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 Vaudaux, P. E.
Right arrow Articles by Berger-Bächi, B.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Vaudaux, P. E.
Right arrow Articles by Berger-Bächi, B.

 Previous Article  |  Next Article 

Antimicrobial Agents and Chemotherapy, March 1998, p. 564-570, Vol. 42, No. 3
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.

Introduction of the mec Element (Methicillin Resistance) into Staphylococcus aureus Alters In Vitro Functional Activities of Fibrinogen and Fibronectin Adhesins

Pierre E. Vaudaux,1,* Vincenza Monzillo,1,dagger Patrice Francois,1 Daniel P. Lew,1 Tim J. Foster,2 and Brigitte Berger-Bächi3

Division of Infectious Diseases, University Hospital, Geneva,1 and Institute of Medical Microbiology, University of Zürich, Zürich,3 Switzerland, and Microbiology Department, Moyne Institute, Trinity College, Dublin 2, Ireland2

Received 10 June 1997/Returned for modification 20 September 1997/Accepted 7 January 1998

Some methicillin-resistant strains of Staphylococcus aureus are defective in the production of major surface components such as protein A, clumping factor, or other important adhesins to extracellular matrix components which may play a role in bacterial colonization and infection. To evaluate the impact of methicillin resistance (mec) determinants on bacterial adhesion mediated by fibrinogen or fibronectin adhesins, we compared the in vitro attachment of two genetically distinct susceptible strains (NCTC8325 and Newman) to protein-coated surfaces with that of isogenic methicillin-resistant derivatives. All strains containing an intact mec element in their chromosomes were found to be defective in adhesion to fibrinogen and fibronectin immobilized on polymethylmethacrylate coverslips, regardless of the presence or absence of additional mutations in the femA, femB, or femC gene, known to decrease expression of methicillin resistance in S. aureus. Western ligand affinity blotting or immunoblotting of cell wall-associated adhesins revealed similar contents of fibrinogen- or fibronectin-binding proteins in methicillin-resistant strains compared to those of their methicillin-susceptible counterparts. In contrast to methicillin-resistant strains carrying a mec element in their genomes, methicillin-resistant strains constructed in vitro, by introducing the mecA gene on a plasmid, retained their adhesion phenotypes. In conclusion, the chromosomal insertion of the mec element into genetically defined strains of S. aureus impairs the in vitro functional activities of fibrinogen or fibronectin adhesins without altering their production. This effect is unrelated to the activity of the mecA gene.

* Corresponding author. Mailing address: Division of Infectious Diseases, University Hospital, CH 1211 Geneva 14, Switzerland. Phone: (4122) 37 29 826. Fax: (4122) 37 29 830. E-mail: vaudaux{at}dminov1.hcuge.ch.

dagger Present address: Laboratorio di Batteriologica, Istituto di Clinica di Malattie Infettive, Pavia, Italy.

Antimicrobial Agents and Chemotherapy, March 1998, p. 564-570, Vol. 42, No. 3
0066-4804/98/$04.00+0
Copyright © 1998, American Society for Microbiology. All rights reserved.


This article has been cited by other articles:

