Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

S54-dependent response to nitrogen limitation and virulence in Burkholderia cenocepacia H111

ABSTRACT: Using a discovery shotgun proteomics approach, the expressed proteome of Burkholderia cenocepacia (strain H111) was analyzed under normal and starved nitrogen growth conditions. B. cenocepacia is an opportunistic human pathogen that is particularly problematic for patients suffering from cystic fibrosis.

OTHER RELATED OMICS DATASETS IN: PRJNA276555

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Burkholderia Cenocepacia H111

SUBMITTER: Ulrich Goldmann

LAB HEAD: Gabriella Pessi

PROVIDER: PXD001924 | Pride | 2015-05-05

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20140106_22_mlminus_ic6.mgf	Mgf
	20140106_22_mlminus_ic6.mzid.gz	Mzid
	20140106_22_mlminus_ic6.pride.mgf.gz	Mgf
	20140106_22_mlminus_ic6.pride.mztab.gz	Mztab
	20140106_22_mlminus_ic6.raw	Raw

Items per page:

1 - 5 of 200

Publications

σ54-Dependent Response to Nitrogen Limitation and Virulence in Burkholderia cenocepacia Strain H111.

Lardi Martina M Aguilar Claudio C Pedrioli Alessandro A Omasits Ulrich U Suppiger Angela A Cárcamo-Oyarce Gerardo G Schmid Nadine N Ahrens Christian H CH Eberl Leo L Pessi Gabriella G

Applied and environmental microbiology 20150403 12

Members of the genus Burkholderia are versatile bacteria capable of colonizing highly diverse environmental niches. In this study, we investigated the global response of the opportunistic pathogen Burkholderia cenocepacia H111 to nitrogen limitation at the transcript and protein expression levels. In addition to a classical response to nitrogen starvation, including the activation of glutamine synthetase, PII proteins, and the two-component regulatory system NtrBC, B. cenocepacia H111 also upreg ...[more]

PMID: 25841012

Similar Datasets

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylation events within FliF and MotB are dispensable for motility. - DIA

Project description:Within the Burkholderia genus O-linked protein glycosylation is now known to be highly conserved at the pathway and glycosylation substrate levels. While inhibition of glycosylation has been shown to be detrimental to virulence in B. cenocepacia, little is known about the role of glycosylation in Burkholderia glycoproteins. Within this study we have sought to improve our understanding of the breadth and dynamics of the B. cenocepacia O-glycoproteome to identify glycoproteins which require glycosylation for functionality. Assessing the glycoproteome across multiple common culturing media (LB, TSB, and artificial sputum medium to simulate cystic fibrosis sputum-like conditions) we demonstrate at least 141 glycoproteins are subjected to glycosylation within B. cenocepacia K56-2. Leveraging this insight, we quantitively assessed the glycoproteome of B. cenocepacia using Data-Independent Acquisition (DIA) across culturing media and growth phases revealing most B. cenocepacia glycoproteins are express under all conditions. Examination of how the absence of glycosylation impacts the glycoproteome reveals only a subset of the glycoproteome (BCAL1086, BCAL2974, BCAL0525, BCAM0505 and BCAL0127) appear impacted by the loss of glycosylation. Assessing the proteomic and phenotypic impacts of the loss of these glycoproteins compared to glycosylation null strains revealing the loss of BCAL0525, and to a lesser extend BCAL0127, mirror the proteomic effects observed in the absence of glycosylation. Finally, we demonstrate the loss of glycosylation within BCAL0525 at Serine-358 results in both loss of motility and proteomic impacts on flagellar apparatus consistent with the loss of apparatus stability. Combined this work demonstrates that O-linked glycosylation of BCAL0525 is functionally important within B. cenocepacia.

2024-04-17 | PXD043280 | Pride

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylation events within FliF and MotB are dispensable for motility. - FliF DIA

2024-04-17 | PXD045246 | Pride

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylation events within FliF and MotB are dispensable for motility. - DIA analysis of glycoprotein mutants

2024-04-17 | PXD043197 | Pride

Gene expression in sRNA deletion mutant Burkholderia cenocepacia J2315 delta ncS35

Project description:The small RNA ncS35 was deleted from the Burkholderia cenocepacia J2315 genome. Gene expression of mutant was compared to wild type in three growth conditions: exponential phase and stationary phase planktonic growth and biofilm growth, all in LB medium.

2017-08-19 | E-MTAB-5526 | biostudies-arrayexpress

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylation events within FliF and MotB are dispensable for motility.-DDA delta BCAM0505

2024-04-17 | PXD043184 | Pride

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylation events within FliF and MotB are dispensable for motility. -DDA BCAL0127

2024-04-17 | PXD043187 | Pride

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylation events within FliF and MotB are dispensable for motility. -DDA BCAL0525

2024-04-17 | PXD043186 | Pride

Proteomic analysis of B. cenocepacia H111 delta pglL strains

Project description:LFQ analysis of B. cenocepacia strain H111 strains to assess the impact of the loss of pglL (I35_RS13570)

2021-07-21 | PXD023755 | Pride

Glycoproteomic and Proteomic analysis of Burkholderia cenocepacia reveals glycosylationevents within FliF and MotB are dispensable for motility. -FAIMS stationary growth

2024-04-17 | PXD043193 | Pride