StressCovidV1, Ncbi, Merge, bibRecord, 000227

The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.

Identifieur interne : 000227 ( Ncbi/Merge ); précédent : 000226; suivant : 000228

The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.

Auteurs : Alan G. Goodman [États-Unis] ; Jennifer A. Smith ; Siddharth Balachandran ; Olivia Perwitasari ; Sean C. Proll ; Matthew J. Thomas ; Marcus J. Korth ; Glen N. Barber ; Leslie A. Schiff ; Michael G. Katze

Source :

Journal of virology [ 0022-538X ] ; 2007.

RBID : pubmed:17166899

Descripteurs français

English descriptors

KwdEn :
- Animals, Base Sequence, Cells, Cultured, Eukaryotic Initiation Factor-2 (metabolism), HSP40 Heat-Shock Proteins (deficiency), HSP40 Heat-Shock Proteins (genetics), HSP40 Heat-Shock Proteins (metabolism), Mice, Mice, Knockout, Models, Biological, Orthomyxoviridae (genetics), Orthomyxoviridae (physiology), Phosphorylation, Protein Biosynthesis, RNA, Messenger (genetics), RNA, Messenger (metabolism), RNA, Viral (genetics), RNA, Viral (metabolism), Reoviridae (genetics), Reoviridae (physiology), Vesicular stomatitis Indiana virus (genetics), Vesicular stomatitis Indiana virus (physiology), Viral Proteins (biosynthesis), Virus Replication, eIF-2 Kinase (metabolism).
MESH :
- chemical , biosynthesis : Viral Proteins.
- chemical , deficiency : HSP40 Heat-Shock Proteins.
- chemical , genetics : HSP40 Heat-Shock Proteins, RNA, Messenger, RNA, Viral.
- chemical , metabolism : Eukaryotic Initiation Factor-2, HSP40 Heat-Shock Proteins, RNA, Messenger, RNA, Viral, eIF-2 Kinase.
- genetics : Orthomyxoviridae, Reoviridae, Vesicular stomatitis Indiana virus.
- physiology : Orthomyxoviridae, Reoviridae, Vesicular stomatitis Indiana virus.
- Animals, Base Sequence, Cells, Cultured, Mice, Mice, Knockout, Models, Biological, Phosphorylation, Protein Biosynthesis, Virus Replication.

Abstract

We previously hypothesized that efficient translation of influenza virus mRNA requires the recruitment of P58(IPK), the cellular inhibitor of PKR, an interferon-induced kinase that targets the eukaryotic translation initiation factor eIF2alpha. P58(IPK) also inhibits PERK, an eIF2alpha kinase that is localized in the endoplasmic reticulum (ER) and induced during ER stress. The ability of P58(IPK) to interact with and inhibit multiple eIF2alpha kinases suggests it is a critical regulator of both cellular and viral mRNA translation. In this study, we sought to definitively define the role of P58(IPK) during viral infection of mammalian cells. Using mouse embryo fibroblasts from P58(IPK-/-) mice, we demonstrated that the absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation. The absence of P58(IPK) also resulted in decreased vesicular stomatitis virus replication but enhanced reovirus yields. In cells lacking the P58(IPK) target, PKR, the trends were reversed-eIF2alpha phosphorylation was decreased, and influenza virus mRNA translation was increased. Although P58(IPK) also inhibits PERK, the presence or absence of this kinase had little effect on influenza virus mRNA translation, despite reduced levels of eIF2alpha phosphorylation in cells lacking PERK. Finally, we showed that influenza virus protein synthesis and viral mRNA levels decrease in cells that express a constitutively active, nonphosphorylatable eIF2alpha. Taken together, our results support a model in which P58(IPK) regulates influenza virus mRNA translation and infection through a PKR-mediated mechanism which is independent of PERK.

DOI: 10.1128/JVI.02151-06
PubMed: 17166899

Links toward previous steps (curation, corpus...)

to stream PubMed, to step Corpus: 000816
to stream PubMed, to step Curation: 000813
to stream PubMed, to step Checkpoint: 000769

Links to Exploration step

pubmed:17166899

Le document en format XML

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<front><div type="abstract" xml:lang="en">We previously hypothesized that efficient translation of influenza virus mRNA requires the recruitment of P58(IPK), the cellular inhibitor of PKR, an interferon-induced kinase that targets the eukaryotic translation initiation factor eIF2alpha. P58(IPK) also inhibits PERK, an eIF2alpha kinase that is localized in the endoplasmic reticulum (ER) and induced during ER stress. The ability of P58(IPK) to interact with and inhibit multiple eIF2alpha kinases suggests it is a critical regulator of both cellular and viral mRNA translation. In this study, we sought to definitively define the role of P58(IPK) during viral infection of mammalian cells. Using mouse embryo fibroblasts from P58(IPK-/-) mice, we demonstrated that the absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation. The absence of P58(IPK) also resulted in decreased vesicular stomatitis virus replication but enhanced reovirus yields. In cells lacking the P58(IPK) target, PKR, the trends were reversed-eIF2alpha phosphorylation was decreased, and influenza virus mRNA translation was increased. Although P58(IPK) also inhibits PERK, the presence or absence of this kinase had little effect on influenza virus mRNA translation, despite reduced levels of eIF2alpha phosphorylation in cells lacking PERK. Finally, we showed that influenza virus protein synthesis and viral mRNA levels decrease in cells that express a constitutively active, nonphosphorylatable eIF2alpha. Taken together, our results support a model in which P58(IPK) regulates influenza virus mRNA translation and infection through a PKR-mediated mechanism which is independent of PERK.</div>
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<Abstract><AbstractText>We previously hypothesized that efficient translation of influenza virus mRNA requires the recruitment of P58(IPK), the cellular inhibitor of PKR, an interferon-induced kinase that targets the eukaryotic translation initiation factor eIF2alpha. P58(IPK) also inhibits PERK, an eIF2alpha kinase that is localized in the endoplasmic reticulum (ER) and induced during ER stress. The ability of P58(IPK) to interact with and inhibit multiple eIF2alpha kinases suggests it is a critical regulator of both cellular and viral mRNA translation. In this study, we sought to definitively define the role of P58(IPK) during viral infection of mammalian cells. Using mouse embryo fibroblasts from P58(IPK-/-) mice, we demonstrated that the absence of P58(IPK) led to an increase in eIF2alpha phosphorylation and decreased influenza virus mRNA translation. The absence of P58(IPK) also resulted in decreased vesicular stomatitis virus replication but enhanced reovirus yields. In cells lacking the P58(IPK) target, PKR, the trends were reversed-eIF2alpha phosphorylation was decreased, and influenza virus mRNA translation was increased. Although P58(IPK) also inhibits PERK, the presence or absence of this kinase had little effect on influenza virus mRNA translation, despite reduced levels of eIF2alpha phosphorylation in cells lacking PERK. Finally, we showed that influenza virus protein synthesis and viral mRNA levels decrease in cells that express a constitutively active, nonphosphorylatable eIF2alpha. Taken together, our results support a model in which P58(IPK) regulates influenza virus mRNA translation and infection through a PKR-mediated mechanism which is independent of PERK.</AbstractText>
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The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.

The cellular protein P58IPK regulates influenza virus mRNA translation and replication through a PKR-mediated mechanism.

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