Browse
Submit Data
Databases
API
Help

Dataset Information

217 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Mtb BfrB interacted proteins - Systematic Identification of Mycobacterium tuberculosis Effectors Reveals that BfrB Suppresses Innate Immunity

ABSTRACT: To identify the protein interacted with Mtb BfrB, we performed the GST Pulldown assay followed by MS.We identified that Mtb BfrB interact with human RPS3.

INSTRUMENT(S): maXis

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture

SUBMITTER: He Xiang

LAB HEAD: He Xiang

PROVIDER: PXD006927 | Pride | 2017-10-17

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Publications

Systematic Identification of <i>Mycobacterium tuberculosis</i> Effectors Reveals that BfrB Suppresses Innate Immunity.

He Xiang X Jiang He-Wei HW Chen Hong H Zhang Hai-Nan HN Liu Yin Y Xu Zhao-Wei ZW Wu Fan-Lin FL Guo Shu-Juan SJ Hou Jing-Li JL Yang Ming-Kun MK Yan Wei W Deng Jiao-Yu JY Bi Li-Jun LJ Zhang Xian-En XE Tao Sheng-Ce SC

Molecular & cellular proteomics : MCP 20171010 12

<i>Mycobacterium tuberculosis</i> (Mtb) has evolved multiple strategies to counter the human immune system. The effectors of Mtb play important roles in the interactions with the host. However, because of the lack of highly efficient strategies, there are only a handful of known Mtb effectors, thus hampering our understanding of Mtb pathogenesis. In this study, we probed Mtb proteome microarray with biotinylated whole-cell lysates of human macrophages, identifying 26 Mtb membrane proteins and se ...[more]

PMID: 29018126

Similar Datasets

He Xiang - BfrB - Systematic Identification of Mycobacterium tuberculosis Effectors Reveals that BfrB Suppresses Innate Immunity

Project description:To identify the macrophage binding partner of Mtb BfrB, we selected and purified BfrB tagged with GST, and incubated it with THP-1 lysates before performing GST Pullodwn. Then the eluted protein were examined by sliver stain. Using mass spectrometry, we identified a protein with an apparent molecular mass of 28 KDa as RPS3, an essential subunit of NF-κB involved in the regulation of key genes in rapid cellular activation response.

2017-10-17 | PXD006929 | Pride

Proteome analysis of the M. tuberculosis Beijing B0/W148 cluster

Project description:The main project purpose is to investigate the fundamental physiological state of M. tuberculosis (MTB) during the infection and the mycobacterial response within the infected host tissue, human lung. High-throughput proteomic analysis of MTB cells will be involved to solve this problem. The description of pattern of proteins expressed in MTB cells extracted directly from clinical material of patients with tuberculosis defines the main novelty of the given project. Undoubtedly, the intermediate project results describing the features of MTB strains proteome in vitro will also be essential for the global scientific community.

2016-07-06 | PXD002542 | Pride

Comparison of gene expression in M. tuberculosis TrxB2-TetON-tetO-WT mutant treated or not with atc

Project description:M. tuberculosis thioredoxin reductase (TrxB2) is essential for Mtb physiology and pathogenesis. To gain insight into its biological functions, we generated the TrxB2-TetON-tetO mutants, in which TrxB2 is partially depleted in the absence of atc without impairing bacterial viability. We grew TrxB2-TetON-tetO-WT in 7H9 medium with 400 ng/ml atc, until the OD reached 0.5~0.6. Then Mtb was washed with 7H9 medium 3 times and suspended in 7H9 medium with or without atc. Then samples were taken 24, 48, 72 and 120 hrs later.

2016-05-12 | E-GEOD-72328 | biostudies-arrayexpress

Ribosomal protein S3: a functional component of NF-kB p65 binding complexes

Project description:To explore the effects on the NF-kB transcriptome after knockdown of RPS3 in stimulated T cells, we performed microarray assays comparing RPS3-silenced versus NS-treated samples on the same chip. p65-silenced versus NS-treated samples were used as a control. Keywords: time series design Jurkat cells transfected with control siRNA versus RPS3 or p65-siRNA were stimuated with TCR for 1, 3, or 6 hours for a total of 6 arrays.

2010-05-26 | E-GEOD-7231 | biostudies-arrayexpress

Genome-Wide Profiling of Peroxisome Proliferator-Activated Receptor M-NM-3 in Primary Epididymal, Inguinal, and Brown Adipocytes Reveals Depot-Selective Binding Correlated with Gene Expression

Project description:Here we have employed chromatin immunoprecipitation combined with deep sequencing to map and compare PPARM-NM-3 binding in in vitro differentiated primary mouse adipocytes isolated from epididymal, inguinal, and brown adipose tissues. While these PPARM-NM-3 binding profiles are overall similar, there are clear depot-selective binding sites. Most PPARM-NM-3 binding sites previously mapped in 3T3-L1 adipocytes can also be detected in primary adipocytes, but there are a large number of PPARM-NM-3 binding sites that are specific to the primary cells, and these tend to be located in closed chromatin regions in 3T3-L1 adipocytes. The depot-selective binding of PPARM-NM-3 is associated with highly depot-specific gene expression. This indicates that PPARM-NM-3 plays a role in the induction of genes characteristic of different adipocyte lineages and that preadipocytes from different depots are differentially preprogrammed to permit PPARM-NM-3 lineage-specific recruitment even when differentiated in vitro. Examination of PPARM-NM-3 binding in in vitro differentiatied adipocytes isolated from three different adipose depots.

