Browse
Submit Data
Databases
API
Help

Dataset Information

220 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

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

ABSTRACT: 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.

INSTRUMENT(S): ultraflex

ORGANISM(S): Homo Sapiens (human) Mycobacterium Tuberculosis

TISSUE(S): Cell Culture, Macrophage

SUBMITTER: He Xiang

LAB HEAD: Tao Shengce

PROVIDER: PXD006929 | 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

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

Project description: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.

2017-10-17 | PXD006927 | Pride

Soybean seed germination LC-MS/MS

Project description:This study aims at addressing soybean seeds (variety Absolute RR) germination, at 48h, during optimal and salt stressed condition when treated with bacterial signal compounds lipo-chitooligosaccharide (LCO) and thuricin 17 (Th17). Soybean growth is negatively affected when exposed to 40 mM NaCl and exposure to 80 mM NaCl is often lethal. When treated with the bacterial signal compounds lipo-chitooligosaccharide (LCO) and thuricin 17 (Th17), soybean seeds (variety Absolute RR) responded positively at salt stress of up to 150 mM NaCl. Shotgun proteomics of unstressed and 100 mM NaCl stressed seeds (48 h) in combination with the LCO and Th17 revealed many known, predicted, hypothetical and unknown proteins. In all, carbon, nitrogen and energy metabolic pathways were affected under both unstressed and salt stressed conditions when treated with signals. PEP carboxylase, Rubisco oxygenase large subunit, pyruvate kinase, and isocitrate lyase were some of the noteworthy proteins enhanced by the signals, along with antioxidant glutathione-S-transferase and other stress related proteins. These findings suggest that the germinating seeds alter their proteome based on bacterial signals and on stress, the specificity of this response plays a crucial role in organ maturation and transition from one stage to another in the plants life cycle; understanding this response is of fundamental importance in agriculture and, as a result, global food security.

2016-09-12 | PXD004106 | Pride

Arabidopsis rosettes proteome in response to LCO and Th17 under salt stress- LC-MS/MS

Project description:Lipo-chitooligosaccharide (LCO) and thuricin 17 (Th17) are two bacterial compounds that have been shown to positively influence plant growth of both legumes and non-legumes. Arabidopsis thaliana responded positively to treatment with the bacterial signal compounds LCO and Th17 in the presence of salt stress (up to 250 mM NaCl). Shotgun proteomics of unstressed and 250 mM NaCl stressed A. thaliana rosettes (7 days post stress) in combination with the LCO and Th17 revealed many known, putative, hypothetical and unknown proteins. Overall, carbon and energy metabolic pathways were affected under both unstressed and salt stressed conditions when treated with these signals. PEP carboxylase, Rubisco-oxygenase large subunit, pyruvate kinase, and proteins of photosystem I and II were some of the noteworthy proteins enhanced by the signals, along with other stress related proteins. These findings suggest that the proteome of A. thaliana rosettes is altered by the bacterial signals tested, and more so under salt stress, thereby imparting a positive effect on plant growth under high salt stress. The roles of the identified proteins are discussed here in relation to salt stress adaptation, which, when translated to field grown crops can be a crucial component and of significant importance in agriculture and global food production.

2016-09-29 | PXD004742 | Pride

DHX15 is involved in SUGP1-mediated RNA missplicing by mutant SF3B1 in cancer

Project description:HEK293T cells were transfected with the plasmid construct expressing FLAG-GST-tagged SUGP1 (aa 543-645), followed by two rounds of affinity purification using FLAG and GST tags. The purified proteins were resolved by SDS-PAGE, followed by staining with QC Colloidal Coomassie Stain (Bio-Rad). The relevant gel region (~85-100 KD) was excised, and the proteins in this gel section were identified by mass spectrometry.

2022-10-07 | MSV000090492 | MassIVE

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

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

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

Transcriptomic analysis of the RPS3-regulated genes in HCC cell line

Project description:The human ribosomal protein S3 (RPS3), a component of the small 40S ribosomal subunit, is mainly involved in ribosomal maturation and initiation of translation through association with initiation factors. In this study, we firstly identified that RPS3 played an important role in HCC progression. We performed RNA sequencing to profile gene expression patterns before and after RPS3 knockdown.

2019-02-01 | GSE118140 | 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