A metabolomic view of Staphylococcus aureus and its ser/thr kinase and phosphatase deletion mutants: involvement in cell wall biosynthesis

Chem Biol. 2010 Aug 27;17(8):820-30. doi: 10.1016/j.chembiol.2010.06.012.

Abstract

Little is known about intracellular metabolite pools in pathogens such as Staphylococcus aureus. We have studied a particular metabolome by means of the presented LC-MS method. By investigating the central carbon metabolism which includes most of the energy transfer molecules like nucleotides, sugar mono- and biphosphates, and cofactors, a conclusion about phenotypes and stress answers in microorganisms is possible. Quantitative metabolite levels of S. aureus grown in complex lysogeny broth and in minimal medium were compared in the wild-type S. aureus strain 8325 and the isogenic eukaryotic-like protein serine/threonine kinase (DeltapknB) and phosphatase (Deltastp) deletion mutants. Detection of several remarkable differences, e.g., in nucleotide metabolism and especially cell wall precursor metabolites, indicates a previously unreported importance of serine/threonine kinase/phosphatase on peptidoglycan and wall teichoic acid biosynthesis. These findings may lead to new insights into the regulation of staphylococcal cell wall metabolism.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Carbon / metabolism
  • Cell Wall / metabolism*
  • Chromatography, Liquid
  • Intracellular Space / metabolism
  • Mass Spectrometry
  • Metabolome / genetics
  • Metabolomics / methods*
  • Nucleotides / metabolism
  • Phosphoric Monoester Hydrolases / deficiency*
  • Phosphoric Monoester Hydrolases / genetics
  • Phosphoric Monoester Hydrolases / metabolism
  • Protein Serine-Threonine Kinases / deficiency*
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism
  • Sequence Deletion*
  • Staphylococcus aureus / cytology*
  • Staphylococcus aureus / enzymology
  • Staphylococcus aureus / growth & development
  • Staphylococcus aureus / metabolism*

Substances

  • Nucleotides
  • Carbon
  • Protein Serine-Threonine Kinases
  • Phosphoric Monoester Hydrolases