Browse
Submit Data
Databases
API
Help

Dataset Information

306 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Enterococcus faecalis V583 - data analysis

ABSTRACT: Genome-scale models represent the link between an organism's genetic information and experimentally observable biological phenotypes. They facilitate metabolic engineering and the discovery of network properties such as the identification of novel drug targets. Most commonly, metabolite consumption data is used to limit the solution space, sometimes in combination with gene expression data. However, information about gene expression only poorly correlates with the abundance of the respective proteins within the cell. As such, we developed a method to map and integrate the whole-cell proteome into genome-scale models on the example of lactic acid bacteria (LAB). To the best of our knowledge, this work represents the first effort to integrate proteome data into genome-scale models on such a scale .

INSTRUMENT(S): TripleTOF 5600

ORGANISM(S): Enterococcus Faecalis (streptococcus Faecalis)

TISSUE(S): Cell Suspension Culture

SUBMITTER: Ben Collins

LAB HEAD: Ursula Kummer

PROVIDER: PXD002869 | Pride | 2016-12-06

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Enterococcus faecalis V583, Part 1

Project description:Genome-scale models represent the link between an organism's genetic information and experimentally observable biological phenotypes. They facilitate metabolic engineering and the discovery of network properties such as the identification of novel drug targets. Most commonly, metabolite consumption data is used to limit the solution space, sometimes in combination with gene expression data. However, information about gene expression only poorly correlates with the abundance of the respective proteins within the cell. As such, we developed a method to map and integrate the whole-cell proteome into genome-scale models on the example of lactic acid bacteria (LAB). To the best of our knowledge, this work represents the first effort to integrate proteome data into genome-scale models on such a scale.

2016-12-06 | PXD001576 | Pride

∆glnA Enterococcus faecalis V583 - data analysis

Project description:A group of gram positive bacteria that share the characteristic of fermenting hexose sugars to lactic acid are generally referred to as lactic acid bacteria (LAB). Enterococcus faecalis is one of the widely studied LABs due to a multiutude of reasons. On the one hand, it plays an important role in dairy industry, being for example a starter in cheese cultures. On the other hand, it accounts for a large part of the infections caused by the LABs in hospital environments. During the past few years, it developed resistance against most of the major antibiotics. Here, in an attempt to study its adaptive metabolism, a glutamine synthetase mutant (∆glnA) of E. faecalis was subjected to pH shift and the results from the integrative analysis of its metabolic network were compared to those of the wild type. The proteome data generated in this study were used to constrain the genome-scale metabolic network at two pH level, aiming to reduce the solution space and improve the accuracy of model simulation. This data particularly helped to come up with a new design for the amino acid transport system in the genome-scale model, resulting in an accurate reproduction of the metabolic behaviour of E. faecalis.

2022-01-14 | PXD030778 | Pride

A primary human T-cell spectral library to facilitate large scale quantitative T-cell proteomics

Project description:Comprehensive spectral libraries are essential in sequential window acquisition of all theoretical mass spectra (SWATH-MS) based high throughput proteomic studies. Even though SWATH-MS assays provide robust quantitative proteomics data its applications to human T-cell studies are limited by the lack of a human T-cell spectral library. To address this resource gap, we generated a high-quality spectral library containing data for 3,941 unique proteins from primary human T-cells across genetically unrelated donors. SWATH-MS analysis of 18 primary T-cell samples using the new human T-cell spectral library identified and quantified 3,022 proteins at 1% FDR, whereas the larger Pan-human spectral library identified and quantified 2,794 proteins, with only 34% overlap. Combining the two libraries resulted in 4,061 proteins, covering ~50% of proteins in immune-related pathways. Overall, this data suggests DDA-MS is suited to discovery projects through to its enhanced sensitivity and SWATH-MS is suited to high-throughput projects.

2020-10-19 | PXD019446 | Pride

DDA files of human cancer cells for the NCI-60 SWATH project PXD003539

Project description:This is the raw files for the DDA library used for intepreting the NCI-60 SWATH project PXD003539

2019-10-21 | PXD009597 | Pride

Dynamic of the Grb2 interactome in primary cells by DDA-MS

Project description:We applied AP-MS to quantify Grb2 interaction dynamics in primary T cells. Data generated here in shotgun/DDA mode were used to build a high quality Grb2 binders-specific SWATH assay library for high-throughput targeted analysis of DIA data.

