Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Francisella tularensis DsbA mutant MS/SILAC analysis

ABSTRACT: Comparison of enriched membrane fractions of Francisella tularensis subsp. holarctica strain FSC200 and its DsbA mutant by SILAC analysis.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Francisella Tularensis Subsp. Holarctica Fsc200

DISEASE(S): Tularemia

SUBMITTER: Jana Klimentova

LAB HEAD: Jiri Stulik

PROVIDER: PXD007682 | Pride | 2018-01-15

REPOSITORIES: pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	05222013_09_JK_MSSILAC_D1a.raw	Raw
	05222013_10_JK_MSSILAC_D2a.raw	Raw
	05222013_11_JK_MSSILAC_D3a.raw	Raw
	05222013_13_JK_MSSILAC_D1b.raw	Raw
	05222013_14_JK_MSSILAC_D2b.raw	Raw

Items per page:

1 - 5 of 30

Publications

The Multiple Localized Glyceraldehyde-3-Phosphate Dehydrogenase Contributes to the Attenuation of the Francisella tularensis dsbA Deletion Mutant.

Pavkova Ivona I Kopeckova Monika M Klimentova Jana J Schmidt Monika M Sheshko Valeria V Sobol Margarita M Zakova Jitka J Hozak Pavel P Stulik Jiri J

Frontiers in cellular and infection microbiology 20171211

The DsbA homolog of Francisella tularensis was previously demonstrated to be required for intracellular replication and animal death. Disruption of the dsbA gene leads to a pleiotropic phenotype that could indirectly affect a number of different cellular pathways. To reveal the broad effects of DsbA, we compared fractions enriched in membrane proteins of the wild-type FSC200 strain with the dsbA deletion strain using a SILAC-based quantitative proteomic analysis. This analys ...[more]

PMID: 29322032

Similar Datasets

Cross-species proteomic comparison of whole cell lysates, outer membrane vesicles and membrane fractions of Francisella tularensis subsp. tularensis versus subsp. holarctica

Project description:Secretion of outer membrane vesicles (OMV) presents an important phenomenon in Gram-negative bacteria and they play multiple roles in their lifestyle including virulence and host-pathogen interaction. Francisella tularensis secretes unusually shaped tubular OMV. We here present a proteomic comparison of whole cell lysates, OMV and membrane fractions derived from two F. tularensis strains: a moderately virulent subsp. holarctica strain FSC200 and highly virulent subsp. tularensis SchuS4 strain. We describe a novel approach to the cross-species proteomic comparison based on creating an intersection protein database from the individual single-species databases. This approach proved to be less prone to quantification errors arising from differences in the protein sequences than using the individual databases. The consecutive comparison of the subproteomes of OMV and membranes of the two strains allowed us to distinguish the differences in protein amounts caused by global expression changes from those caused by preferential protein packing to OMV or membrane. Amongst the most different proteins we detected proteins involved in the biosynthesis and metabolism of the bacterial envelope components like O-antigen, lipid A, phospholipids, and fatty acids, as well as some of the major structural outer membrane proteins.

2021-02-08 | PXD022406 | Pride

Identification of immunoreactive proteins in murine sera after immunization with outer membrane vesicles isolated from Francisella tularensis subsp. holarctica strain FSC200

2024-02-22 | PXD047830 | Pride

Proteomic characterization and label-free comparison of outer membrane vesicles from Francisella tularensis subsp. holarctica strain FSC200 isolated from different cultivation conditions

Project description:Francisella tularensis is a Gram-negative, facultative intracellular bacterium, causing a severe disease known as tularemia. It is known to secrete unusually shaped nanotubular outer membrane vesicles (OMV) loaded with number of virulence factors and immunoreactive proteins. In this study the nanotubes were purified from a clinical isolate of subsp. holarctica strain FSC200. We here provide a comprehensive proteomic characterization of OMV isolated from bacteria grown under different cultivation conditions simulating the diverse conditions of F. tularensis life cycle. These included conditions mimicking the environment inside the mammalian host during inflammation: oxidative stress, low pH and high temperature (42 °C); and by contrast, low temperature (25 °C) that mimicked the external milieu and agar plate cultivation. We observed several-fold increase in vesiculation rate at high temperature and low pH but the differences were not only in the amount of secreted OMV but particularly in their protein cargo. Amongst the proteins preferentially selectively packed into OMV under conditions mimicking mammalian host many were previously described as virulence factors connected to the unique intracellular trafficking of Francisella. Protein changes revealed also high probability of alterations of the bacterial surface on the level of lipopolysaccharide, polysaccharide capsule and phospholipids.

2019-09-30 | PXD013074 | Pride

Francisella tularensis subsp. holarctica FSC200

Project description:Francisella tularensis subsp. holarctica FSC200 hybrid sequencing

| PRJNA510899 | ENA

Gene expression data from F. tularensis-exposed neutrophils

Project description:We demonstrated recently that both constitutive and FAS-triggered apoptosis of human neutrophils are profoundly impaired by Francisella tularensis, but how this is achieved is largely unknown. To test the hypothesis that changes in neutrophil gene expression contribute to this phenotype, we used human oligonucleotide microarrays to identify differentially regulated genes in cells infected with F. tularensis strain LVS compared with uninfected controls. In order to examine the effect of F. tularensis on the neutrophil transcriptome, we performed microarray expression analysis on human neutrophils treated with F. tularensis subsp. holarctica live vaccine strain (LVS). Polymorphonuclear leukocytes (PMNs) were isolated from the blood of healthy donors. Control and F. tularensis-exposed PMNs were incubated at 37C for 0, 3, 6, 12, 24, and 48 hours.

