This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental material
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 Gründling, A.
Right arrow Articles by Schneewind, O.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Gründling, A.
Right arrow Articles by Schneewind, O.
Right arrowPubmed/NCBI databases
*Substance via MeSH

 Previous Article  |  Next Article 

Journal of Bacteriology, April 2006, p. 2463-2472, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2463-2472.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Cross-Linked Peptidoglycan Mediates Lysostaphin Binding to the Cell Wall Envelope of Staphylococcus aureus{dagger}

Angelika Gründling and Olaf Schneewind*

Department of Microbiology, University of Chicago, Chicago, Illinois 60637

Received 29 November 2005/ Accepted 19 January 2006

Staphylococcus simulans bv. staphylolyticus secretes lysostaphin, a bacteriocin that cleaves pentaglycine cross bridges in the cell wall of Staphylococcus aureus. The C-terminal cell wall-targeting domain (CWT) of lysostaphin is required for selective binding of this bacteriocin to S. aureus cells; however, the molecular target for this was unknown. We used purified green fluorescent protein fused to CWT (GFP-CWT) to reveal species-specific association of the reporter with staphylococci. GFP-CWT bound S. aureus cells as well as purified peptidoglycan sacculi. The addition of cross-linked murein, disaccharides linked to interconnected wall peptides, blocked GFP-CWT binding to staphylococci, whereas murein monomers or lysostaphin-solubilized cell wall fragments did not. S. aureus strain Newman variants lacking the capacity for synthesizing polysaccharide capsule (capFO), poly-N-acetylglucosamine (icaAC), lipoprotein (lgt), cell wall-anchored proteins (srtA), or the glycolipid anchor of lipoteichoic acid (ypfP) bound GFP-CWT similar to wild-type staphylococci. A tagO mutant strain, defective in the synthesis of polyribitol wall teichoic acid attached to the cell wall envelope, displayed increased GFP-CWT binding. In contrast, a femAB mutation, reducing both the amount and the length of peptidoglycan cross-linking (monoglycine cross bridges), showed a dramatic reduction in GFP-CWT binding. Thus, the CWT domain of lysostaphin directs the bacteriocin to cross-linked peptidoglycan, which also serves as the substrate for its glycyl-glycine endopeptidase domain.

* Corresponding author. Mailing address: Department of Microbiology, 920 E. 58th St., Chicago, IL 60637. Phone: (773) 843-9060. Fax: (773) 834-8150. E-mail: oschnee{at}bsd.uchicago.edu.

{dagger} Supplemental material for this article may be found at http://jb.asm.org/.

Journal of Bacteriology, April 2006, p. 2463-2472, Vol. 188, No. 7
0021-9193/06/$08.00+0     doi:10.1128/JB.188.7.2463-2472.2006
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Gargis, S. R., Gargis, A. S., Heath, H. E., Heath, L. S., LeBlanc, P. A., Senn, M. M., Berger-Bachi, B., Simmonds, R. S., Sloan, G. L. (2009). Zif, the Zoocin A Immunity Factor, Is a FemABX-Like Immunity Protein with a Novel Mode of Action. Appl. Environ. Microbiol. 75: 6205-6210 [Abstract] [Full Text]  
  • Beltramini, A. M., Mukhopadhyay, C. D., Pancholi, V. (2009). Modulation of Cell Wall Structure and Antimicrobial Susceptibility by a Staphylococcus aureus Eukaryote-Like Serine/Threonine Kinase and Phosphatase. Infect. Immun. 77: 1406-1416 [Abstract] [Full Text]  
  • Meredith, T. C., Swoboda, J. G., Walker, S. (2008). Late-Stage Polyribitol Phosphate Wall Teichoic Acid Biosynthesis in Staphylococcus aureus. J. Bacteriol. 190: 3046-3056 [Abstract] [Full Text]  
  • Seo, H. S., Michalek, S. M., Nahm, M. H. (2008). Lipoteichoic Acid Is Important in Innate Immune Responses to Gram-Positive Bacteria. Infect. Immun. 76: 206-213 [Abstract] [Full Text]  
  • Ikeda, R., Saito, F., Matsuo, M., Kurokawa, K., Sekimizu, K., Yamaguchi, M., Kawamoto, S. (2007). Contribution of the Mannan Backbone of Cryptococcal Glucuronoxylomannan and a Glycolytic Enzyme of Staphylococcus aureus to Contact-Mediated Killing of Cryptococcus neoformans. J. Bacteriol. 189: 4815-4826 [Abstract] [Full Text]  
  • Grundling, A., Schneewind, O. (2007). Genes Required for Glycolipid Synthesis and Lipoteichoic Acid Anchoring in Staphylococcus aureus. J. Bacteriol. 189: 2521-2530 [Abstract] [Full Text]  
  • Sass, P., Bierbaum, G. (2007). Lytic Activity of Recombinant Bacteriophage {phi}11 and {phi}12 Endolysins on Whole Cells and Biofilms of Staphylococcus aureus. Appl. Environ. Microbiol. 73: 347-352 [Abstract] [Full Text]  
  • Grundling, A., Missiakas, D. M., Schneewind, O. (2006). Staphylococcus aureus Mutants with Increased Lysostaphin Resistance.. J. Bacteriol. 188: 6286-6297 [Abstract] [Full Text]  


Copyright © 2009 by the American Society for Microbiology.   For an alternate route to Journals.ASM.org, visit: http://intl-journals.asm.org | More Info»