Contact of Corynebacterium diphtheriae with macrophages induce adaptations on both bacterial and cellular sides. Using an experimental design involving gentamicin protection and liquid chromagraphy followed by mass-spectrometry, a multi-species proteomic dataset was analyzed at different time points of the infection assay. Several previously undescribed Corynebacterium proteins were differentially regulated, as well as key macrophage components of the phagolysosome. Overall, Bacteria responded to phagocytosis by changes in DNA repair, transcription and cell wall synthesis proteins, while macrophages showed changes in components of the innate immune system.
This dataset consists of:
- ThermoFisher's .raw files of three biological replicates of the infection assays (total proteome mixture of bacteria and eukaryotic cells and tagged using TMT-10). They can be downloaded all at once via the .zip file.
- Protein abundance data for Macrophage THP-1 cells (M0) obtained by LC-MS/MS followed by peptide sequencing using Proteome Discoverer (ThermoFisher) -see .zip folder.
- Protein abundance data for Macrophage C. diphtheriae ISS3319 (CD) obtained by LC-MS/MS followed by peptide sequencing using Proteome Discoverer (ThermoFisher) - see .zip folder.
- Differential protein abundance analysis for CD and M0 using LIMMA.
- Data underlying the growth curves observed in CD in RPMI + 10% FBS conditions (infection assay conditions).
- BLASTP searches, PFAM clans, and InterPro annotations for CD.
- STRING-based PPI network (baseline) and APSPs between differentially abundant proteins in CD.
- Related R scripts.
[doi:10.25345/C5N01059C]
[dataset license: CC0 1.0 Universal (CC0 1.0)]
Keywords: Host-pathogen interaction ; Microbiology ; Macrophage, THP-1 Null cells ; Gentamicin protection assay ; Corynebacterium diphtheriae ; Diphtheria ; DatasetType:Proteomics
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Principal Investigators: (in alphabetical order) |
Andreas Burkovski, Friedrich-Alexander-Universitaet Erlangen-Nuernberg (FAU), Germany |
| Submitting User: | Muszeb |
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FTP Download Link (click to copy):
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