2017-03-09 | PXD003973 | Pride

Comparative analysis of mRNA degradation and protein degradation in 68 pairs of adjacent prostate tissue samples indicates high stability of proteins

Project description:Here we investigated the degradation of mRNA and protein in 68 pairs of adjacent prostate tissue samples using RNA-seq and pressure cycling technology (PCT) coupled with SWATH mass spectrometry and developed a score, the Proteome Integrity Number (PIN), to quantify the extent of protein degradation in the samples.

2019-06-12 | PXD007841 | Pride

In vivo and in vitro proteome analysis of HIV-1 infected, human CD4+ T cells

Project description:Host directed therapies against HIV-1 are thought to be critical for long term containment of the HIV-1 pandemic but remain elusive. Since HIV-1 infects and manipulates important effectors of both the innate and adaptive immune system, identifying modulations of the host cell systems in humans during HIV-1 infection may be crucial for the development of immune based therapies. Here, we quantified the changes of the proteome in human CD4+ T cells upon HIV-1 infection, both in vitro and in vivo. A SWATH-MS approach was used to measure the proteome of human primary CD4+ T cells infected with HIV-1 in vitro as well as CD4+ T cells from HIV-1 infected patients with paired samples on and off antiretroviral treatment. In the in vitro experiment, the proteome of CD4+ T cells was quantified over a time course following HIV-1 infection. 1,725 host cell proteins and 4 HIV-1 proteins were quantified, with 145 proteins changing significantly during the time course. Changes in the proteome peaked 24 hours after infection, concomitantly with significant HIV-1 protein production. In the in vivo branch of the study, CD4+ T cells from viremic patients and those with no detectable viral load after treatment were sorted and the proteomes quantified. We consistently detected 895 proteins, 172 of which were considered to be significantly different between viraemic patients and patients undergoing successful treatment. The proteome of in vitro infected CD4+ T cells was modulated on multiple functional levels, including TLR-4 signalling and the type 1 interferon signalling pathway. Perturbations in the type 1 interferon signalling pathway were recapitulated in CD4+ T cells from patients. The study shows that proteome maps generated by SWATH-MS indicate a range of functionally significant changes in the proteome of HIV infected human CD4+ T cells. Exploring these perturbations in more detail may help identify new targets for immune based interventions.

2017-02-28 | PXD005234 | Pride

Inference and quantification of peptidoforms in large sample cohorts by SWATH-MS: Twin blood plasma quantitative variance components

Project description:This data set represents a reanalysis of human blood plasma samples measured by SWATH-MS of 36 pairs of monozygotic and 22 pairs of dizygotic twins that were sampled at two longitudinal time points (Liu et al., 2015, PMID:25652787). The data were used to determine the overall quantitative variability of 4322 peptidoforms in the sample cohort and to assign the measured variability to heritability, environmental or longitudinal effects.

2017-06-06 | PXD004574 | Pride

Inference and quantification of peptidoforms in large sample cohorts by SWATH-MS: PTM-SWATH-MS Gold Standard data set

Project description:The PTM-SWATH MS Gold Standard data set consists of a previously published (Soste et al., 2014, PMID:25194849) set of 579 unpurified, synthetic, heavy-isotope labeled phosphopeptides (Thermo Scientific Biopolymers). These phosphopeptides represent biologically relevant sequences from S. cerevisiae proteins, which have been found altered in their phosphorylation status under various conditions. The complete peptide set contains a mixture of singly and doubly phosphorylated sequences with in average more than 3 modifiable residues per peptide (serines, threonines or tyrosins, often in close proximity to each other). All peptides were mixed with equal volumes (concentrations are unknown due to the unpurified status of the peptides) and the resulting peptide mix was either analyzed directly in DDA mode for assay library generation or spiked into a human cell line background proteome in a 13-step dilution series and analyzed in SWATH mode for the generation of the SWATH Gold Standard data set.

2017-06-12 | PXD004573 | Pride

Yeast proteomic analysis upon temperature shift

Project description:DIA/SWATH analysis of yeast upon temperature shift.

2021-06-28 | PXD016320 | Pride