Browse
Submit Data
Databases
API
Help

Dataset Information

226 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

A proteomic analysis of the surface attachment in Pseudomonas aeruginosa early as 20 minutes incubation.

ABSTRACT: The goal of the project is the study of molecular events occurring during the attachment phase, first step of the biofilms formation. Thanks to an original growth system developed in our laboratory, we were able to compare, for the first time, the protein content of P. aeruginosa immobilized for 20 minutes only to that of their planktonic counterparts.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Pseudomonas Aeruginosa Pao1

TISSUE(S): Cell Suspension Culture, Biofilm

SUBMITTER: Stephane Claverol

LAB HEAD: Marc Bonneu

PROVIDER: PXD002942 | Pride | 2017-07-11

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	sv140708_FT1.msf	Msf
	sv140708_FT1_01.raw	Raw
	sv140708_FT1_02.raw	Raw
	sv140708_FT1_03c.raw	Raw
	sv140708_FT1_04b.raw	Raw

Items per page:

1 - 5 of 30

Publications

Pseudomonas aeruginosa cells attached to a surface display a typical proteome early as 20 minutes of incubation.

Crouzet Marc M Claverol Stéphane S Lomenech Anne-Marie AM Le Sénéchal Caroline C Costaglioli Patricia P Barthe Christophe C Garbay Bertrand B Bonneu Marc M Vilain Sébastien S

PloS one 20170705 7

Biofilms are present in all environments and often result in negative effects due to properties of the biofilm lifestyle and especially antibiotics resistance. Biofilms are associated with chronic infections. Controlling bacterial attachment, the first step of biofilm formation, is crucial for fighting against biofilm and subsequently preventing the persistence of infection. Thus deciphering the underlying molecular mechanisms involved in attachment could allow discovering molecular targets from ...[more]

PMID: 28678862

Similar Datasets

Proteomic study of low-birth-weight nephropathy molecular pathogenesis in rats

Project description:We investigated the molecular pathogenesis of LBW rats obtained by intraperitoneal injection of dexamethasone into pregnant animals. Normal-birth-weight (NBW) rats were used as controls with seven animals per group. When the rats were four weeks old, the left kidneys were removed and used for comprehensive label-free proteomic studies

2022-02-15 | PXD018948 | Pride

Label-free proteomics of immuno-purified SYP61-trans-Golgi Network compartment in control condition and upon sphingolipid acyl-chain length reduction by metazachlor.

Project description:The trans-Golgi Network (TGN) in plants is a main sorting hub for proteins and lipids. The lipid composition at the TGN is instrumental to the polar sorting of the auxin efflux carrier PIN2 from TGN to the apical membrane. Here, we immuno-purified the full and intact TGN using the TGN-resident syntaxin SYP61 to identify and quantify TGN-proteins which abundance at TGN is dependent on the acyl-chain length of very-long chain fatty acids-containing lipids such as sphingolipids.

2021-12-01 | PXD026252 | Pride

Critical role of Aquaporin-1 and telocytes in infantile hemangioma response to propranolol beta-blockade

Project description:Propranolol, a non-selective β-adrenergic receptor (ADRB) antagonist, is the first-line therapy for severe infantile hemangiomas (IH). Since the incidental discovery of propranolol efficacy in IH, preclinical and clinical investigations have shown evidence of adjuvant propranolol response in some malignant tumors. However, the mechanism for propranolol antitumor effect is still largely unknown, owing to the absence of a tumor model responsive to propranolol at non-toxic concentrations. Immunodeficient mice engrafted with different human tumor cell lines were treated with anti-VEGF bevacizumab, to create a model sensitive to propranolol. Proteomics analysis was used to reveal propranolol-mediated protein alteration correlating with tumor growth inhibition and Aquaporin-1 (AQP1), a water channel modulated in tumor cell migration and invasion, was identified. IH tissues and cells were then functionally investigated. Our functional protein association networks analysis and knockdown of ADRB2 and AQP1 indicated that propranolol treatment and AQP1 downregulation trigger the same pathway, suggesting that AQP1 is a major driver of betablockers antitumor response. Examining AQP1 in human hemangioma samples, we found it exclusively in a perivascular layer, so far unrecognized in IH, made of telocytes (TC). Functional in vitro studies showed that AQP1-positive telocytes play a critical role in IH response to propranolol and that modulation of AQP1 in IH-TC by propranolol or shAQP1 decreases capillary-like tube formation in a Matrigel based angiogenesis assay. We conclude that IH sensitivity to propranolol may rely at least in part to a cross talk between lesional vascular cells and stromal telocytes.

