Influenza A virus inhibits cytoplasmic stress granule formation.
Identifieur interne : 001309 ( Main/Exploration ); précédent : 001308; suivant : 001310Influenza A virus inhibits cytoplasmic stress granule formation.
Auteurs : Denys A. Khaperskyy [Canada] ; Todd F. Hatchette ; Craig MccormickSource :
- FASEB journal : official publication of the Federation of American Societies for Experimental Biology [ 1530-6860 ] ; 2012.
Descripteurs français
- KwdFr :
- Animaux, Cellules HeLa, Cytoplasme (métabolisme), Granulations cytoplasmiques (métabolisme), Humains, Interféron de type I (antagonistes et inhibiteurs), Protéines virales non structurales (génétique), Protéines virales non structurales (métabolisme), Réplication virale, Souris, Stress physiologique, Virus de la grippe A (génétique), Virus de la grippe A (métabolisme), eIF-2 Kinase (métabolisme).
- MESH :
- antagonistes et inhibiteurs : Interféron de type I.
- génétique : Protéines virales non structurales, Virus de la grippe A.
- métabolisme : Cytoplasme, Granulations cytoplasmiques, Protéines virales non structurales, Virus de la grippe A, eIF-2 Kinase.
- Animaux, Cellules HeLa, Humains, Réplication virale, Souris, Stress physiologique.
English descriptors
- KwdEn :
- Animals, Cytoplasm (metabolism), Cytoplasmic Granules (metabolism), HeLa Cells, Humans, Influenza A virus (genetics), Influenza A virus (metabolism), Interferon Type I (antagonists & inhibitors), Mice, Stress, Physiological, Viral Nonstructural Proteins (genetics), Viral Nonstructural Proteins (metabolism), Virus Replication, eIF-2 Kinase (metabolism).
- MESH :
- chemical , antagonists & inhibitors : Interferon Type I.
- genetics : Influenza A virus, Viral Nonstructural Proteins.
- metabolism : Cytoplasm, Cytoplasmic Granules, Influenza A virus, Viral Nonstructural Proteins, eIF-2 Kinase.
- Animals, HeLa Cells, Humans, Mice, Stress, Physiological, Virus Replication.
Abstract
An important component of the mammalian stress response is the reprogramming of translation. A variety of stresses trigger abrupt polysome disassembly and the accumulation of stalled translation preinitiation complexes. These complexes nucleate cytoplasmic stress granules (SGs), sites of mRNA triage in which mRNAs from disassembling polysomes are sorted and the fates of individual transcripts are determined. Here, we demonstrate that influenza A virus (IAV) actively suppresses SG formation during infection, thereby allowing translation of viral mRNAs. Complete inhibition of SG formation is dependent on the function of the viral nonstructural protein 1 (NS1); at late times postinfection, cells infected with NS1-mutant viruses formed SGs in a double-stranded RNA-activated protein kinase (PKR)-dependent fashion. In these cells, SG formation correlated with inhibited viral protein synthesis. Together, these experiments demonstrate the antiviral potential of SGs and reveal a viral countermeasure that limits SG formation.
DOI: 10.1096/fj.11-196915
PubMed: 22202676
Affiliations:
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Le document en format XML
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<front><div type="abstract" xml:lang="en">An important component of the mammalian stress response is the reprogramming of translation. A variety of stresses trigger abrupt polysome disassembly and the accumulation of stalled translation preinitiation complexes. These complexes nucleate cytoplasmic stress granules (SGs), sites of mRNA triage in which mRNAs from disassembling polysomes are sorted and the fates of individual transcripts are determined. Here, we demonstrate that influenza A virus (IAV) actively suppresses SG formation during infection, thereby allowing translation of viral mRNAs. Complete inhibition of SG formation is dependent on the function of the viral nonstructural protein 1 (NS1); at late times postinfection, cells infected with NS1-mutant viruses formed SGs in a double-stranded RNA-activated protein kinase (PKR)-dependent fashion. In these cells, SG formation correlated with inhibited viral protein synthesis. Together, these experiments demonstrate the antiviral potential of SGs and reveal a viral countermeasure that limits SG formation.</div>
</front>
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