Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Quantitative phosphoproteomic analysis of Streptococcus pneumoniae reveals that competence modulates protein phosphorylation

ABSTRACT: Extensive phosphoproteomic studies have revealed that protein phosphorylation on serine, threonine and tyrosine residues is a widespread regulatory post-translational modification in bacteria. In this study, we carried out a biological triplicate of quantitative proteomic and phosphoproteomic analyses on the pathogenic bacterium Streptococcus pneumoniae in the non-competent and the competent states. Competence is a developmental genetic program triggered by a signaling pathway that is key for natural genetic transformation and consequently bacterial horizontal gene transfer. We used dimethyl-tag labeling for the calculation of peptide abundance ratios between non-competent and competent samples, Titanium dioxide (TiO2) beads for phosphopeptide enrichment and LC-MS/MS determination. Our proteome covers 62.7% of the total protein content of the bacteria with 75 proteins having different abundance ratios, including proteins not previously described to be involved in competence. 103 phosphopeptides were identified including 48 having different abundance ratios. Notably, the proteins with a change in phosphorylation in competent cells are different from the proteins with a change in expression, highlighting different pathways induced by competence and regulated by phosphorylation. This is the first report that phosphorylation of some proteins is regulated during competence in Streptococcus pneumoniae, a key pathway for the bacteria to evade vaccines or acquire antibiotic resistance.

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Streptococcus Pneumoniae (ncbitaxon:1313)

SUBMITTER: Christophe Grangeasse

PROVIDER: MSV000094842 | MassIVE | Thu May 23 01:29:00 BST 2024

REPOSITORIES: MassIVE

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
		Other

Items per page:

1 - 1 of 1

Similar Datasets

Influenza A virus modulation of Streptococcus pneumoniae infection using ex vivo transcriptomics in a human primary lung epithelial cell

Project description:Deep sequencing of cDNA from Streptococcus pneumoniae EF3030 bacteria and normalized human broncial epithelial cells (nHBEC), alone, together, and after coincubation with Influenza A virus pH1N1.

2023-02-16 | GSE225108 | GEO

Santos2018 - Pneumococcal infection in alveoli

Project description:Multiscale mathematical model of pneumococcal alveolar infection. This model analyses the role of cellular and molecular interactions during the first 10 h after alveolar invasion of Streptococcus pneumoniae bacteria. By “multi-level” we mean that we simulated the interplay between different temporal and spatial scales in a single computational model. In this instance, we included the intracellular scale of processes driving lung epithelial cell activation together with the scale of cell-to-cell interactions between bacteria and alveolar macrophages at the alveolar tissue. The model combines agent-based modelling and ODE modelling strategies. The original article of the article can be found in https://doi.org/10.3389/fcimb.2018.00159.

2018-11-14 | MODEL1805170001 | BioModels

The five homologous CiaR-controlled sRNAs modulate Streptococcus pneumoniae Zn-resistance

Project description:Zn and Mn are essential micronutrients for many bacteria including Streptococcus pneumoniae. While Zn performs vital structural or catalytic roles in certain proteins, in excess, Zn can inhibit Mn uptake by S. pneumoniae and displace, but not functionally replace Mn from key enzymes including superoxide dismutase A (SodA). Here, we show that the Ccn small regulatory RNAs promote S. pneumoniae Mn uptake and resistance to the oxidative stress. Furthermore, we demonstrate that these small regulatory RNAs modulate the ability of S. pneumoniae to cause invasive pneumonia. Altogether, these findings reveal a new layer of regulation of S. pneumoniae Zn and Mn homeostasis and suggest that there are factors in addition to known transporters that modulate intracellular Mn levels.

2024-09-23 | GSE246655 | GEO

Streptococcus pneumoniae strain D39V were grown in six different conditions, mimicking the host niches

Project description:Streptococcus pneumoniae strain D39V were grown in six different conditions, mimicking the host niches

2021-12-14 | GSE128366 | GEO

Identification of KhpA/B-associated RNAs in Brucella suis by deep sequencing in Streptococcus pneumoniae

Project description:We report the identification of RNAs in Streptococcus pneumoniae D39 that are associated to the KhpA/B proteins

