Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

EspB deletion mutant of Mycobacterium tuberculosis

ABSTRACT: The ESX-1, type VII, secretion system represents the major virulence determinant of Mycobacterium tuberculosis, one of the most successful intracellular pathogens. Here, by combining genetic and high-throughput approaches, we investigate the effect of espB on the secretion of ESX-1 components and other proetins, as well as virulence.

INSTRUMENT(S): Orbitrap Fusion Lumos

ORGANISM(S): Mycobacterium Tuberculosis H37rv

TISSUE(S): Cell Culture, Cell Line Cell

DISEASE(S): Pulmonary Tuberculosis

SUBMITTER: Andrej Benjak

LAB HEAD: Stewart Thomas Cole

PROVIDER: PXD011475 | Pride | 2021-09-24

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	CS_180308_Lumos_A.raw	Raw
	CS_180308_Lumos_B.raw	Raw
	CS_180308_Lumos_C.raw	Raw
	CS_180308_Lumos_D.raw	Raw
	CS_180308_Lumos_E.raw	Raw

Items per page:

1 - 5 of 16

Similar Datasets

espL deletion mutant of Mycobacterium tuberculosis

Project description:The ESX-1, type VII, secretion system represents the major virulence determinant of Mycobacterium tuberculosis, one of the most successful intracellular pathogens. Here, by combining genetic and high-throughput approaches, we show that EspL, a protein of 115 amino acids, is essential for mediating ESX-1-dependent virulence and for stabilization of EspE, EspF and EspH protein levels. Indeed, an espL knock-out mutant was unable to replicate intracellularly, secrete ESX-1 substrates or stimulate innate cytokine production. Moreover, proteomic studies detected greatly reduced amounts of EspE, EspF and EspH in the espL mutant as compared to the wild type strain, suggesting a role for EspL as a chaperone. The latter conclusion was further supported by discovering that EspL interacts with EspD, which was previously demonstrated to stabilize the ESX-1 substrates and effector proteins, EspA and EspC. Moreover, loss of EspL also leads to downregulation in M. tuberculosis of WhiB6, a redox-sensitive transcriptional activator of ESX-1 genes. Overall, our data highlight the importance of a so-far overlooked, though conserved, component of the ESX-1 secretion system and begin to delineate the role played by EspE, EspF and EspH in virulence and host-pathogen interaction.

2018-12-10 | PXD010929 | Pride

Mass-spectrometry-based analysis of the secretome of M. tuberculosis mutants

2018-12-10 | PXD011466 | Pride

Convergence of distinct RNA-silencing pathways on GW182/Tnrc6

Project description:The RNA-binding protein Trim71/Lin41 is a phylogenetically conserved developmental regulator that functions in mammalian stem cell reprogramming, brain development and cancer. Trim71 recognizes target mRNAs through hairpin motifs and silences them through molecular mechanisms that await identification. Deposited data are mass spectrometry data from immunoprecipitation experiments with endogenously tagged Trim71, Ago2, and Tnrc6a. Experiments are carried out in mouse embryonic stem cells (mESCs) and uncover reciprocal interactions of Trim71, Ago2, and Tnrc6a. Trim71 protein interactions are largely independent of Ago2 levels, but strongly depend on the presence of RNA. A second set of experiments is mass spectrometry data from immunoprecipitation experiments in mESCs overexpressing a tagged peptide derived from Homo sapiens TNRC6B (‘FLAG-HA::T6BWT::Cherry’), that is known to block the Tnrc6-Ago2 interaction. We show that a wild-type version strongly binds Ago1 and Ago2, but not Trim71, while a mutant version binds neither Ago1, 2, nor Trim71.

2023-07-04 | PXD034537 | Pride

Convergence of distinct RNA-silencing pathways on GW182/Tnrc6

2023-07-04 | PXD041242 | Pride

HDAC6 interacting proteins under different stresses

Project description:we treated MFE cell (WT and HDAC6 KO) with different stresses, incluing MG132, CytoD and IAV infection, then use home-made HDAC6 antibody to capture HDAC6 and coimmunoprecipitate its interacting proteins.

