Publication Title
Sci Rep
Document Type
Article
Publication Date
9-8-2017
Keywords
Animals; Bacterial Proteins; Computational Biology; Epithelial Cells; Host-Pathogen Interactions; Humans; Ions; Mice; Peptides; Proteome; Proteomics; Respiratory Mucosa; Staphylococcal Infections; Staphylococcus aureus
Abstract
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
Specialty/Research Institute
Institute for Systems Biology
Specialty/Research Institute
Infectious Diseases