  • Dancer, S. J. (2008). The effect of antibiotics on methicillin-resistant Staphylococcus aureus. J Antimicrob Chemother 61: 246-253 [Abstract] [Full Text]  
  • Luczak-Kadlubowska, A., Krzyszton-Russjan, J., Hryniewicz, W. (2006). Characteristics of Staphylococcus aureus Strains Isolated in Poland in 1996 to 2004 That Were Deficient in Species-Specific Proteins. J. Clin. Microbiol. 44: 4018-4024 [Abstract] [Full Text]  
  • Li, D., Renzoni, A., Estoppey, T., Bisognano, C., Francois, P., Kelley, W. L., Lew, D. P., Schrenzel, J., Vaudaux, P. (2005). Induction of Fibronectin Adhesins in Quinolone-Resistant Staphylococcus aureus by Subinhibitory Levels of Ciprofloxacin or by Sigma B Transcription Factor Activity Is Mediated by Two Separate Pathways. Antimicrob. Agents Chemother. 49: 916-924 [Abstract] [Full Text]  
  • Grundmeier, M., Hussain, M., Becker, P., Heilmann, C., Peters, G., Sinha, B. (2004). Truncation of Fibronectin-Binding Proteins in Staphylococcus aureus Strain Newman Leads to Deficient Adherence and Host Cell Invasion Due to Loss of the Cell Wall Anchor Function. Infect. Immun. 72: 7155-7163 [Abstract] [Full Text]  
  • Roche, F. M., Downer, R., Keane, F., Speziale, P., Park, P. W., Foster, T. J. (2004). The N-terminal A Domain of Fibronectin-binding Proteins A and B Promotes Adhesion of Staphylococcus aureus to Elastin. J. Biol. Chem. 279: 38433-38440 [Abstract] [Full Text]  
  • Kruszewska, D., Sahl, H.-G., Bierbaum, G., Pag, U., Hynes, S. O., Ljungh, A. (2004). Mersacidin eradicates methicillin-resistant Staphylococcus aureus (MRSA) in a mouse rhinitis model. J Antimicrob Chemother 54: 648-653 [Abstract] [Full Text]  
  • Renzoni, A., Francois, P., Li, D., Kelley, W. L., Lew, D. P., Vaudaux, P., Schrenzel, J. (2004). Modulation of Fibronectin Adhesins and Other Virulence Factors in a Teicoplanin-Resistant Derivative of Methicillin-Resistant Staphylococcus aureus. Antimicrob. Agents Chemother. 48: 2958-2965 [Abstract] [Full Text]  
  • Bisognano, C., Kelley, W. L., Estoppey, T., Francois, P., Schrenzel, J., Li, D., Lew, D. P., Hooper, D. C., Cheung, A. L., Vaudaux, P. (2004). A RecA-LexA-dependent Pathway Mediates Ciprofloxacin-induced Fibronectin Binding in Staphylococcus aureus. J. Biol. Chem. 279: 9064-9071 [Abstract] [Full Text]  
  • Katayama, Y., Takeuchi, F., Ito, T., Ma, X. X., Ui-Mizutani, Y., Kobayashi, I., Hiramatsu, K. (2003). Identification in Methicillin-Susceptible Staphylococcus hominis of an Active Primordial Mobile Genetic Element for the Staphylococcal Cassette Chromosome mec of Methicillin-Resistant Staphylococcus aureus. J. Bacteriol. 185: 2711-2722 [Abstract] [Full Text]  
  • Vaudaux, P., Francois, P., Bisognano, C., Kelley, W. L., Lew, D. P., Schrenzel, J., Proctor, R. A., McNamara, P. J., Peters, G., Von Eiff, C. (2002). Increased Expression of Clumping Factor and Fibronectin-Binding Proteins by hemB Mutants of Staphylococcus aureus Expressing Small Colony Variant Phenotypes. Infect. Immun. 70: 5428-5437 [Abstract] [Full Text]  
  • Ma, X. X., Ito, T., Tiensasitorn, C., Jamklang, M., Chongtrakool, P., Boyle-Vavra, S., Daum, R. S., Hiramatsu, K. (2002). Novel Type of Staphylococcal Cassette Chromosome mec Identified in Community-Acquired Methicillin-Resistant Staphylococcus aureus Strains. Antimicrob. Agents Chemother. 46: 1147-1152 [Abstract] [Full Text]  
  • Savolainen, K., Paulin, L., Westerlund-Wikstrom, B., Foster, T. J., Korhonen, T. K., Kuusela, P. (2001). Expression of pls, a Gene Closely Associated with the mecA Gene of Methicillin-Resistant Staphylococcus aureus, Prevents Bacterial Adhesion In Vitro. Infect. Immun. 69: 3013-3020 [Abstract] [Full Text]  
  • Bisognano, C., Vaudaux, P., Rohner, P., Lew, D. P., Hooper, D. C. (2000). Induction of Fibronectin-Binding Proteins and Increased Adhesion of Quinolone-Resistant Staphylococcus aureus by Subinhibitory Levels of Ciprofloxacin. Antimicrob. Agents Chemother. 44: 1428-1437 [Abstract] [Full Text]  
  • Peacock, S. J., Lina, G., Etienne, J., Foster, T. J. (1999). Staphylococcus schleiferi subsp. schleiferi Expresses a Fibronectin-Binding Protein. Infect. Immun. 67: 4272-4275 [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»