Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Bacteroides thetaiotaomicron OMV, TM and WC comparsion of delta BT4720, delta BT_4721, delta BT_4720_4721 and WT

ABSTRACT: Proteomic comparsion of Bacteroides thetaiotaomicron OMV, TM and WC of delta BT4720, delta BT_4721, delta BT_4720_4721 and WT

INSTRUMENT(S): Orbitrap Exploris 480

ORGANISM(S): Bacteroides Thetaiotaomicron

SUBMITTER: Nichollas Scott

LAB HEAD: Mario Feldman

PROVIDER: PXD043360 | Pride | 2024-02-08

REPOSITORIES: Pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20230118_NSco-5634_MF_Batch1_Sample01.raw	Raw
	20230118_NSco-5634_MF_Batch1_Sample02.raw	Raw
	20230118_NSco-5634_MF_Batch1_Sample03.raw	Raw
	20230118_NSco-5634_MF_Batch1_Sample04.raw	Raw
	20230118_NSco-5634_MF_Batch1_Sample05.raw	Raw

Items per page:

1 - 5 of 50

Similar Datasets

Bacteroides thetaiotaomicron OMV proteomics

Project description:Comparative proteomics of Bacteroides thetaiotaomicron samples comparing the total membrane (TM) and outer membrane vesicles (OMV) of WT B. thetaiotaomicron and delta 4364

2024-10-15 | PXD043219 | Pride

Identification of levoglucosan degradation pathways in bacteria

Project description:Levoglucosan is produced in the pyrolysis of cellulose and starch, including from bushfires or the burning of biofuels, and is deposited from the atmosphere across the surface of the earth. We describe two levoglucosan degrading Paenarthrobacter spp. (Paenarthrobacter nitrojuajacolis LG01 and Paenarthrobacter histidinolovorans LG02) that were isolated by metabolic enrichment on levoglucosan as sole carbon source. Genome sequencing and proteomics analysis revealed expression of a series of gene clusters encoding known levoglucosan degrading enzymes, levoglucosan dehydrogenase (LGDH, LgdA), 3-keto-levoglucosan b-eliminase (LgdB1) and glucose 3-dehydrogenase (LgdC), along with an ABC transporter cassette and associated solute binding protein. However, no homologues of 3-ketoglucose dehydratase (LgdB2) were evident. The expressed gene clusters contained a range of putative sugar phosphate isomerase/xylose isomerases with weak similarity to LgdB2. Sequence similarity network analysis of genome neighbors revealed that homologues of LgdA, LgdB1 and LgdC are generally conserved in a range of bacteria in the phyla Firmicutes, Actinobacteria and Proteobacteria. One sugar phosphate isomerase/xylose isomerase cluster (LgdB3) was identified with limited distribution mutually exclusive with LgdB2. LgdB1, LgdB2 and LgdB3 adopt similar predicted 3D folds suggesting overlapping function in processing intermediates in LG metabolism. Our findings highlight the diversity within the LGDH pathway through which bacteria utilize levoglucosan as a nutrient source.

2023-05-10 | PXD039086 | Pride

Novel cell-to-cell interactions revealed by cryotomography of a DPANN coculture system

Project description:DPANN are a widespread and highly diverse group of archaea characterised by their small size, reduced genome, limited metabolic pathways, and symbiotic existence. DPANNs are predominantly obligate ectosymbionts that depend on their host for their survival and proliferation. Despite the recent expansion in this clade, the structural and molecular details of host recognition, host-DPANN intercellular communication, and host adaptation in response to DPANN attachment remain unknown. Here, we used electron cryotomography (cryo-ET) to reveal that the Candidatus Micrarchaeota” (ARM-1) interacts with its host through intercellular proteinaceous nanotubes. These tubes (~4.5 nm wide) originate in the host, extend all the way to the DPANN cytoplasm and act like tunnels for intercellular exchange. Combining cryo-ET and sub-tomogram averaging, we revealed the in situ architectures of host and DPANN S-layers and the structures of the nanotubes in their primed and extended states, providing mechanistic insights into substrate exchange. Additionally, we performed comparative proteomics and genomic analyses to identify host proteomic changes in response to the DPANN attachment. Our results showed striking alterations in host-proteome during symbiosis and upregulation/downregulation of key cellular pathways. Collectively, these results provided unprecedented insights into the structural basis of host-DPANN communication and deepen our understanding of the host ectosymbiotic relationships.

2024-05-28 | PXD045678 | Pride

Enterococcus faecium mutant proteome analysis

Project description:DIA based comparsion of padR mutant, complement and WT strains

2024-08-15 | PXD039832 | Pride

Proteomic analysis Enterococcus faecium

Project description:Proteomic analysis Enterococcus faecium samples to assess proteomic alterations (20220922_NSco_Stinear)

2024-08-15 | PXD039831 | Pride

Impact of TrmB on the Acinetobacter baumannii proteomic

Project description:With this work the Impact of TrmB on the Acinetobacter baumannii proteomic was examined (=/-) H2O2

2023-07-19 | PXD040002 | Pride

indentification of PA modified proteins

Project description:Enrichment of polysialylated proteins from NK92 cells