MAVS-mediated apoptosis and its inhibition by viral proteins.
Identifieur interne : 001918 ( PubMed/Curation ); précédent : 001917; suivant : 001919MAVS-mediated apoptosis and its inhibition by viral proteins.
Auteurs : Yu Lei [États-Unis] ; Chris B. Moore ; Rachael M. Liesman ; Brian P. O'Connor ; Daniel T. Bergstralh ; Zhijian J. Chen ; Raymond J. Pickles ; Jenny P-Y TingSource :
- PloS one [ 1932-6203 ] ; 2009.
Descripteurs français
- KwdFr :
- Animaux, Apoptose (immunologie), Apoptose (physiologie), Caspases (métabolisme), Cellules cultivées, Facteur de transcription NF-kappa B (métabolisme), Facteur-3 de régulation d'interféron (antagonistes et inhibiteurs), Facteur-3 de régulation d'interféron (génétique), Humains, Interactions hôte-pathogène (immunologie), Interactions hôte-pathogène (physiologie), Interféron de type I (biosynthèse), Lignée cellulaire, Mitochondries (métabolisme), Modèles biologiques, Petit ARN interférent (génétique), Protéines adaptatrices de la transduction du signal (), Protéines adaptatrices de la transduction du signal (déficit), Protéines adaptatrices de la transduction du signal (génétique), Protéines adaptatrices de la transduction du signal (physiologie), Protéines virales (physiologie), Protéines virales non structurales (physiologie), RNA replicase (physiologie), Souris, Souris knockout, Structure tertiaire des protéines, Séquence nucléotidique, Virus Sendai (pathogénicité).
- MESH :
- antagonistes et inhibiteurs : Facteur-3 de régulation d'interféron.
- biosynthèse : Interféron de type I.
- déficit : Protéines adaptatrices de la transduction du signal.
- génétique : Facteur-3 de régulation d'interféron, Petit ARN interférent, Protéines adaptatrices de la transduction du signal.
- immunologie : Apoptose, Interactions hôte-pathogène.
- métabolisme : Caspases, Facteur de transcription NF-kappa B, Mitochondries.
- pathogénicité : Virus Sendai.
- physiologie : Apoptose, Interactions hôte-pathogène, Protéines adaptatrices de la transduction du signal, Protéines virales, Protéines virales non structurales, RNA replicase.
- Animaux, Cellules cultivées, Humains, Lignée cellulaire, Modèles biologiques, Protéines adaptatrices de la transduction du signal, Souris, Souris knockout, Structure tertiaire des protéines, Séquence nucléotidique.
English descriptors
- KwdEn :
- Adaptor Proteins, Signal Transducing (chemistry), Adaptor Proteins, Signal Transducing (deficiency), Adaptor Proteins, Signal Transducing (genetics), Adaptor Proteins, Signal Transducing (physiology), Animals, Apoptosis (immunology), Apoptosis (physiology), Base Sequence, Caspases (metabolism), Cell Line, Cells, Cultured, Host-Pathogen Interactions (immunology), Host-Pathogen Interactions (physiology), Humans, Interferon Regulatory Factor-3 (antagonists & inhibitors), Interferon Regulatory Factor-3 (genetics), Interferon Type I (biosynthesis), Mice, Mice, Knockout, Mitochondria (metabolism), Models, Biological, NF-kappa B (metabolism), Protein Structure, Tertiary, RNA Replicase (physiology), RNA, Small Interfering (genetics), Sendai virus (pathogenicity), Viral Nonstructural Proteins (physiology), Viral Proteins (physiology).
- MESH :
- chemical , antagonists & inhibitors : Interferon Regulatory Factor-3.
- chemical , biosynthesis : Interferon Type I.
- chemical , chemistry : Adaptor Proteins, Signal Transducing.
- chemical , deficiency : Adaptor Proteins, Signal Transducing.
- chemical , genetics : Adaptor Proteins, Signal Transducing, Interferon Regulatory Factor-3, RNA, Small Interfering.
- chemical , metabolism : Caspases, NF-kappa B.
