Animals; Bacterial Proteins; Computational Biology; Epithelial Cells; Host-Pathogen Interactions; Humans; Ions; Mice; Peptides; Proteome; Proteomics; Respiratory Mucosa; Staphylococcal Infections; Staphylococcus aureus
Data-independent acquisition mass spectrometry promises higher performance in terms of quantification and reproducibility compared to data-dependent acquisition mass spectrometry methods. To enable high-accuracy quantification of Staphylococcus aureus proteins, we have developed a global ion library for data-independent acquisition approaches employing high-resolution time of flight or Orbitrap instruments for this human pathogen. We applied this ion library resource to investigate the time-resolved adaptation of S. aureus to the intracellular niche in human bronchial epithelial cells and in a murine pneumonia model. In epithelial cells, abundance changes for more than 400 S. aureus proteins were quantified, revealing, e.g., the precise temporal regulation of the SigB-dependent stress response and differential regulation of translation, fermentation, and amino acid biosynthesis. Using an in vivo murine pneumonia model, our data-independent acquisition quantification analysis revealed for the first time the in vivo proteome adaptation of S. aureus. From approximately 2.15 × 10
Institute for Systems Biology
Michalik, Stephan; Depke, Maren; Murr, Annette; Gesell Salazar, Manuela; Kusebauch, Ulrike; Sun, Zhi; Meyer, Tanja C; Surmann, Kristin; Pförtner, Henrike; Hildebrandt, Petra; Weiss, Stefan; Palma Medina, Laura Marcela; Gutjahr, Melanie; Hammer, Elke; Becher, Dörte; Pribyl, Thomas; Hammerschmidt, Sven; Deutsch, Eric W; Bader, Samuel L; Hecker, Michael; Moritz, Robert L; Mäder, Ulrike; Völker, Uwe; and Schmidt, Frank, "A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions." (2017). Articles, Abstracts, and Reports. 1821.