A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions. Academic Article uri icon

Overview

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 × 105 S. aureus cells, 578 proteins were identified. Increased abundance of proteins required for oxidative stress response, amino acid biosynthesis, and fermentation together with decreased abundance of ribosomal proteins and nucleotide reductase NrdEF was observed in post-infection samples compared to the pre-infection state.

publication date

  • September 8, 2017

Research

keywords

  • Bacterial Proteins
  • Host-Pathogen Interactions
  • Proteome
  • Proteomics
  • Staphylococcal Infections
  • Staphylococcus aureus

Identity

PubMed Central ID

  • PMC5591248

Scopus Document Identifier

  • 85028967340

Digital Object Identifier (DOI)

  • 10.1016/j.jprot.2015.07.034

PubMed ID

  • 28887440

Additional Document Info

volume

  • 7

issue

  • 1