Browse
Submit Data
Databases
API
Help

Dataset Information

0 Views

0 Connections

0 Citations

0 Reanalyses

0 Downloads

Omics score: 0

Proteome data of a BP1092 mutant of Bordetella pertussis

ABSTRACT: Proteome data of a BP1092 mutant of Bordetella pertussis under virulence modulating and non-modulating conditions

INSTRUMENT(S): Q Exactive HF

ORGANISM(S): Bordetella Pertussis (strain Tohama I / Atcc Baa-589 / Nctc 13251)

TISSUE(S): Cell Culture

SUBMITTER: Kristin Surmann

LAB HEAD: Uwe Völker

PROVIDER: PXD041940 | Pride | 2024-05-24

REPOSITORIES: pride

ACCESS DATA

Json Xml

Dataset's files

Source:

			Action	DRS
	20220502_HF_KRIS_BIOPIC_10_delta1092_SO4_BR2.raw	Raw
	20220502_HF_KRIS_BIOPIC_11_compl1092_BR2.raw	Raw
	20220502_HF_KRIS_BIOPIC_12_compl1092_SO4_BR2.raw	Raw
	20220502_HF_KRIS_BIOPIC_13_wt_BR3.raw	Raw
	20220502_HF_KRIS_BIOPIC_14_wt_SO4_BR3.raw	Raw

Items per page:

1 - 5 of 28

Publications

Role of the Putative Histidine Kinase BP1092 in Bordetella pertussis Virulence Regulation and Intracellular Survival.

Debandi Martina M Carrica Mariela M Hentschker Christian C Baroli Carlos C Völker Uwe U Rodriguez Maria Eugenia ME Surmann Kristin K Lamberti Yanina Y

Journal of proteome research 20240422 5

Bordetella pertussis persists inside host cells, and virulence factors are crucial for intracellular adaptation. The regulation of B. pertussis virulence factor transcription primarily occurs through the modulation of the two-component system (TCS) known as BvgAS. However, additional regulatory systems have emerged as potential contributors to virulence regulation. Here, we investigate the impact of BP1092, a putative TCS histidine kinase that shows increased levels after bacterial ...[more]

PMID: 38644792

Similar Datasets

Proteins of outer membrane vesicles of Bordetella pertussis

Project description:proteome analysis OMV extracted from B. pertussis Tohama I wildtype

2023-05-03 | PXD033489 | Pride

Proteomics of Bordetella pertussis whole-cell and acellular vaccines

Project description:Bordetella pertussis is the etiological agent of whooping cough, a bacterial infection of especially children, which may be fatal without treatment. In frame of studies to investigate putative effects of vaccination on host-pathogen interaction and clonal distribution of strains, in addition to Corynebacterium diphtheriae and Clostridium tetani toxoid vaccines, also whole-cell and acellular pertussis vaccines were analyzed by mass spectrometry.

2019-05-14 | PXD013804 | Pride

Shotgun proteomic analysis of Bordetella pertussis response to iron availability

Project description:B. pertussis Tohama I was cultivated in iron-depleted or iron-repleted medium in order to monitor proteins which are influence by iron supply. More than 200 proteins displayed increased or decreased levels. Proteins involved in iron acquisition, biofilm production and oxidative stress response were increased during iron starvation. Limited iron supply caused on the other hand decreased levels of virulence factors regulated by the BvgAS system.

2015-03-16 | PXD001280 | Pride

BtcB (BP2265) is a T3SS chaperone of the CesT family in Bordetella pertussis

Project description:Bordetella pertussis is a Gram-negative, strictly human respiratory pathogen and the causative agent of whooping cough (pertussis). Similar to other Gram-negative pathogens, B. pertussis produces a functional type III secretion system, but its role in pathogenesis of B. pertussis is enigmatic and has not yet been elucidated. Here, we applied omics RNA-seq as well as LC-MS/MS techniques and co-immunoprecipitation method to identify and characterize the novel CesT family T3SS chaperone BP2265. Our results show that the chaperone BP2265 specifically interacts with the secreted T3SS anti-sigma factor BtrA. Moreover, in the absence of the chaperone, secretion but not production of BtrA and several early, intermediate, and late T3SS substrates is severely impaired. It appears that the role of BtrA in regulating T3SS is more complex and extends beyond its activity as an antagonist of the sigma factor BtrS. We propose to rename BP2265 as BtcB for the Bordetella type III chaperone of BtrA.

