reticulum, Glycosylation, Protein Transport, Virus Replication.
- Animals, Cell Line, Humans.
Abstract
Nitazoxanide (NTZ) inhibits influenza, Japanese encephalitis, hepatitis B and hepatitis C virus replication but effects on the replication of other members of the Flaviviridae family has yet to be defined. The pestivirus bovine viral diarrhoea virus (BVDV) is a surrogate model for HCV infection and NTZ induced PKR and eIF2α phosphorylation in both uninfected and BVDV-infected cells. This led to the observation that NTZ depletes ATP-sensitive intracellular Ca(2+) stores. In addition to PKR and eIF2α phosphorylation, consequences of NTZ-mediated Ca(2+) mobilisation included induction of chronic sub-lethal ER stress as well as perturbation of viral protein N-linked glycosylation and trafficking. To adapt to NTZ-mediated ER stress, NTZ treated cells upregulated translation of Ca(2+)-binding proteins, including the ER chaperone Bip and the cytosolic pro-survival and anti-viral protein TCTP. Depletion of intracellular Ca(2+) stores is the primary consequence of NTZ treatment and is likely to underpin all antiviral mechanisms attributed to the thiazolide.
DOI: 10.1016/j.virol.2014.05.015
PubMed: 24971706
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pubmed:24971706Le document en format XML
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The pestivirus bovine viral diarrhoea virus (BVDV) is a surrogate model for HCV infection and NTZ induced PKR and eIF2α phosphorylation in both uninfected and BVDV-infected cells. This led to the observation that NTZ depletes ATP-sensitive intracellular Ca(2+) stores. In addition to PKR and eIF2α phosphorylation, consequences of NTZ-mediated Ca(2+) mobilisation included induction of chronic sub-lethal ER stress as well as perturbation of viral protein N-linked glycosylation and trafficking. To adapt to NTZ-mediated ER stress, NTZ treated cells upregulated translation of Ca(2+)-binding proteins, including the ER chaperone Bip and the cytosolic pro-survival and anti-viral protein TCTP. Depletion of intracellular Ca(2+) stores is the primary consequence of NTZ treatment and is likely to underpin all antiviral mechanisms attributed to the thiazolide. </div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">24971706</PMID><DateCompleted><Year>2014</Year><Month>09</Month><Day>29</Day></DateCompleted><DateRevised><Year>2016</Year><Month>11</Month><Day>25</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1096-0341</ISSN><JournalIssue CitedMedium="Internet"><Volume>462-463</Volume><PubDate><Year>2014</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Virology</Title><ISOAbbreviation>Virology</ISOAbbreviation></Journal><ArticleTitle>Nitazoxanide, an antiviral thiazolide, depletes ATP-sensitive intracellular Ca(2+) stores.</ArticleTitle><Pagination><MedlinePgn>135-48</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.virol.2014.05.015</ELocationID><ELocationID EIdType="pii" ValidYN="Y">S0042-6822(14)00229-3</ELocationID><Abstract><AbstractText>Nitazoxanide (NTZ) inhibits influenza, Japanese encephalitis, hepatitis B and hepatitis C virus replication but effects on the replication of other members of the Flaviviridae family has yet to be defined. The pestivirus bovine viral diarrhoea virus (BVDV) is a surrogate model for HCV infection and NTZ induced PKR and eIF2α phosphorylation in both uninfected and BVDV-infected cells. This led to the observation that NTZ depletes ATP-sensitive intracellular Ca(2+) stores. In addition to PKR and eIF2α phosphorylation, consequences of NTZ-mediated Ca(2+) mobilisation included induction of chronic sub-lethal ER stress as well as perturbation of viral protein N-linked glycosylation and trafficking. To adapt to NTZ-mediated ER stress, NTZ treated cells upregulated translation of Ca(2+)-binding proteins, including the ER chaperone Bip and the cytosolic pro-survival and anti-viral protein TCTP. Depletion of intracellular Ca(2+) stores is the primary consequence of NTZ treatment and is likely to underpin all antiviral mechanisms attributed to the thiazolide. </AbstractText><CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ashiru</LastName><ForeName>Omodele</ForeName><Initials>O</Initials><AffiliationInfo><Affiliation>Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK. Electronic address: Omodele.Ashiru@nibsc.org.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Howe</LastName><ForeName>Jonathon D</ForeName><Initials>JD</Initials><AffiliationInfo><Affiliation>Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK. Electronic address: jonathon.howe@bioch.ox.ac.uk.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Butters</LastName><ForeName>Terry D</ForeName><Initials>TD</Initials><AffiliationInfo><Affiliation>Oxford Glycobiology Institute, Department of Biochemistry, University of Oxford, South Parks Road, Oxford, Oxfordshire OX1 3QU, UK. Electronic address: terry.butters@bioch.ox.ac.uk.</Affiliation></AffiliationInfo></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>2014</Year><Month>06</Month><Day>25</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Virology</MedlineTA><NlmUniqueID>0110674</NlmUniqueID><ISSNLinking>0042-6822</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000998">Antiviral Agents</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D013844">Thiazoles</NameOfSubstance></Chemical><Chemical><RegistryNumber>8L70Q75FXE</RegistryNumber><NameOfSubstance UI="D000255">Adenosine 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MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002460" MajorTopicYN="N">Cell Line</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D003593" MajorTopicYN="N">Cytoplasm</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="Y">chemistry</QualifierName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D030241" MajorTopicYN="N">Diarrhea Virus 1, Bovine Viral</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004721" MajorTopicYN="N">Endoplasmic Reticulum</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006031" MajorTopicYN="N">Glycosylation</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013844" MajorTopicYN="N">Thiazoles</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014779" MajorTopicYN="N">Virus Replication</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">ER stress</Keyword><Keyword MajorTopicYN="N">Flaviviridae</Keyword><Keyword MajorTopicYN="N">Intracellular Ca(2+)</Keyword><Keyword MajorTopicYN="N">N-linked glycans</Keyword><Keyword MajorTopicYN="N">PKR</Keyword><Keyword MajorTopicYN="N">TCTP</Keyword></KeywordList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2014</Year><Month>02</Month><Day>27</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2014</Year><Month>04</Month><Day>01</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2014</Year><Month>05</Month><Day>14</Day></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2014</Year><Month>6</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2014</Year><Month>6</Month><Day>28</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2014</Year><Month>9</Month><Day>30</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">24971706</ArticleId><ArticleId IdType="pii">S0042-6822(14)00229-3</ArticleId><ArticleId 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Butters</name><name sortKey="Howe, Jonathon D" sort="Howe, Jonathon D" uniqKey="Howe J" first="Jonathon D" last="Howe">Jonathon D. Howe</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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