2012-10-11 | E-GEOD-41481 | biostudies-arrayexpress

Ribosomal protein S3 regulates GLI2-mediated osteosarcoma invasion

Project description:It has been reported that GLI2 promotes proliferation, migration, and invasion of mesenchymal stem cell and osteosarcoma cells. To examine the molecular mechanisms of GLI2-mediated osteosarcoma metastasis, we performed a microarray analysis. The gene encoding ribosomal protein S3 (RPS3) was identified as a target of GLI2. Real-time PCR revealed that RPS3 was upregulated in osteosarcoma cell lines compared with normal osteoblast cells. Knockdown of GLI2 decreased RPS3 expression, whereas forced expression of a constitutively active form of GLI2 upregulated the expression of RPS3. RPS3 knockdown by siRNA decreased the migration and invasion of osteosarcoma cells. Although forced expression of constitutively active GLI2 increased the migration of human mesenchymal stem cells, knockdown of RPS3 reduced the up-regulated migration. In contrast, forced expression of RPS3 increased migration and invasion of osteosarcoma cells. Moreover, reduction of migration by GLI2 knockdown was rescued by forced expression of RPS3. Immunohistochemical analysis showed that RPS3 expression was increased in primary osteosarcoma lesions with lung metastases compared with those without. These findings indicate that GLI2–RPS3 signaling may be a marker of invasive osteosarcoma and a therapeutic target for patients with osteosarcoma.

2012-12-14 | GSE42903 | GEO

Mycobacterium tuberculosis gene expression in response to thioridazine (THZ)

Project description:The gene expression profiles of Mtb after treatment at the minimal inhibitory concentration (MIC) or 4 X MIC at an early stage (up to 6 hours) was compared to untreated Mtb. Our experiment is designed to in order to ensure that the primary effects (0-6h) of the drugs and any dose (1X MIC and 4X MIC) responses would be captured.

2010-05-16 | E-GEOD-16626 | biostudies-arrayexpress

Ribosomal protein S3 mediates drug resistance of proteasome inhibitor: therapeutic application in multiple myeloma

Project description:Multiple myeloma (MM) remains incurable due to drug resistance. Ribosomal protein S3 (RPS3) has been identified as a non-Rel subunit of NF-κB. However, the detailed biological roles of RPS3 remain unclear. Here, we report for the first time that RPS3 is necessary for MM survival and drug resistance. RPS3 was highly expressed in MM, and knockout of RPS3 in MM inhibited cell growth and induced cell apoptosis both in vitro and in vivo. Overexpression of RPS3 mediated the proteasome inhibitor resistance of MM and delayed the survival of MM tumour-bearing animals. Moreover, our present study found an interaction between RPS3 and the thyroid hormone receptor interactor 13 (TRIP13), an oncogene related to MM tumorigenesis and drug resistance. We demonstrated that the phosphorylation of RPS3 was mediated by TRIP13 via PKCδ, which played an important role in activating the canonical NF-κB signalling and inducing cell survival and drug resistance in MM. Notably, the inhibition of NF-κB signalling by the small-molecule inhibitor targeting TRIP13, DCZ0415, was capable of triggering synergistic cytotoxicity when combined with bortezomib in drug-resistant MM. This study identifies RPS3 as a novel biomarker and therapeutic target in MM.

2023-08-18 | GSE240978 | GEO

HEK293T cell proteome remodeling upon Torin1 treatment or amino acid withdraw in WT and RPS3-Halo knock-in cells with or without NUFIP1 deletion. Related to Supplementary Table 5 from An et al (2020)

Project description:HEK293T proteome (single shot) with knock-in or not for RPS3-Halo and Knock out or not for NUFIP1. Cells were treated or not with Torin1 or deprived of amino acids.

2020-04-30 | PXD017851 | Pride

Effect of RPS3 Serine 149 mutation on gene expression in hiPSC-derived cardiomyocytes during Ang II administration

Project description:Angiotensin II (Ang II) treatment contributes to hypertrophic growth and mitochondrial dysfunction in hiPSC-derived cardiomyocytes. Here, we report enhanced RPS3 phosphorylation at serine 149 in nuclear compartment and abnormal mitochondrial biogenesis during Ang II incubation. Furthermore, RPS3 S149 mutation attenuated Ang II induced cardiomyocyte hypertrophy and improved mitochondrial biogenesis and dysfunction. Mechanistically, RPS3 Ser149 mutation promoted mitochondrial RNA stabilization and blunt Ang II induced mitochodnrial RNA alternative splicing for degradation, by which RPS3 dephosphorylation restored mitochondrial complex assembly in cardiomyocytes.

2023-07-30 | GSE238123 | GEO

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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