Abstract
To simultaneously obtain proteome data of host and pathogen from an internalization experiment, human alveolar epithelial A549 cells were infected with Staphylococcus aureus HG001 which carried a plasmid (pMV158GFP) encoding a continuously expressed green fluorescent protein (GFP). Samples were taken hourly between 1.5 h and 6.5 h post infection. By fluorescence activated cell sorting GFP-expressing bacteria could be enriched from host cell debris, but also infected host cells could be separated from those which did not carry bacteria after contact (exposed). Additionally, proteome data of A549 cells which were not exposed to S. aureus but underwent the same sample processing steps are provided as a control. Time-resolved changes in bacterial protein abundance were quantified in a label-free approach. Proteome adaptations of host cells were monitored by comparative analysis to a stable isotope labeled cell culture (SILAC) standard. Proteins were extracted from the cells, digested proteolytically, measured by nanoLC–MS/MS, and subsequently identified by database search and then quantified. The data presented here are related to a previously published research article describing the interplay of S. aureus HG001 and human epithelial cells (Surmann et al., 2015 [1]). They have been deposited to the ProteomeXchange platform with the identifiers PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002384 for the S. aureus HG001 proteome dataset and PRIDE: http://www.ebi.ac.uk/pride/archive/projects/PXD002388 for the A549 proteome dataset.
Highlights
To simultaneously obtain proteome data of host and pathogen from an internalization experiment, human alveolar epithelial A549 cells were infected with Staphylococcus aureus HG001 which carried a plasmid encoding a continuously expressed green fluorescent protein (GFP)
Proteome data of A549 cells which were not exposed to S. aureus but underwent the same sample processing steps are provided as a control
We provide data from an internalization approach to allow simultaneous and complementing proteome analysis of host (A549 cells) and pathogen (S. aureus) employing a combination of cell sorting and nanoLC–MS/MS
Summary
MS data, tables Data-dependent acquisition of tandem mass spectra using an LTQ Orbitrap Velos mass spectrometer (Thermo Fischer Scientific, Germany). .raw files A549 cells were infected with S. aureus HG001 pMV158GFP. We provide data from an internalization approach to allow simultaneous and complementing proteome analysis of host (A549 cells) and pathogen (S. aureus) employing a combination of cell sorting and nanoLC–MS/MS. The data will be of value to researchers studying proteomics of infection and internalization with S. aureus or other pathogenic bacteria. For the pathogen the data will allow assessment of protein synthesis rates and stability after infection due to the pulse-chase approach in which bacteria were labeled with heavy amino acids prior to infection. Proteome data of internalized bacteria and infected host cells collected hourly in the first hours post infection are presented.
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