2012-10-22 | E-GEOD-37416 | biostudies-arrayexpress

The identification of bacterial protein interaction partners pointed out to new intracellular functions of Francisella tularensis glyceraldehyde-3-phosphate dehydrogenase

Project description:Glyceraldehyde-3-phopshate dehydrogenase (GAPDH) is well-known for its involvement in numerous non-metabolic processes inside the mammalian cells. Alternative functions of prokaryotic GAPDH are mainly deduced from its extracellular localization and the ability to bind to selected host proteins. Data on its participation in intracellular bacterial processes are scarce as there is so far only one study dealing with this issue. We previously reported several evidence that the GAPDH homologue of Francisella tularensis, GapA, might also exert additional non-enzymatic functions. To follow up our former observation, here we decided to find out GapA’s interacting partners within the bacterial proteome to explore its new roles at the intracellular level. The quantitative proteomics approach based on stable isotope labelling of amino acids in cell culture (SILAC) in combination with affinity purification and mass spectrometry enabled us to identify 18 proteins potentially interacting with GapA, six of those interactions were further confirmed by alternative methods. Half of the identified proteins were involved in non-metabolic processes. Further analysis together with the quantitative label-free comparative analysis of proteomes isolated from the wild-type strain and strain with deleted gapA gene suggests that the GapA is implicated in DNA repair processes. The absence of GapA promotes secretion of its most potent interaction partner, the hypothetical protein with peptidase propeptide domain (PepSY) indicating its impact on subcellular distribution of some proteins.

2020-08-31 | PXD019739 | Pride

Phosphoproteome analysis of bone marrow-derived dendritic cells infected by Francisella tularensis

Project description:Francisella tularensis is a highly infective Gram-negative bacterium, also known as the causative agent of tularemia. The disease is characterized by the delayed onset of the adaptive immune response which provides time for the bacterial replication. As an intracellular pathogen, Francisella proliferates mainly in the cytosol of host phagocytes, which are linkers between the innate and the adaptive immunity. In particular, dendritic cells (DCs) are known to be the most effective antigen-presenting cells and thus they are crucial for the induction of the adaptive response. However, Francisella is able to invade and to proliferate inside DCs while avoiding their effective activation and maturation. The goal of this study was to map phosphoproteome changes in DCs infected by Francisella in order to reveal host signaling pathways involved in Francisella-DC interaction. The focus was laid on early intervals (<1 h p.i.) because of the ability of Francisella to escape in this time period from the phagosome to the cytosol where it establishes its replicative niche. For comparison, attenuated and in vivo-protective Francisella strain was used in parallel in experiments. DC phosphoproteome was analyzed by the means of shotgun LC-MS-based proteomics and relative changes were quantified by the stable isotope labeling method specially developed for primary bone marrow-derived DCs.

2017-10-26 | PXD005747 | Pride

Characterization of F. tularensis LVS outer membrane vesicles

Project description:Francisella tularensis is a Gram-negative bacteria responsible for tularemia, a disease for which the high prevalence of failure and relapses is a main concern. Directed evolution experiments carried out in presence of antibiotics revealed that acquisition of fluoroquinolones (FQ) resistance was not exclusively related to mutations in DNA gyrase genes which are the first targets of these molecules. Here, using F. tularensis LVS as model, we investigated the role of FupA/B (Fer-Utilization Protein), whose possible contribution to FQ resistance was suggested by genomic analysis of resistant isolates. Using trans-complementation/mutagenesis approaches we definitely connected FupA/B expression to FQ sensitivity. Furthermore, we showed that the virulent strain F. tularensis subsp. tularensis SCHU S4, lacking the homologous FupA protein, exhibited a lower FQ susceptibility. Importantly, the deletion of this lipoprotein promoted an increased secretion of outer membrane vesicles (OMVs). Mass spectrometry-based quantitative proteomic characterization of OMVs from LVS and LVS-∆fupA/B strains led to the identification of 801 proteins among which a subset of 23 proteins exhibited a differential abundance between OMVs from both strains and may therefore contribute to the observed increased FQ susceptibility. We finally demonstrated that OMVs are structural key elements of F. tularensis LVS biofilms providing protection against FQ. Taken together, these results showed that mutations targeting FupA/B contribute to antimicrobial resistance through quantitative and qualitative modulations of OMV biogenesis and biofilm formation, providing new basis for understanding and fighting against Francisella antibiotic resistance and/or persistence.

2019-11-12 | PXD010305 | Pride

Gene expression in F. tularensis subsp. tularensis SCHU P0, P5, and P9 strains.

Project description:The microarray analysis of Francisella tularensis subsp. tularensis strains SCHU P9 (virulent) and SCHU P0/P5 (attenuated) revealed significant differences in gene expression. The results showed that 19 genes were upregulated in the virulent SCHU P9 strain, while two genes, including ftt_0965c, were significantly downregulated

2024-12-31 | GSE274776 | GEO

Phosphoproteome analysis of bone marrow-derived dendritic cells infected by Francisella tularensis – proteome dataset

2017-10-26 | PXD006759 | Pride