Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Type II sectection within A. baumannii (WT vs gspD)

ABSTRACT: Comparsion of the secretome of A. baumannii (WT vs gspD)

INSTRUMENT(S): Q Exactive

ORGANISM(S): Acinetobacter Calcoaceticus/baumannii Complex

SUBMITTER: Nichollas Scott

LAB HEAD: Mario F. Feldman

PROVIDER: PXD030491 | Pride | 2022-04-06

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Similar Datasets

Sectection analysis of A. baumannii (WT vs gspD vs HlyD1 vs HlyD2 vs RTX)

Project description:Comparsion of the secretome of A. baumannii (WT vs gspD vs HlyD1 vs HlyD2 vs RTX)

2022-04-06 | PXD030460 | Pride

UPAB1 secretome analysis of hlyD1 vs hlyD2 vs Wt.

Project description:A. baumannii UPAB1 secretome analysis of hlyD1 vs Wt and hlyD2 vs Wt.

2021-08-09 | PXD024736 | Pride

RNA sequencing of ATCC 17978hm Acineotbacter baumannii strain and CpdA mutant

Project description:Difference in RNA expression levels between Acinetobacter baumannii cells expressing high and low levels of cyclic AMP Total RNA obtained from Acineotbacter baumannii bacterial cells in Log phase gown in MH broth culture, isolated RNA in triplicate from three expreiment. cpdA::Tn mutant and 17978hm strain compared. Assessing increased levels of cAMP within the cell

2015-06-21 | E-GEOD-64935 | biostudies-arrayexpress

CBU1543 immunopercipation (CBU1543 vs empty vector)

Project description:immunopercipation of CBU1543 to identify interaction partners

2023-08-07 | PXD030191 | Pride

PAA and the A. baumannii ATCC17978 proteome

Project description:Analysis of proteome changes in respond to PAA, PAA+ST, DMSO and ST.

2022-04-06 | PXD025651 | Pride

neisserial OTases have different protein specificies

Project description:Proteomic investigation on the glycosylation substrates and proteome effects of altering neisserial OTases within the proteome of N. gonorrhoeae MS11

2022-04-04 | PXD024737 | Pride

Confirmation of Arg-Glucosylation on multiple Death domain proteins

Project description:In vitro and tranfection analysis of death domain containing proteins to assess the ability of NleB2 to glycosylate these proteins.

2021-05-25 | PXD025531 | Pride

Arg-Glycosylation of NleB2 during infections

Project description:Analysis of NleB2 mediated glycosylation of RIPK1DD during infections.

2021-05-25 | PXD025057 | Pride

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

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 | PXD043197 | 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

OmicsDI is part of the ELIXIR infrastructure

OmicsDI is an Elixir interoperability service. Learn more ›

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