- chemical , physiology : Adaptor Proteins, Signal Transducing, RNA Replicase, Viral Nonstructural Proteins, Viral Proteins.
- immunology : Apoptosis, Host-Pathogen Interactions.
- metabolism : Mitochondria.
- pathogenicity : Sendai virus.
- physiology : Apoptosis, Host-Pathogen Interactions.
- Animals, Base Sequence, Cell Line, Cells, Cultured, Humans, Mice, Mice, Knockout, Models, Biological, Protein Structure, Tertiary.
Abstract
Host responses to viral infection include both immune activation and programmed cell death. The mitochondrial antiviral signaling adaptor, MAVS (IPS-1, VISA or Cardif) is critical for host defenses to viral infection by inducing type-1 interferons (IFN-I), however its role in virus-induced apoptotic responses has not been elucidated.
DOI: 10.1371/journal.pone.0005466
PubMed: 19404494
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pubmed:19404494Le document en format XML
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<term>Adaptor Proteins, Signal Transducing (physiology)</term>
<term>Animals</term>
<term>Apoptosis (immunology)</term>
<term>Apoptosis (physiology)</term>
<term>Base Sequence</term>
<term>Caspases (metabolism)</term>
<term>Cell Line</term>
<term>Cells, Cultured</term>
<term>Host-Pathogen Interactions (immunology)</term>
<term>Host-Pathogen Interactions (physiology)</term>
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<term>Interferon Regulatory Factor-3 (genetics)</term>
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<term>Mice</term>
<term>Mice, Knockout</term>
<term>Mitochondria (metabolism)</term>
<term>Models, Biological</term>
<term>NF-kappa B (metabolism)</term>
<term>Protein Structure, Tertiary</term>
<term>RNA Replicase (physiology)</term>
<term>RNA, Small Interfering (genetics)</term>
<term>Sendai virus (pathogenicity)</term>
<term>Viral Nonstructural Proteins (physiology)</term>
<term>Viral Proteins (physiology)</term>
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<term>Interactions hôte-pathogène (physiologie)</term>
<term>Interféron de type I (biosynthèse)</term>
<term>Lignée cellulaire</term>
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<term>Modèles biologiques</term>
<term>Petit ARN interférent (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal ()</term>
<term>Protéines adaptatrices de la transduction du signal (déficit)</term>
<term>Protéines adaptatrices de la transduction du signal (génétique)</term>
<term>Protéines adaptatrices de la transduction du signal (physiologie)</term>
<term>Protéines virales (physiologie)</term>
<term>Protéines virales non structurales (physiologie)</term>
<term>RNA replicase (physiologie)</term>
<term>Souris</term>
<term>Souris knockout</term>
<term>Structure tertiaire des protéines</term>
<term>Séquence nucléotidique</term>
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<term>Interferon Regulatory Factor-3</term>
<term>RNA, Small Interfering</term>
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<term>Viral Proteins</term>
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<term>Petit ARN interférent</term>
<term>Protéines adaptatrices de la transduction du signal</term>
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<term>Interactions hôte-pathogène</term>
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<term>Host-Pathogen Interactions</term>
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<term>Mitochondries</term>
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<keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Apoptose</term>
<term>Interactions hôte-pathogène</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Protéines virales</term>
<term>Protéines virales non structurales</term>
<term>RNA replicase</term>
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<term>Host-Pathogen Interactions</term>
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<term>Base Sequence</term>
<term>Cell Line</term>
<term>Cells, Cultured</term>
<term>Humans</term>
<term>Mice</term>
<term>Mice, Knockout</term>
<term>Models, Biological</term>
<term>Protein Structure, Tertiary</term>
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<term>Cellules cultivées</term>
<term>Humains</term>
<term>Lignée cellulaire</term>
<term>Modèles biologiques</term>
<term>Protéines adaptatrices de la transduction du signal</term>
<term>Souris</term>
<term>Souris knockout</term>