2021-01-25 | PXD021457 | Pride

Proteome of mouse striatal dopamine synaptosomes purified by fluorescence sorting

Project description:Dopamine transmission is a monoaminergic system involved in reward processing and motor control. Volume transmission is thought to be the main mechanism by which monoamines modulate effector transmission though synaptic structures are scarcely described. In the present work we aimed to unravel the cellular and molecular synaptome of single projection pathways (Zhu F, Cizeron M, Qiu Z, Benavides-Piccione R, Kopanitsa MV, Skene NG, Koniaris B, DeFelipe J, Fransén E, Komiyama NH & Grant SGN (2018) Architecture of the Mouse Brain Synaptome. Neuron 99: 781–799.e10). To that end, we established a workflow combining fluorescence tracing of the dopaminergic pathway, fluorescence activated synaptosome sorting and mass spectrometry-based proteomics. With this approach we provide the first ex-vivo model to thoroughly analyse the cellular and molecular organisation of dopaminergic synapses from mouse striatum.

2022-06-09 | PXD027534 | Pride

Proteomic analysis of the entorhinal cortex and CA1 subfields of the hippocampus of macaques injected with tau seeds from Alzheimer’s brain

Project description:The "prion-like" features of Alzheimer’s disease (AD) tauopathy and its relationship with amyloid β (Aβ) has never been experimentally studied in primates phylogenetically close to humans. We injected 17 macaques in the entorhinal cortex with nanograms of tau proteopathic seeds purified from AD brains or control extracts from aged-matched healthy brains, with or without intracerebroventricular co-injections of recombinant Aβ oligomers. After neuropathological examination of the macaque’s brain, we also performed mass spectrometry-based proteomics of macaques’ entorhinal cortex and CA1 to study the spatial response (local and distant) to tau seeds injections (and its modulation by oligomeric Aβ).

2024-01-02 | PXD040522 | Pride

Proteome of Douglas-fir: a resource for genomic research

Project description:First Douglas fir proteomes by nLC-MS/MS from 12 different organs : root, stem, xylem, needle, bud, female and male flowers, immature and mature seed, immature and mature somatic embryos and callus.

2023-10-24 | PXD037815 | Pride

Highlighting the dramatic effects of high temperature on developing Cabernet Sauvignon grape berry through proteomic and metabolomic approaches

Project description:The goal of this project aims to decipher the molecular effects of high temperature on developing Cabernet Sauvignon berries. Using grapevine fruiting cuttings, control and heat-treated berries were sampled to conduct transcriptomic, proteomic and metabolomic analysis.

2020-01-29 | PXD014693 | Pride

Proteomic analysis of the cellular targets of a divalent synthetic SH3 domain ligand

Project description:Comparative LC/MS/MS analysis of pull-down material from an adult rat brain lysate between streptavidin-coated magnetic beads functionalized with either a biotinylated divalent peptide derived from the dynamin proline-rich domain or biotin

2019-11-12 | PXD015292 | Pride

Analysis of the sarkosyl-insoluble proteomes of Parkinson’s disease and Multiple System Atrophy subject brain samples

Project description:Aggregated alpha-synuclein (α-syn) is a principal constituent of Lewy bodies (LBs) and glial cytoplasmic inclusions (GCIs) that are observed respectively inside neurons in Parkinson’s disease (PD) and oligodendrocytes in multiple system atrophy (MSA). Yet, the cellular origin, the exact pathophysiological role, and the mechanism of formation of these inclusions remain to be elucidated. It has recently been proposed that pathological α-syn inclusions are capable of eventually causing the demise of the host cell by virtue of the cumulative sequestration of partner proteins and organelles. In particular, the hypothesis of a local cross-seeding of other fibrillization-prone proteins like tau or TDP-43 has also been put forward. The objective of this study was to examine the composition of these inclusions to gain insight into their origin and mechanisms of formation. We submitted sarkosyl-insoluble extracts of post-mortem brain tissue from PD and MSA patients and control subjects to a comparative proteomic analysis to address these points.

2022-02-17 | PXD024998 | Pride

Analysis of the total and sarkosyl-insoluble proteomes of controls, Parkinson’s disease and multiple system atrophy subject brain samples

Project description:Aggregated alpha-synuclein (α-syn) is a principal constituent of Lewy bodies (LBs) and glial cytoplasmic inclusions (GCIs) that are observed respectively inside neurons in Parkinson’s disease (PD) and oligodendrocytes in multiple system atrophy (MSA). Yet, the cellular origin, the exact pathophysiological role, and the mechanism of formation of these inclusions remain to be elucidated. It has recently been proposed that pathological α-syn inclusions are capable of eventually causing the demise of the host cell by virtue of the cumulative sequestration of partner proteins and organelles. In particular, the hypothesis of a local cross-seeding of other fibrillization-prone proteins like tau or TDP-43 has also been put forward. The objective of this study was to examine the composition of these inclusions to gain insight into their origin and mechanisms of formation. We submitted total solubilized and sarkosyl-insoluble extracts of post-mortem brain tissue from PD and MSA patients and control subjects to a comparative proteomic analysis to address these points. In parallel, we used proteomics for α-syn quantification in total solubilized brain homogenates and the respective sarkosyl-insoluble pellets as an unbiased validation of our results obtained by immunoblotting of these samples and fractions.

2024-03-25 | PXD039575 | 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