2024-01-26 | PXD044487 | Pride

Hfq is involved in global protein expression and stress response in Bordetella pertussis

Project description:In this study, we used gel-free nanoLC-MS/MS-based proteomics to compare the protein profile of B. pertussis wild type and an isogenic hfq defective mutant strain under control an iron limited conditions. We found that Hfq affects the abundance of 302 proteins, which represents 8% of the total B. pertussis coding sequence. The absence of Hfq induced changes in the abundance of proteins involved in metabolic pathways, stress response and virulence. Hfq was also found involved in B. pertussis adaptation to iron starvation, one of the main stresses this pathogen faces inside the host. Altogether, these results indicate that B. pertussis Hfq is involved in bacterial physiological processes as well as bacterial pathogenesis.

2020-02-18 | PXD011753 | Pride

Acetylome analysis of Bordetella pertussis reveals possible targets of novel BP0960 gene-encoded lysine deacetylase

Project description:Acetylation on ε-amino groups of lysine residues (N-ε-lysine acetylation) represents an important mechanism of post-translational regulation of protein function. However, its role and extent in the whooping cough agent Bordetella pertussis remain unknown. In this study, we analyzed the acetylomes of two bacterial mutants lacking putative lysine deacetylases encoded by genes BP0960 and BP3063 and compared them with the acetylome of wild-type B. pertussis. The results suggest that acetylation on lysine residues may modulate the activities of proteins involved in bacterial virulence and of multiple histone-like proteins.

2020-07-19 | PXD016384 | Pride

Integrating proteomic data with metabolic modelling provides insight into key pathways in Bordetella pertussis biofilms

Project description:Pertussis, commonly known as whooping cough is a severe respiratory disease caused by the bacterium, Bordetella pertussis. Despite widespread vaccination, pertussis resurgence has been observed globally. The development of the current acellular vaccine (ACV) has been based on planktonic studies. However, recent studies have shown that B. pertussis readily forms biofilms. A better understanding of B. pertussis biofilms is important for developing novel vaccines that can target all aspects of B. pertussis infection. This study compared the proteomic expression of biofilm and planktonic B. pertussis cells to identify key changes between the conditions. Major differences were identified in virulence factors including an upregulation of toxins (adenylate cyclase toxin and dermonecrotic toxin) and strong downregulation of pertactin and type III secretion system proteins in biofilm cells. To further dissect metabolic pathways that are altered during the biofilm lifestyle, the proteomic data was then incorporated into a genome scale metabolic model using the integrated metabolic analysis tool (iMAT). The analysis revealed that planktonic cells utilised the glyoxylate shunt while biofilm cells completed the full tricarboxylic acid cycle. Differences in processing aspartate, arginine and alanine were identified as well as unique export of valine out of biofilm cells which may have a role in inter-bacterial communication and regulation. Finally, increased polyhydroxybutyrate accumulation and superoxide dismutase activity in biofilm cells may contribute to increased persistence during infection. Taken together, this study modelled major proteomic and metabolic changes that occur in biofilm cells which helps lay the groundwork for further understanding B. pertussis pathogenesis.

