This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrowReprints and Permissions
Right arrow Copyright Information
Right arrow Books from ASM Press
Right arrow MicrobeWorld
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Glanzmann, P.
Right arrow Articles by Berger-Bächi, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Glanzmann, P.
Right arrow Articles by Berger-Bächi, B.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, February 1999, p. 240-245, Vol. 43, No. 2
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.

glmM Operon and Methicillin-Resistant glmM Suppressor Mutants in Staphylococcus aureus

Philipp Glanzmann,1 John Gustafson,1,dagger Hithoshi Komatsuzawa,2 Kouji Ohta,2 and Brigitte Berger-Bächi1,*

Institute for Medical Microbiology, University of Zürich, CH-8028 Zürich, Switzerland,1 and Department of Microbiology, Hiroshima University School of Dentistry, Kasumi 1-2-3, Minami-ku, Hiroshima City, Hiroshima 734-8553, Japan2

Received 10 August 1998/Returned for modification 2 October 1998/Accepted 12 November 1998

The Staphylococcus aureus phosphoglucosamine mutase gene glmM was shown to be the last gene of a three-cistron operon, orf1-orf2-glmM. One transcriptional start was identified upstream of orf1, and a second start producing a monocistronic transcript was identified upstream of glmM. Disruption of glmM abolished GlmM production, decreased methicillin resistance, and resulted in teicoplanin hypersusceptibility without affecting the production of the endogenous penicillin-binding proteins and PBP 2'. Complementation of the glmM mutation by the complete glmM operon restored both methicillin resistance and normal teicoplanin susceptibility. In contrast, a highly methicillin-resistant suppressor mutant obtained by selection for growth in the presence of methicillin remained GlmM deficient and teicoplanin hypersusceptible. The suppressor mutation was not linked to the glmM operon but was correlated with decreased autolysis and increased production of a 49-kDa protein, suggesting that there is an alternative pathway for glucosamine-1-phosphate synthesis in S. aureus.


* Corresponding author. Mailing address: Institute for Medical Microbiology, University of Zürich, Gloriastr. 32, P.O. Box, CH8028 Zürich, Switzerland. Phone: 41-1 634 26 50. Fax: 41-1 634 49 06. E-mail: bberger{at}immv.unizh.ch.

dagger Present address: Curtin University of Technology, P.O. Box U1987, Perth 6001, Western Australia.


Antimicrobial Agents and Chemotherapy, February 1999, p. 240-245, Vol. 43, No. 2
0066-4804/99/$04.00+0
Copyright © 1999, American Society for Microbiology. All rights reserved.



This article has been cited by other articles:

  • McCallum, N., Brassinga, A. K. C., Sifri, C. D., Berger-Bachi, B. (2007). Functional Characterization of TcaA: Minimal Requirement for Teicoplanin Susceptibility and Role in Caenorhabditis elegans Virulence. Antimicrob. Agents Chemother. 51: 3836-3843 [Abstract] [Full Text]  
  • Wang, L., Trawick, J. D., Yamamoto, R., Zamudio, C. (2004). Genome-wide operon prediction in Staphylococcus aureus. Nucleic Acids Res 32: 3689-3702 [Abstract] [Full Text]  
  • Cordwell, S. J., Larsen, M. R., Cole, R. T., Walsh, B. J. (2002). Comparative proteomics of Staphylococcus aureus and the response of methicillin-resistant and methicillin-sensitive strains to Triton X-100. Microbiology 148: 2765-2781 [Abstract] [Full Text]  
  • Komatsuzawa, H., Ohta, K., Sugai, M., Fujiwara, T., Glanzmann, P., Berger-Bachi, B., Suginaka, H. (2000). Tn551-mediated insertional inactivation of the fmtB gene encoding a cell wall-associated protein abolishes methicillin resistance in Staphylococcus aureus. J Antimicrob Chemother 45: 421-431 [Abstract] [Full Text]