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 specifi
cally and constitutively expressed in the sweat glands, secreted into the s
weat and transported to the epidermal surface. In sweat, a proteolytically
processed 47-amino acid peptide was generated that showed antimicrobial act
ivity in response to a variety of pathogenic microorganisms. The activity o
f the peptide was maintained over a broad pH range and in high salt concent
rations that resembled the conditions in human sweat. This indicated that s
weat plays a role in the regulation of human skin flora through the presenc
e of an antimicrobial peptide. This peptide may help limit infection by pot
ential pathogens in the first few hours following bacterial colonization.