2023-08-07 | PXD033664 | Pride

Proteome analysis of Bordetella pertussis isolated from human macrophages

Project description:Previous studies indicated that B. pertussis, historically considered as extracellular pathogen, can invade and replicate within human macrophages. In order to investigate factors involved in the intracellular survival, we analyzed the proteome of intracellular B. pertussis at 3h and 48 h post macrophage infection. From totally 762 identified proteins, we observed differences in gene expression profiles of intracellular bacteria as compared to extracellular bacteria. More than 300 proteins showed significant differences in the level of expression (p< 0.05) between internalized and non-internalized samples. Different intensities were found for proteins associated with virulence, stress response, cell division, transport, and many genes with unknown functions. Proteins involved in stress response increased in level early after infection, including ClpX, GroEL and HsIU. Two proteins involved in iron uptake were found increased as early as 3 h post infection and remained at high level 48 h post-infection. These proteins are BfrD and BfrE, recently identified as TonB-dependent outer membrane catecholamine receptors involved in iron uptake from transferrin in B. bronchiseptica. Interestingly, we found at least three proteins of the Type III Secretion System (TTSS) increased already at 3 h after infection, the proteins BteA, BscC, and BopN suggesting that TTSS becomes operative when bacteria infect human macrophages. Selected virulence factors and metabolic enzymes were validated using the multiple reaction monitoring. These results represent the first characterization of intracellular B. pertussis proteome and demonstrate that this pathogen undergoes an adaptive response that enables the development of an intracellular infection.

2016-02-29 | PXD002997 | Pride

Multi-omics analysis of Bordetella pertussis fermentation

Project description:Bordetella pertussis is the bacterial causative agent of whooping cough, a serious respiratory illness. An extensive knowledge on its virulence regulation and metabolism is a key factor to ensure pertussis vaccine manufacturing process robustness. The aim of this study was to refine our comprehension of B. pertussis physiology along the fermentation process. A longitudinal multi-omics analysis was carried out over a 26-hour small-scale fermentation of B. pertussis. Fermentations were performed in batch mode and under culture conditions intending to mimic industrial processes. Putative cysteine and proline starvations were respectively observed at the beginning of the exponential phase (from 4h to 8h) and during the exponential phase (18h45). As revealed by multi-omics analyses, the proline starvation induced major molecular changes, including a transient metabolism with internal stock consumption. In the meantime, growth and specific total PT, PRN and Fim2 antigen productions were negatively affected. Interestingly, the master virulence-regulating two-component system of B. pertussis (BvgASR) was not evidenced as the sole virulence regulator in this in vitro growth condition. Indeed, novel intermediate regulators were identified as putatively involved in the expression of some virulence-activated genes (vags). Such longitudinal multi-omics analysis applied to B. pertussis fermentation process emerges as a powerful tool for characterization and incremental optimization of vaccine antigen production.

2023-03-11 | PXD039615 | Pride

Comparative phosphoproteomics of classical bordetellae elucidates the role of serine, threonine and tyrosine phosphorylation in Bordetella biology and virulence

Project description:This study characterised the Ser/Thr/Tyr phosphoproteome of classical Bordetella species and examined its role in Bordetella biology and virulence. This study found 70 unique phosphorylated proteins in the classical bordetellae group with a high degree of conservation observed and phosphorylation was a key regulator of Bordetella metabolism with proteins involved in gluconeogenesis, TCA cycle, amino acid and nucleotide synthesis significantly enriched. We also identified the phosphorylation of three key virulence pathways which separates classical from non-classical bordetellae including the type III secretion system, alcaligin synthesis (the primary siderophore produced by Bordetella) and the BvgAS master transcriptional regulatory system for virulence genes in Bordetella. Seven new phosphosites were identified in BvgA with 6 located in the DNA binding domain. Of the 7 new phosphosites, four were not detected in non-classical bordetellae. This suggests that serine/threonine phosphorylation may play an important role in stabilising or destabilising BvgA binding to DNA for fine-tuning of virulence gene expression and that BvgA phosphorylation may be an important factor that separates classical from non-classical bordetellae. This study provides the first insight into the phosphoproteome of classical Bordetella species and the role Ser/Thr/Tyr phosphorylation plays in Bordetella biology and virulence.

2021-03-26 | PXD020866 | Pride