Autophagy diminishes the early interferon-β response to influenza A virus resulting in differential expression of interferon-stimulated genes.
Identifieur interne : 000930 ( Ncbi/Merge ); précédent : 000929; suivant : 000931Autophagy diminishes the early interferon-β response to influenza A virus resulting in differential expression of interferon-stimulated genes.
Auteurs : Brieuc P. Perot [France] ; Jeremy Boussier [France] ; Nader Yatim [France] ; Jeremy S. Rossman [Royaume-Uni] ; Molly A. Ingersoll [France] ; Matthew L. Albert [France]Source :
- Cell death & disease [ 2041-4889 ] ; 2018.
Descripteurs français
- KwdFr :
- Animaux, Autophagosomes (immunologie), Infections à Orthomyxoviridae (anatomopathologie), Infections à Orthomyxoviridae (génétique), Infections à Orthomyxoviridae (immunologie), Interféron bêta (génétique), Interféron bêta (immunologie), Lignée cellulaire, Protéine-5 associée à l'autophagie (génétique), Protéine-5 associée à l'autophagie (immunologie), Régulation de l'expression des gènes (immunologie), Souris, Souris knockout, Virus de la grippe A (génétique), Virus de la grippe A (immunologie).
- MESH :
- anatomopathologie : Infections à Orthomyxoviridae.
- génétique : Infections à Orthomyxoviridae, Interféron bêta, Protéine-5 associée à l'autophagie, Virus de la grippe A.
- immunologie : Autophagosomes, Infections à Orthomyxoviridae, Interféron bêta, Protéine-5 associée à l'autophagie, Régulation de l'expression des gènes, Virus de la grippe A.
- Animaux, Lignée cellulaire, Souris, Souris knockout.
English descriptors
- KwdEn :
- Animals, Autophagosomes (immunology), Autophagy-Related Protein 5 (genetics), Autophagy-Related Protein 5 (immunology), Cell Line, Gene Expression Regulation (immunology), Influenza A virus (genetics), Influenza A virus (immunology), Interferon-beta (genetics), Interferon-beta (immunology), Mice, Mice, Knockout, Orthomyxoviridae Infections (genetics), Orthomyxoviridae Infections (immunology), Orthomyxoviridae Infections (pathology).
- MESH :
- chemical , genetics : Autophagy-Related Protein 5, Interferon-beta.
- genetics : Influenza A virus, Orthomyxoviridae Infections.
- immunology : Autophagosomes, Autophagy-Related Protein 5, Gene Expression Regulation, Influenza A virus, Interferon-beta, Orthomyxoviridae Infections.
- pathology : Orthomyxoviridae Infections.
- Animals, Cell Line, Mice, Mice, Knockout.
Abstract
Influenza A virus (IAV) infection perturbs metabolic pathways such as autophagy, a stress-induced catabolic pathway that crosstalks with cellular inflammatory responses. However, the impact of autophagy perturbation on IAV gene expression or host cell responses remains disputed. Discrepant results may be a reflection of in vivo studies using cell-specific autophagy-related (Atg) gene-deficient mouse strains, which do not delineate modification of developmental programmes from more proximal effects on inflammatory response. In vitro experiments can be confounded by gene expression divergence in wild-type cultivated cell lines, as compared to those experiencing long-term absence of autophagy. With the goal to investigate cellular processes within cells that are competent or incompetent for autophagy, we generated a novel experimental cell line in which autophagy can be restored by ATG5 protein stabilization in an otherwise Atg5-deficient background. We confirmed that IAV induced autophagosome formation and p62 accumulation in infected cells and demonstrated that perturbation of autophagy did not impact viral infection or replication in ATG5-stablized cells. Notably, the induction of interferon-stimulated genes (ISGs) by IAV was diminished when cells were autophagy competent. We further demonstrated that, in the absence of ATG5, IAV-induced interferon-β (IFN-β) expression was increased as compared to levels in autophagy-competent lines, a mechanism that was independent of IAV non-structural protein 1. In sum, we report that induction of autophagy by IAV infection reduces ISG expression in infected cells by limiting IFN-β expression, which may benefit viral replication and spread.
DOI: 10.1038/s41419-018-0546-5
PubMed: 29748576
Links toward previous steps (curation, corpus...)
