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Antimicrobial Agents and Chemotherapy, August 2006, p. 2608-2620, Vol. 50, No. 8
0066-4804/06/$08.00+0     doi:10.1128/AAC.00181-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

Naturally Processed Dermcidin-Derived Peptides Do Not Permeabilize Bacterial Membranes and Kill Microorganisms Irrespective of Their Charge

H. Steffen,1 S. Rieg,1 I. Wiedemann,2 H. Kalbacher,3 M. Deeg,4 H.-G. Sahl,2 A. Peschel,5 F. Götz,6 C. Garbe,1 and B. Schittek1*

Department of Dermatology, Eberhard-Karls-University of Tübingen, Tübingen, Germany,1 Institute for Medical Microbiology and Immunology, Rheinische Friedrich-Wilhelms-University Bonn, Germany,2 Medical and Natural Sciences Research Center, Eberhard-Karls-University of Tübingen, Tübingen, Germany,3 Section for Transplantation Immunology and Immunohematology, Eberhard-Karls-University of Tübingen, Tübingen, Germany,4 Cellular and Molecular Microbiology, Medical Microbiology and Hygiene Department, Eberhard-Karls-University of Tübingen, Tübingen, Germany,5 Microbial Genetics, Eberhard-Karls-University of Tübingen, Tübingen, Germany6

Received 2 February 2006/ Returned for modification 14 April 2006/ Accepted 11 May 2006

Dermcidin (DCD) is a recently described antimicrobial peptide, which is constitutively expressed in eccrine sweat glands and transported via sweat to the epidermal surface. By postsecretory proteolytic processing in sweat the dermcidin protein gives rise to several truncated DCD peptides which differ in length and net charge. In order to understand the mechanism of antimicrobial activity, we analyzed the spectrum of activity of several naturally processed dermcidin-derived peptides, the secondary structure in different solvents, and the ability of these peptides to interact with or permeabilize the bacterial membrane. Interestingly, although all naturally processed DCD peptides can adopt an {alpha}-helical conformation in solvents, they have a diverse and partially overlapping spectrum of activity against gram-positive and gram-negative bacteria. This indicates that the net charge and the secondary structure of the peptides are not important for the toxic activity. Furthermore, using carboxyfluorescein-loaded liposomes, membrane permeability studies and electron microscopy we investigated whether DCD peptides are able to permeabilize bacterial membranes. The data convincingly show that irrespective of charge the different DCD peptides are not able to permeabilize bacterial membranes. However, bacterial mutants lacking specific cell envelope modifications exhibited different susceptibilities to killing by DCD peptides than wild-type bacterial strains. Finally, immunoelectron microscopy studies indicated that DCD peptides are able to bind to the bacterial surface; however, signs of membrane perturbation were not observed. These studies indicate that DCD peptides do not exert their activity by permeabilizing bacterial membranes.

* Corresponding author. Mailing address: Department of Dermatology, Eberhard-Karls-University Tübingen, Liebermeisterstr. 25, D-72076 Tübingen, Germany. Phone: 49-7071-2980832. Fax: 49-7071-295187. E-mail: birgit.schittek{at}med.uni-tuebingen.de.

Antimicrobial Agents and Chemotherapy, August 2006, p. 2608-2620, Vol. 50, No. 8
0066-4804/06/$08.00+0     doi:10.1128/AAC.00181-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Senyurek, I., Paulmann, M., Sinnberg, T., Kalbacher, H., Deeg, M., Gutsmann, T., Hermes, M., Kohler, T., Gotz, F., Wolz, C., Peschel, A., Schittek, B. (2009). Dermcidin-Derived Peptides Show a Different Mode of Action than the Cathelicidin LL-37 against Staphylococcus aureus. Antimicrob. Agents Chemother. 53: 2499-2509 [Abstract] [Full Text]  


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