Abstract
Antimicrobial peptides are an important component of the innate response in many species. Here we describe the isolation of the gene Dermcidin, which encodes an antimicrobial peptide that has a broad spectrum of activity and no homology to other known antimicrobial peptides. This protein was specifically and constitutively expressed in the sweat glands, secreted into the sweat and transported to the epidermal surface. In sweat, a proteolytically processed 47–amino acid peptide was generated that showed antimicrobial activity in response to a variety of pathogenic microorganisms. The activity of the peptide was maintained over a broad pH range and in high salt concentrations that resembled the conditions in human sweat. This indicated that sweat plays a role in the regulation of human skin flora through the presence of an antimicrobial peptide. This peptide may help limit infection by potential pathogens in the first few hours following bacterial colonization.
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Acknowledgements
We thank T. Iftner and colleagues for DNA sequencing; M. Schwarz and colleagues for the use of radioisotopes and Phosphorimager; B. Fehrenbacher and H. Bischof for electron microscopy; A. Nordheim for mass spectrometry; E. Maczey for technical assistance; and P. Gött, T. Paul, M. Stark and F. Lang for discussions. Supported by the Fortüne-program of the Eberhard-Karls-University Tübingen (432-0-1), the Bundesministerium für Bildung und Forschung (IZKF, Fö01KS9602) and the Deutsche Forschungsgemeinschaft (SFB510).
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Web Figure 1.
Sequence of DCD. (a) Full-length cDNA of DCD (458 bp). Exons, positions of introns, start and stop codons are indicated. UTS: untranslated regions. (b) Predicted amino acid sequence of DCD. (GIF 14 kb)
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Schittek, B., Hipfel, R., Sauer, B. et al. Dermcidin: a novel human antibiotic peptide secreted by sweat glands. Nat Immunol 2, 1133–1137 (2001). https://doi.org/10.1038/ni732
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DOI: https://doi.org/10.1038/ni732
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