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<front><div type="abstract" xml:lang="en">Host responses to viral infection include both immune activation and programmed cell death. The mitochondrial antiviral signaling adaptor, MAVS (IPS-1, VISA or Cardif) is critical for host defenses to viral infection by inducing type-1 interferons (IFN-I), however its role in virus-induced apoptotic responses has not been elucidated.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">19404494</PMID>
<DateCompleted><Year>2009</Year>
<Month>06</Month>
<Day>17</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>03</Month>
<Day>26</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1932-6203</ISSN>
<JournalIssue CitedMedium="Internet"><Volume>4</Volume>
<Issue>5</Issue>
<PubDate><Year>2009</Year>
</PubDate>
</JournalIssue>
<Title>PloS one</Title>
<ISOAbbreviation>PLoS ONE</ISOAbbreviation>
</Journal>
<ArticleTitle>MAVS-mediated apoptosis and its inhibition by viral proteins.</ArticleTitle>
<Pagination><MedlinePgn>e5466</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1371/journal.pone.0005466</ELocationID>
<Abstract><AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Host responses to viral infection include both immune activation and programmed cell death. The mitochondrial antiviral signaling adaptor, MAVS (IPS-1, VISA or Cardif) is critical for host defenses to viral infection by inducing type-1 interferons (IFN-I), however its role in virus-induced apoptotic responses has not been elucidated.</AbstractText>
<AbstractText Label="PRINCIPAL FINDINGS" NlmCategory="RESULTS">We show that MAVS causes apoptosis independent of its function in initiating IFN-I production. MAVS-induced cell death requires mitochondrial localization, is caspase dependent, and displays hallmarks of apoptosis. Furthermore, MAVS(-/-) fibroblasts are resistant to Sendai virus-induced apoptosis. A functional screen identifies the hepatitis C virus NS3/4A and the Severe Acute Respiratory Syndrome coronavirus (SARS-CoV) nonstructural protein (NSP15) as inhibitors of MAVS-induced apoptosis, possibly as a method of immune evasion.</AbstractText>
<AbstractText Label="SIGNIFICANCE" NlmCategory="CONCLUSIONS">This study describes a novel role for MAVS in controlling viral infections through the induction of apoptosis, and identifies viral proteins which inhibit this host response.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lei</LastName>
<ForeName>Yu</ForeName>
<Initials>Y</Initials>
<AffiliationInfo><Affiliation>Lineberger Comprehensive Cancer Center, University of North Carolina, Chapel Hill, North Carolina, USA.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Moore</LastName>
<ForeName>Chris B</ForeName>
<Initials>CB</Initials>
</Author>
<Author ValidYN="Y"><LastName>Liesman</LastName>
<ForeName>Rachael M</ForeName>
<Initials>RM</Initials>
</Author>
<Author ValidYN="Y"><LastName>O'Connor</LastName>
<ForeName>Brian P</ForeName>
<Initials>BP</Initials>
</Author>
<Author ValidYN="Y"><LastName>Bergstralh</LastName>
<ForeName>Daniel T</ForeName>
<Initials>DT</Initials>
</Author>
<Author ValidYN="Y"><LastName>Chen</LastName>
<ForeName>Zhijian J</ForeName>
<Initials>ZJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Pickles</LastName>
<ForeName>Raymond J</ForeName>
<Initials>RJ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Ting</LastName>
<ForeName>Jenny P-Y</ForeName>
<Initials>JP</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
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<ArticleDate DateType="Electronic"><Year>2009</Year>
<Month>03</Month>
<Day>07</Day>
</ArticleDate>
</Article>
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<MedlineTA>PLoS One</MedlineTA>
<NlmUniqueID>101285081</NlmUniqueID>
<ISSNLinking>1932-6203</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D048868">Adaptor Proteins, Signal Transducing</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C512612">IPS-1 protein, mouse</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C494232">IRF3 protein, human</NameOfSubstance>
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</Chemical>
<Chemical><RegistryNumber>EC 2.7.7.48</RegistryNumber>
<NameOfSubstance UI="D012324">RNA Replicase</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>EC 3.1.-</RegistryNumber>
<NameOfSubstance UI="C000657925">nidoviral uridylate-specific endoribonuclease</NameOfSubstance>
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<Chemical><RegistryNumber>EC 3.4.22.-</RegistryNumber>
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