> Detailanzeige

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; Schmidt, Frank

A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions

Literatur-
verwaltung

Zur
Merkliste

Lösche von
Merkliste

Per Whatsapp teilen

Schließen

Merkliste



Sie können Bookmarks mittels Listen verwalten, loggen Sie sich dafür bitte in Ihr SLUB Benutzerkonto ein.
  • Medientyp: E-Artikel
  • Titel: A global Staphylococcus aureus proteome resource applied to the in vivo characterization of host-pathogen interactions
  • Beteiligte: 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; Schmidt, Frank
  • Erschienen: Springer Science and Business Media LLC, 2017
  • Erschienen in: Scientific Reports
  • Sprache: Englisch
  • DOI: 10.1038/s41598-017-10059-w
  • ISSN: 2045-2322
  • Schlagwörter: Multidisciplinary
  • Entstehung:
  • Anmerkungen:
  • Beschreibung: <jats:title>Abstract</jats:title><jats:p>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 <jats:italic>Staphylococcus aureus</jats:italic> 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 <jats:italic>S. aureus</jats:italic> to the intracellular niche in human bronchial epithelial cells and in a murine pneumonia model. In epithelial cells, abundance changes for more than 400 <jats:italic>S. aureus</jats:italic> 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 <jats:italic>in vivo</jats:italic> murine pneumonia model, our data-independent acquisition quantification analysis revealed for the first time the <jats:italic>in vivo</jats:italic> proteome adaptation of <jats:italic>S. aureus</jats:italic>. From approximately 2.15 × 10<jats:sup>5</jats:sup>  <jats:italic>S. aureus</jats:italic> 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.</jats:p>
  • Zugangsstatus: Freier Zugang