This Article Full Text Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Reprints and Permissions Copyright Information Books from ASM Press MicrobeWorld Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Netz, D. J. A. Articles by Sahl, H.-G. Search for Related Content PubMed PubMed Citation Articles by Netz, D. J. A. Articles by Sahl, H.-G. Agricola Articles by Netz, D. J. A. Articles by Sahl, H.-G.

 Previous Article  |  Next Article 

Applied and Environmental Microbiology, November 2002, p. 5274-5280, Vol. 68, No. 11
0099-2240/02/$04.00+0     DOI: 10.1128/AEM.68.11.5274-5280.2002
Copyright © 2002, American Society for Microbiology. All Rights Reserved.

Mode of Action of the Antimicrobial Peptide Aureocin A53 from Staphylococcus aureus

Departamento de Microbiologia Geral, Instituto de Microbiologia, Universidade Federal do Rio de Janeiro, Rio de Janeiro, Brazil,¹ Institut für Medizinische Mikrobiologie und Immunologie, Universität Bonn, Bonn, Germany²

Received 21 March 2002/ Accepted 5 August 2002

We investigated the mode of action of aureocin A53 on living bacterial cells and model membranes. Aureocin A53 acted bactericidally against Staphylococcus simulans 22, with >90% of the cells killed within a few minutes. Cell death was followed by lysis, as indicated by a clearing of the cell suspension and Gram staining. Aureocin A53 rapidly dissipated the membrane potential and simultaneously stopped biosynthesis of DNA, polysaccharides, and protein. Aureocin A53 induced a rapid release of preaccumulated glutamate and Rb⁺. Experiments on model membranes demonstrated that aureocin A53 provoked significant leakage of carboxyfluorescein (CF) exclusively from acidic liposomes but only at relatively high concentrations (0.5 to 8 mol%). Thus, the bactericidal activity of aureocin A53 derives from membrane permeation via generalized membrane destruction rather than by formation of discrete pores within membranes. Tryptophan emission fluorescence spectroscopy demonstrated interaction of aureocin A53 with both acidic and neutral membranes, as indicated by similar blue shifts. Since there was no significant aureocin A53-induced CF leakage from neutral liposomes, its appears that the peptide does interact with neutral lipids without provoking membrane damage.

This article has been cited by other articles:

• Ventura, M., Canchaya, C., Tauch, A., Chandra, G., Fitzgerald, G. F., Chater, K. F., van Sinderen, D. (2007). Genomics of Actinobacteria: Tracing the Evolutionary History of an Ancient Phylum. Microbiol. Mol. Biol. Rev. 71: 495-548 [Abstract] [Full Text]  
• Fujita, K., Ichimasa, S., Zendo, T., Koga, S., Yoneyama, F., Nakayama, J., Sonomoto, K. (2007). Structural Analysis and Characterization of Lacticin Q, a Novel Bacteriocin Belonging to a New Family of Unmodified Bacteriocins of Gram-Positive Bacteria. Appl. Environ. Microbiol. 73: 2871-2877 [Abstract] [Full Text]  
• Sibbald, M. J. J. B., Ziebandt, A. K., Engelmann, S., Hecker, M., de Jong, A., Harmsen, H. J. M., Raangs, G. C., Stokroos, I., Arends, J. P., Dubois, J. Y. F., van Dijl, J. M. (2006). Mapping the Pathways to Staphylococcal Pathogenesis by Comparative Secretomics. Microbiol. Mol. Biol. Rev. 70: 755-788 [Abstract] [Full Text]