2018-02-14 | GSE103735 | GEO

A new structural paradigm in copper resistance in a human pathogen

Project description:Copper is essential for both innate and adaptive immune function and copper resistance has emerged as an important determinant of virulence of microbial pathogens. In the human pathogen Streptococcus pneumoniae (Spn), cytoplasmic copper resistance is mediated by an operon encoding the copper-responsive repressor CopY, CupA, of unknown function, and CopA, a copper effluxing P1B-type ATPase. We show that CupA is a novel cell membrane-anchored Cu(I) chaperone for CopA, and that a Cu(I)-binding competent, membrane-localized CupA, like CopA, is obligatory for copper resistance. Bacteria were grown statically in Brain Heart Infusion media (Bacto BHI, Becton Dickinson) at 37C in an atmosphere of 5% CO2 to a culture density of OD620~0.2 and were processed as described in the related Sample record. Strain IU1781 (D39 rpsL1) served as the reference for the strain comparison. The experiment was repeated one time, and results are consistent with those observed by Shafeeq et al (Mol Microbiol. 2011). Data normalization was performed using the BioArray Software Environment (BASE 1.2; Saal et al, Genome Biol. 2002) using the Lowess (subgrid) method. Median spot intensities were normalized without background subtraction and used to calculate expression ratios. The cut-off for statistical significance of differential expression was set at an average up or down fold change of at least 1.8 fold.

2013-05-24 | E-GEOD-39176 | biostudies-arrayexpress

Identification and Tetramer Structure of SPD_0310 Hemin-storage Protein Linked to Streptococcus pneumoniae Iron Homeostasis and Virulence

Project description:We found that the homologous proteins of SPD_0310 of Streptococcus pneumoniae widely exists in Gram-positive bacteria. SPD_0310 has heme binding ability. In the GST pull-down experiment, we found that it can interact with several proteins.

2022-08-12 | PXD030298 | Pride

Proteomic investigation into the action mechanism of inhibitor ptsc1 against Streptococcus pneumoniae

Project description:Phenyl-thiazolylurea-sulfonamides compound 1 (ptsc1) is a new and efficient bacterial inhibitor. Although the inhibitor has antibacterial activity against several model bacteria, the details of its mechanism in Streptococcus pneumoniae (S. pneumoniae) have not been revealed. In the current study, we found that ptsc1 can significantly inhibit the growth of S. pneumoniae. To further investigate the molecular mechanism of its antibacterial effects, quantitative proteomics was performed to identify differential expressed proteins in S. pneumoniae. Compared with the normal group, the expression levels of 38 proteins were upregulated, whereas those of 88 proteins were downregulated (> 1.3 fold-change) in the experimental group (P < 0.05). KEGG pathways analysis revealed that ptsc1 regulated proteins were mainly involved in carbohydrate metabolism, DNA replication and repair, pyrimidine metabolism, fatty acid biosynthesis and oxidative phosphorylation pathways. The results of GO enrichment analysis showed that the inhibitor could lead to dysregulation of bacterial translation and energy metabolism, and cause intracellular oxidative stress.

2022-01-12 | PXD030534 | Pride

Methionine starvation caused reprogrammed metabolism in Streptococcus pneumoniae

Project description:In our study, deletion of methionine synthesis gene metE (SPD_0510) impaired the growth of Streptococcus pneumoniae strain D39 significantly when bacteria were cultured in chemically defined medium with a low concentration of methionine. Bacteria undergo methionine starvation in this condition. We aimed to know how S. pneumoniae responses to methionine starvation, particularly at the transcriptional level. RNA-seq results show that 804 genes (41.2 % of whole genome) were differentially expressed under methionine starvation. Among them, 258 genes (32.1 %) are related to cell metabolism, with 75 genes involved in sugar and carbon metabolism, 88 genes for synthesis of metabolic products and 95 genes for uptake of amino acids and sugars. Combined with other experiments data, this showed the reprogrammed metabolism in S. pneumoniae under methionine starvation.

2022-04-01 | GSE184094 | GEO

Streptococcus pneumoniae and IAV co infection induces altered polyubiquitination in A549 cells

Project description:Epithelial cells are the first line of defense within the lung. Disruption of the epithelial barrier by pathogens enables the systematic dissemination of bacteria or viruses within the host, leading to severe diseases with fatal outcomes. Thus, the lung epithelium can be damaged by seasonal and pandemic influenza A viruses. Influenza A virus infection induced dysregulation of the immune system is beneficial for the dissemination of bacteria to the lower respiratory tract, causing bacterial and viral co-infection. Host cells regulate protein homeostasis and the response to different stimuli, for instance pathogen infections, by post translational modification of proteins. Aside from protein phosphorylation, ubiquitination of proteins is an essential regulatory tool in virtually every cellular process, such as protein homeostasis, the host immune response, cell morphology, and in clearing of cytosolic pathogens. Here, we analyzed the proteome and ubiquitinome of A549 cells in response to Streptococcus pneumoniae D39 Δcps and influenza A virus H1N1 as well as bacterial and viral co-infection. Pneumococcal infection induced alterations in the ubiquitination of proteins involved in the organization of the actin cytoskeleton and Rho GTPases, but had minor effects on the abundance of host proteins. H1N1 infection is reflected by an anti-viral state of A549 cells. Finally, co infection resembled the imprints of both infecting pathogens with a minor increase in the observed alterations in protein and ubiquitination abundance.

2022-02-24 | PXD028465 | 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