Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

SARS-CoV-2 utilizes a multipronged strategy to suppress host protein synthesis

ABSTRACT: SARS-CoV-2 utilizes a multipronged strategy to suppress host protein synthesis

PROVIDER: PRJNA681523 | ENA |

REPOSITORIES: ENA

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	SRR13165879.fastq.gz	Fastqsanger.gz
	SRR13165880.fastq.gz	Fastqsanger.gz
	SRR13165881.fastq.gz	Fastqsanger.gz
	SRR13165882.fastq.gz	Fastqsanger.gz
	SRR13165883.fastq.gz	Fastqsanger.gz

Items per page:

1 - 5 of 54

Similar Datasets

SARS-CoV-2 utilizes a multipronged strategy to suppress host protein synthesis

Project description:Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is the cause of the ongoing coronavirus disease 19 (COVID-19) pandemic. Despite the urgent need, we still do not fully understand the molecular basis of SARS-CoV-2 pathogenesis and its ability to antagonize innate immune responses. Here, we use RNA-sequencing and ribosome profiling along SARS-CoV-2 infection and comprehensively define the mechanisms that are utilized by SARS-CoV-2 to shutoff cellular protein synthesis. We show SARS-CoV-2 infection leads to a global reduction in translation but that viral transcripts are not preferentially translated. Instead, we reveal that infection leads to accelerated degradation of cytosolic cellular mRNAs which facilitates viral takeover of the mRNA pool in infected cells. Moreover, we show that the translation of transcripts whose expression is induced in response to infection, including innate immune genes, is impaired, implying infection prevents newly transcribed cellular mRNAs from accessing the ribosomes. Overall, our results uncover the multipronged strategy employed by SARS-CoV-2 to commandeer the translation machinery and to suppress host defenses.

2021-04-01 | GSE162323 | GEO

ADAR1 utilizes independent mechanisms to suppress MDA5 and PKR activation by cellular double-stranded RNA

Project description:ADAR1 utilizes independent mechanisms to suppress MDA5 and PKR activation by cellular double-stranded RNA

| PRJNA814746 | ENA

mTORC1 couples cyst(e)ine availability with GPX4 protein synthesis and ferroptosis regulation

Project description:Glutathione peroxidase 4 (GPX4) utilizes glutathione (GSH) to detoxify lipid peroxidation and plays an essential role in inhibiting ferroptosis. As a selenoprotein, GPX4 protein synthesis is highly inefficient and energetically costly. How cells coordinate GPX4 synthesis with nutrient availability remains unclear. In this study, integrated proteomic and functional analyses reveal that SLC7A11-mediated cystine uptake promotes not only GSH synthesis but also GPX4 protein synthesis. Mechanistically, cyst(e)ine activates mechanistic/mammalian target of rapamycin complex 1 (mTORC1) and promotes GPX4 protein synthesis at least partly through the mTORC1-4E-BP signaling axis. Pharmacologic inhibition of mTORC1 decreases GPX4 protein levels, sensitizes cancer cells to ferroptosis, and synergizes with ferroptosis inducers (FINs) to suppress patient-derived xenograft tumor growth in vivo. Together, our results reveal a hitherto unrecognized regulatory mechanism to coordinate GPX4 protein synthesis with cyst(e)ine availability and suggest to use the combination of mTORC1 inhibitors and FINs in cancer treatment.

2020-08-25 | MSV000086009 | MassIVE

life strategy

Project description:life strategy

| PRJEB48189 | ENA

Oncogenic Herpesvirus utilizes stress-induced cell cycle checkpoints for efficient lytic replication.

Project description:ChIP-sequencing reads from Oncogenic Herpesvirus utilizes stress-induced cell cycle checkpoints for efficient lytic replication, accepted to PLOS Pathogens

2016-06-01 | E-MTAB-4356 | biostudies-arrayexpress

A Multipronged Unbiased Strategy Guides the Development of an anti-EGFR/EPHA2 Bispecific Antibody for Combination Cancer Therapy

Project description:A Multipronged Unbiased Strategy Guides the Development of an anti-EGFR/EPHA2 Bispecific Antibody for Combination Cancer Therapy

| PRJNA721399 | ENA

Bifidobacterium infantis utilizes N-acetylglucosamine nitrogen

Project description:15N-labeled N-acetylglucosamine (NAG) fed to B. infantis cells are incorporated into its proteome. This indicates that NAG, an amino sugar residue of human milk oligosaccharides (HMO) and other biopolymers, is used as a nitrogen source. Transcriptomics while subsisting on NAG nitrogen are consistent with the proteomics results. This further indicates that B. infantis utilizes NAG nitrogen in and shunts it towards a fundamental cellular processes.

2023-05-18 | PXD035809 | Pride

FBXO7 Ubiquitinates PRMT1 to Suppress Serine Synthesis and Tumor Growth in HCC

Project description:Cancer cells are often addicted to de novo serine synthesis to support their survival and rapid proliferation. However, how serine synthesis is regulated in cancer is not well understood. Our recent report demonstrated that protein arginine methyltransferase 1 (PRMT1) is upregulated in hepatocellular carcinoma (HCC) and methylates phosphoglycerate dehydrogenase (PHGDH, the first and rate-limiting enzyme in serine synthesis) at arginine 236, thereby activating PHGDH and promoting serine synthesis. Nevertheless, the mechanisms underlying upregulation of PRMT1 and regulation of PRMT1-PHGDH axis in HCC remain unknown. Here, using label-free quantitative proteomics analysis, we identified the potential interacting proteins of PRMT1.

2024-02-01 | PXD049069 |

FGFR3 alterations in bladder cancer stimulate serine synthesis to induce immune-inert macrophages that suppress T-cell recruitment and activation

Project description:FGFR3 alterations in bladder cancer stimulate serine synthesis to induce immune-inert macrophages that suppress T-cell recruitment and activation

| PRJNA1016348 | ENA

Oncogenic Herpesvirus utilizes stress-induced cell cycle checkpoints for efficient lytic replication.

Project description:Oncogenic Herpesvirus utilizes stress-induced cell cycle checkpoints for efficient lytic replication.

| PRJEB12546 | ENA