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Resistance to dermcidin-derived peptides is independent of bacterial protease activity.

Authors :
Senyürek I
Döring G
Kalbacher H
Deeg M
Peschel A
Wolz C
Schittek B
Source :
International journal of antimicrobial agents [Int J Antimicrob Agents] 2009 Jul; Vol. 34 (1), pp. 86-90. Date of Electronic Publication: 2009 Feb 07.
Publication Year :
2009

Abstract

Dermcidin (DCD) is an antimicrobial peptide constitutively expressed in eccrine sweat glands in human skin. By post-secretory proteolytic processing in sweat, the DCD protein gives rise to anionic and cationic DCD peptides that are able to kill several Gram-positive and Gram-negative bacteria but are only weakly active against Pseudomonas aeruginosa. Here, we questioned whether bacterial resistance to DCD peptides is mediated by proteolytic degradation. It was shown that DCD-derived peptides are degraded by purified bacterial proteases and by extracellular proteases secreted by P. aeruginosa in a concentration-dependent manner. However, protease-deficient mutants of P. aeruginosa PAO1 lacking either lasA, lasB (elastase) or both showed a similar sensitivity towards DCD-derived peptides as the wild-type strain. Finally, inhibition of total protease activity indicated that proteases secreted by P. aeruginosa are not responsible for the poor activity of DCD-derived peptides against P. aeruginosa. These data suggest that the decreased sensitivity of P. aeruginosa to DCD-derived peptides is not mediated by proteolytic degradation under physiological conditions.

Details

Language :
English
ISSN :
1872-7913
Volume :
34
Issue :
1
Database :
MEDLINE
Journal :
International journal of antimicrobial agents
Publication Type :
Academic Journal
Accession number :
19201578
Full Text :
https://doi.org/10.1016/j.ijantimicag.2008.12.008