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MetabolomicsComparative analysis of the adaptation of Staphylococcus aureus to internalization by different types of human non-professional phagocytic host cells (NMR assay)
Staphylococcus aureus is a human pathogen that can cause a wide range of diseases. Although formerly regarded as extracellular pathogen, it has been shown that S. aureus can also be internalized by host cells and persist within these cells. In the present study, we comparatively analyzed survival an...
2015-07-01 | MTBLS102 | MetaboLights
ProteomicsProteomic characterization of the interplay of Staphylococcus aureus and human alveolar epithelial cells during infection - S. aureus proteins
Since infectious diseases caused by Staphylococcus aureus are still a major threat for human health we aimed to gain a detailed understanding of the molecular interplay of pathogen and host upon internalization by proteome analyses. In the present study we infected human alveolar epithelial A549 cel...
ORGANISM(S): Staphylococcus aureus 
2015-08-05 | PXD002384 | Pride
Proteomics Host-pathogen interaction Epithelial cells Internalization Staphylococcus aureus 
ProteomicsProteomic characterization of the interplay of Staphylococcus aureus and human alveolar epithelial cells during infection - host cell proteins
Since infectious diseases caused by Staphylococcus aureus are still a major threat for human health we aimed to gain a detailed understanding of the molecular interplay of pathogen and host upon internalization by proteome analyses. In the present study we infected human alveolar epithelial A549 cel...
ORGANISM(S): Homo sapiens (Human) 
2015-08-05 | PXD002388 | Pride
Proteomics Host-pathogen interaction Epithelial cells Internalization Staphylococcus aureus 
ProteomicsProteome analysis of Bordetella pertussis isolated from human macrophages
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 macro...
ORGANISM(S): Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2016-02-29 | PXD002997 | Pride
Proteomics Macrophages B. pertussis Internalization 
ProteomicsAnalysis of secreted S. aureus proteins after isolation of phagosomes from infected human epithelial cells
Bacteria such as Staphylococcus aureus are generally engulfed by the host with a membrane when internalized by non-professional phagocytic host cells. These vacuoles then mature to phagosomes which can fuse with lysosomes enabling killing and digestion of the pathogen. Former proteome approaches enr...
ORGANISM(S): Homo sapiens (Human) Staphylococcus aureus 
2018-06-29 | PXD007885 | Pride
Host-pathogen-interaction Phagosomes Staphylococcus aureus Quantitative proteomics Single reaction monitoring (srm) Virulence factors 
ProteomicsShotgun proteomic analysis of Bordetella pertussis response to iron availability
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 ...
ORGANISM(S): Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2015-03-16 | PXD001280 | Pride
Shotgun proteomics Iron limitation B. pertussis 
ProteomicsProteins of outer membrane vesicles of Bordetella pertussis
proteome analysis OMV extracted from B. pertussis Tohama I wildtype
ORGANISM(S): Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2023-05-03 | PXD033489 | Pride
Proteomics Outer membrane vesicles Infection B. pertussis tohama i 
ProteomicsHfq is involved in global protein expression and stress response in Bordetella pertussis
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. pe...
ORGANISM(S): Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2020-02-18 | PXD011753 | Pride
Proteomics Iron limitation Stress response Hfq B. pertussis 
ProteomicsProteome data of clinical Klebsiella pneumoniae
Proteome data of clinical Klebsiella pneumoniae and two reference strains after growth in urine mimicking medium
ORGANISM(S): Klebsiella pneumoniae KP-1 
2025-08-13 | PXD047744 | Pride
Clinical isolates Proteomics Mass spectrometry Klebsiella pneumoniae 
ProteomicsProteome data of a BP1092 mutant of Bordetella pertussis
Proteome data of a BP1092 mutant of Bordetella pertussis under virulence modulating and non-modulating conditions
ORGANISM(S): Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251) 
2024-05-24 | PXD041940 | Pride
Proteomics Bp1092 Bordetella pertussis Virulence factors 
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