Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Profiling of RNAs downregulated by influenza A virus PA-X ribonuclease

ABSTRACT: Profiling of RNAs downregulated by influenza A virus PA-X ribonuclease

PROVIDER: PRJNA491905 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR7878050.fastq.gz	Fastqsanger.gz
	SRR7878060.fastq.gz	Fastqsanger.gz
	SRR7878070.fastq.gz	Fastqsanger.gz
	SRR7878051.fastq.gz	Fastqsanger.gz
	SRR7878061.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 26

Similar Datasets

Profiling of RNAs downregulated by influenza A virus PA-X ribonuclease

Project description:The goal of this analysis was to investigate the targets of the influenza A host shutoff ribonuclease PA-X. We profiled the relative levels of cellular RNAs in cells infected with influenza A virus (A/PuertoRico/8/1934 H1N1) comparing wild-type and mutants that make reduced levels of PA-X and/or make a truncated and inactive PA-X. We also profiled relative RNA levels in cells overexpressing wild-type PA-X or a catalytically inactive mutant (D108A).

2019-04-10 | GSE120183 | GEO

Transcriptome-wide identification of the influenza A virus endoribonuclease PA-X cut sites by 5' RACE-Seq

Project description:Influenza A virus induces host shutoff mainly through its endoribonuclease PA-X. Like many host shutoff nucleases, PA-X activity affects different host RNAs to varying degrees. To understand how PA-X discriminates between different mRNAs, we took a high-throughput approach to directly identify PA-X cut sites transcriptome-wide and examine PA-X cleavage characteristics. To do this, we compared RNA fragments from mock infected cells to cells infected with the wild-type (WT) A/PuertoRico/8/1934 H1N1 (PR8) influenza virus strain, or the same strain engineered to lack PA-X, referred to as PR8-PA(∆X).

2023-04-20 | GSE207253 | GEO

Identification of components in protein complex of influenza A virus PA protein

Project description:Influenza A virus is mainly transmitted through the respiratory route and can cause severe illness in humans. Proteins encoded by influenza A virus can interact with cellular factors and dysregulate host biological processes to facilitate viral replication and pathogenicity. The influenza viral PA protein is not only a subunit of influenza viral polymerase but also a virulence factor involved in pathogenicity during infection. To explore the role of the influenza virus PA protein in regulating host biological processes, we conducted immunoprecipitation and LC-MS/MS to globally identify cellular factors that interact with the PA proteins of the influenza A H1N1, 2009 pandemic H1N1, H3N2, and H7N9 viruses. The results demonstrated that proteins located in the mitochondrion, proteasome, and nucleus are associated with the PA protein. We further discovered that the PA protein is located in mitochondria by immunofluorescence and mitochondrial fractionation and that overexpression of the PA protein reduces mitochondrial respiration. In addition, our results revealed the interaction between PA and the mitochondrial matrix protein PYCR2 and the antiviral role of PYCR2 during influenza A virus replication. Moreover, we found that the PA protein could also trigger autophagy and disrupt mitochondrial homeostasis. Overall, our research revealed the impacts of the influenza A virus PA protein on mitochondrial function and autophagy.

2024-06-23 | PXD050585 | Pride

Ribonuclease L Targets Discrete Sites in Influenza Virus RNA

Project description:We used 2', 3'-cyclic phosphate cDNA synthesis and Illumina sequencing to identify and quantify ribonuclease L cleavage sites in host and viral RNAs.

2014-12-16 | GSE60581 | GEO

RNA-seq data of 293T cells trasfected with different viral PA-X proteins of influenza viruses

Project description:PA-X is a small accessory protein that modulates the virulence of various influenza A virus both in mammals and birds. However, the specific role of PA-X in the pathogenesis of highly pathogenic avian influenza virus (HPAIV) H7N9 subtype in mammals and avian species is largely unknown. By functional analysis, we want to investigate critical amino acids that contribute to the host shutoff ability of the PA-X protein of the H7N9 virus in 293T cells

2024-05-02 | GSE204790 | GEO

An anti-influenza A virus microbial metabolite acts by degrading viral endonuclease PA

Project description:The emergence of new highly pathogenic and drug-resistant influenza strains urges the development of novel therapeutics for influenza A virus (IAV). Here, we report the discovery of an anti-IAV microbial metabolite called APL-16-5 that was originally isolated from the plant endophytic fungus Aspergillus sp. CPCC 400735. APL-16-5 binds to both the E3 ligase TRIM25 and IAV polymerase subunit PA, leading to TRIM25 ubiquitination of PA and subsequent degradation of PA in the proteasome. This mode of action conforms to that of a proteolysis targeting chimera which employs the cellular ubiquitin-proteasome machinery to chemically induce the degradation of target proteins. Importantly, APL-16-5 potently inhibits IAV and protects mice from lethal IAV infection. Therefore, we have identified a natural microbial metabolite with potent in vivo anti-IAV activity and the potential of becoming a new IAV therapeutic. The antiviral mechanism of APL-16-5 opens the possibility of improving its anti-IAV potency and specificity by adjusting its affinity for TRIM25 and viral PA protein through medicinal chemistry.

2022-05-20 | PXD031993 | Pride

poly(A) specific ribonuclease (PARN)-dependent trimming of H ACA box RNAs

Project description:Microarray comprising probe sets for miRNAs and other small RNAs was used to determine which and how many small RNAs are potential substrates of poly(A) specific ribonuclease (PARN) in U2OS cells . Hybridization probes were generated by oligo(dT) priming.

2012-02-17 | E-MEXP-3344 | biostudies-arrayexpress

Anti-Influenza Activity of the Ribonuclease Binase in A549 cells

Project description:Ribonucleases (RNases) of different origin demonstrate antiviral effects that are mediated by the direct RNase action on RNA species and can also involve signal transduction modulation. To reveal cellular targets and explain the mechanisms underlying the antiviral effect employed by the small extra-cellular ribonuclease of Bacillus pumilus (binase) both in vitro and in vivo, a shotgun proteomic analysis of influenza A virus (H1N1pdm09)-infected A549 cells upon binase treatment, was performed.

2019-04-17 | PXD013540 | JPOST Repository

Effect of the ribonuclease binase on the proteome of A549 cell infected by influenza A(H1N1pdm09) virus

Project description:Ribonucleases (RNases) of different origin demonstrate antiviral effects that are mediated by the direct RNase action on RNA species and can also involve signal transduction modulation. To reveal cellular targets and explain the mechanisms underlying the antiviral effect employed by the small extracellular ribonuclease of Bacillus pumilus (binase) both in vitro and in vivo, a shotgun proteomic analysis of influenza A virus (H1N1pdm09)-infected A549 cells upon binase treatment, was performed.

2019-07-29 | PXD014809 | JPOST Repository

Effect of the ribonuclease binase on the proteome of A549 cell infected by influenza A(H1N1pdm09) virus

2019-04-18 | PXD013545 | JPOST Repository