- to stream PubMed, to step Corpus: 000268
- to stream PubMed, to step Curation: 000268
- to stream PubMed, to step Checkpoint: 000288
Links to Exploration step
pubmed:29748576Le document en format XML
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<term>Cell Line</term>
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<front><div type="abstract" xml:lang="en">Influenza A virus (IAV) infection perturbs metabolic pathways such as autophagy, a stress-induced catabolic pathway that crosstalks with cellular inflammatory responses. However, the impact of autophagy perturbation on IAV gene expression or host cell responses remains disputed. Discrepant results may be a reflection of in vivo studies using cell-specific autophagy-related (Atg) gene-deficient mouse strains, which do not delineate modification of developmental programmes from more proximal effects on inflammatory response. In vitro experiments can be confounded by gene expression divergence in wild-type cultivated cell lines, as compared to those experiencing long-term absence of autophagy. With the goal to investigate cellular processes within cells that are competent or incompetent for autophagy, we generated a novel experimental cell line in which autophagy can be restored by ATG5 protein stabilization in an otherwise Atg5-deficient background. We confirmed that IAV induced autophagosome formation and p62 accumulation in infected cells and demonstrated that perturbation of autophagy did not impact viral infection or replication in ATG5-stablized cells. Notably, the induction of interferon-stimulated genes (ISGs) by IAV was diminished when cells were autophagy competent. We further demonstrated that, in the absence of ATG5, IAV-induced interferon-β (IFN-β) expression was increased as compared to levels in autophagy-competent lines, a mechanism that was independent of IAV non-structural protein 1. In sum, we report that induction of autophagy by IAV infection reduces ISG expression in infected cells by limiting IFN-β expression, which may benefit viral replication and spread.</div>
</front>
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<Abstract><AbstractText>Influenza A virus (IAV) infection perturbs metabolic pathways such as autophagy, a stress-induced catabolic pathway that crosstalks with cellular inflammatory responses. However, the impact of autophagy perturbation on IAV gene expression or host cell responses remains disputed. Discrepant results may be a reflection of in vivo studies using cell-specific autophagy-related (Atg) gene-deficient mouse strains, which do not delineate modification of developmental programmes from more proximal effects on inflammatory response. In vitro experiments can be confounded by gene expression divergence in wild-type cultivated cell lines, as compared to those experiencing long-term absence of autophagy. With the goal to investigate cellular processes within cells that are competent or incompetent for autophagy, we generated a novel experimental cell line in which autophagy can be restored by ATG5 protein stabilization in an otherwise Atg5-deficient background. We confirmed that IAV induced autophagosome formation and p62 accumulation in infected cells and demonstrated that perturbation of autophagy did not impact viral infection or replication in ATG5-stablized cells. Notably, the induction of interferon-stimulated genes (ISGs) by IAV was diminished when cells were autophagy competent. We further demonstrated that, in the absence of ATG5, IAV-induced interferon-β (IFN-β) expression was increased as compared to levels in autophagy-competent lines, a mechanism that was independent of IAV non-structural protein 1. In sum, we report that induction of autophagy by IAV infection reduces ISG expression in infected cells by limiting IFN-β expression, which may benefit viral replication and spread.</AbstractText>
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<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Perot</LastName>
<ForeName>Brieuc P</ForeName>
<Initials>BP</Initials>
<AffiliationInfo><Affiliation>Unit of Dendritic Cell Immunobiology, Department of Immunology, Institut Pasteur, Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Inserm 1223, Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Ecole Doctorale Physiologie, Physiopathologie et Thérapeutique, Université Pierre et Marie Curie (Université Paris 6), Paris, France.</Affiliation>
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<AffiliationInfo><Affiliation>Inserm 1223, Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>International Group for Data Analysis, Institut Pasteur, Paris, France.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Ecole Doctorale Frontières du Vivant, Université Paris Diderot, Paris, France.</Affiliation>
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<AffiliationInfo><Affiliation>Inserm 1223, Paris, France.</Affiliation>
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<AffiliationInfo><Affiliation>Inserm 1223, Paris, France. molly.ingersoll@pasteur.fr.</Affiliation>
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<AffiliationInfo><Affiliation>Inserm 1223, Paris, France. albert.matthew@gene.com.</Affiliation>
</AffiliationInfo>
<AffiliationInfo><Affiliation>Department of Cancer Immunology, Genentech Inc., South San Francisco, CA, USA. albert.matthew@gene.com.</Affiliation>
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