2023-10-17 | PXD038816 | Pride

The interactomes of Ubn1 and Ubn2 in mouse embryonic stem cells

Project description:Ubn1 and Ubn2 are essential subunits of the Histone Regulator A (HiRA) complex, the H3.3 histone variant chaperone for euchromatin. We pulled-down Ubn1 and Ubn2 with a C-terminal AVI-tag in mouse embryonic stem cells and identified, besides all known components of the complex, transcription factors that may play a role in the recruitment of HiRA to chromatin.

2021-07-14 | PXD025466 | Pride

DARPin F10 interactome with AP-MS

Project description:Identifying the HDAC6 targeting DARPin F10 interacting protein in human cells. Proteins are expressed as GFP fused protein and captured by GFP-trap beads. DARPin CTR is a control DARPin that binds to nothing.

2023-10-17 | PXD031799 | Pride

Proteome analysis of pig heart tissue to study the molecular consequences of hyperbaric oxygen treatment

Project description:The overall goal of the project was to confirm the presence of different energetic states of mitochondrial subpopulations depending on their subcellular localization within cardiomyocytes, i.e., subsarcolemmal (SSM) and interfibrillar mitochondria (IFM). Here we analysed proteomic changes upon treatment of pigs with hyperbaric oxygen.

2024-06-22 | PXD047678 | Pride

The interactome of Zbtb2 in mouse embryonic stem cells

Project description:Zbtb2 is a transcription factor that plays a role in mouse embryonic stem cell (mESC) differentiation. We pulled-down endogenously tagged Zbtb2-FLAG in mESCs and found a complex interactome. We characterized the Zbtb2 complex further by co-pull-downs of overexpressed Zbtb2-AVI, after mutation of individual Zbtb2 domains or of complex subunits, as well as by taking advantage of a tagged construct displaying dominant negative activity (Zbtb2-HAF).

2021-07-14 | PXD025520 | Pride

STIM1 Translocation to The Nucleus Protects Cells from DNA Damage

Project description:DNA damage represents a challenge for cells as this damage must be eliminated to preserve cell viability and the transmission of genetic information. To reduce or eliminate unscheduled chemical modifications in genomic DNA, an extensive signaling network, known as the DNA damage response (DDR) pathway, ensures this repair. In this work, and by means of a proteomic analysis aimed at the study of the STIM1 protein interactome, we have found that STIM1 is closely related to the protection from endogenous DNA damage, replicative stress, as well as in the response to interstrand crosslinks (ICLs). Here we show that STIM1 has a nuclear localization signal (NLS) that mediates its translocation to the nucleus, and that this translocation and the association of STIM1 to chromatin is enhanced in response to mitomycin C (MMC), an ICL-inducing agent. Consequently, STIM1-deficient cell lines show a higher level of basal DNA damage, replicative stress, and a higher sensitivity to MMC. We show that STIM1 normalizes FANCD2 protein levels in the nucleus, explaining the increased sensitivity to MMC in STIM1-KO cells. Our results show for the first time a nuclear function for the endoplasmic reticulum protein STIM1 and increase the number of genes involved in DNA repair.

2023-12-22 | PXD041181 | Pride

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

Tweets

OmicsDI Databases

PRIDE
PeptideAtlas
MassIVE
JPOST Repository
Physiome Model Repository

EGA
EVA
ENA
LINCS
PAXDB
Cell Collective

MetaboLights
Metabolomics Workbench
MetabolomeExpress
GNPS
BioModels
FAIRDOMHub

ArrayExpress
dbGaP
ExpressionAtlas
GEO
NODE

Information

Databases
Help
API
Contact us
Code on GitHub
Terms of use
Submit Data