The Muropeptide Composition of the Peptidoglycan of Staphylococcus aureus Determined with Reversed-Phase High Performance Liquid Chromatography

  • Boudewijn L. M. de Jonge
  • Alexander Tomasz
Part of the Federation of European Microbiological Societies Symposium Series book series (FEMS, volume 65)


While extensive early studies on the chemical composition of the cell walls of Staphylococcus aureus have been described in the literature (e.g., Tipper and Strominger, 1965), the high resolution technique of reversed-phase high performance liquid chromatography (HPLC), recently developed by Glauner et al. (1988), has not been applied to staphylococcal cell walls until now. In this communication, we report the results of studies in which the HPLC method, adapted to staphylococci, was used to determine the muropeptide composition of a highly methicillin resistant isolate of S. aureus and some of its transposon mutants with decreased antibiotic resistance.


High Performance Liquid Chromatography High Performance Liquid Chromatography High Performance Liquid Chromatography Method Beta Lactam Antibiotic Methicillin Resistance 
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  1. Berger-Bachi, B., and Kohler, M.L. (1983) A novel site on the chromosome of Staphvlococcus aureus influencing the level of methicillin resistance: genetic mapping. FEMS Microbiol. Lett. 20, 305–309.CrossRefGoogle Scholar
  2. De Jonge, B.L.M., Chang, Y.-S., Gage, D., and Tomasz, A. (1992a) Peptidoglycan composition of a highly methicill in-resistant Staphvlococcus aureus strain: the role of penicillin binding protein 2A. J. Biol. Chem. 267, in press.Google Scholar
  3. De Jonge, B.L.M., Chang, Y.-S., Gage, D., and Tomasz, A. (1992b) Peptidoglycan composition in heterogeneous Tn551 mutants of a methicillin-resistant Staphvlococcus aureus strain. J. Biol. Chem. 267, in press.Google Scholar
  4. Glauner, B., Holtje, J.-V., and Schwarz, U. (1988) The composition of the murein of Escherichia coli. J. Biol. Chem. 263, 10888–10095.Google Scholar
  5. Matthews, P., and Tomasz, A. (1990) Insertional inactivation of the mec gene in a transposon mutant of a methicill in-resistant clinical isolate of Staphvlococcus aureus. Antimicrob. Agents Chemother. 34, 1777–1779.PubMedCrossRefGoogle Scholar
  6. Kornblum, J., Hartman, B.J., Novick, R.P., and Tomasz, A. (1986) Conversion of a homogeneously methicillin-resistant strain of Staphvlococcus aureus to heterogeneous resistance by Tn551-mediated insertional inactivation. J. Clin. Microbiol. 5, 714–718.CrossRefGoogle Scholar
  7. Murakami, K., and Tomasz, A. (1989) Involvement of multiple genetic determinants in high-level methicillin resistance in Staphvlococcus aureus. J. Bacteriol. 171, 874–879.PubMedGoogle Scholar
  8. Song, M.D., Wachi, M., Doi, M., Ishino, F., and Matsuhashi, M. (1987) Evolution of an inducible penicillin-target protein in methicillin-resistant Staphvlococcus aureus by gene fusion. FEBS Lett. 221, 167–171.PubMedCrossRefGoogle Scholar
  9. Tipper, D.J., and Strominger, J.L. (1965) Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. USA 54, 1133–1141.PubMedCrossRefGoogle Scholar
  10. Tipper, D.J., and Strominger, J.L. (1968) Biosynthesis of the peptidoglycan of bacterial cell walls. XII Inhibition of cross-linking by penicillins and cephalosporins: studies in Staphvlococcus aureus in vivo. J. Biol. Chem. 243, 3169–3179.PubMedGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1993

Authors and Affiliations

  • Boudewijn L. M. de Jonge
    • 1
  • Alexander Tomasz
    • 1
  1. 1.Laboratory of MicrobiologyThe Rockefeller UniversityNew YorkUSA

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