Defensins (alpha and beta) are cationic peptides with a broad spectrum of antimicrobial activity that comprise an important arm of the innate immune system. The ª-defensins are distinguished from the ß-defensins by the pairing of their three disulfide bonds. To date, four human ß-defensins have been identified; BD-1, BD-2, BD-3 and BD-4. ß-defensins are expressed on some leukocytes and at epithelial surfaces. In addition to their direct antimicrobial activities, they are chemoattractant towards immature dendritic cells and memory T cells. The ß-defensin proteins are expressed as the C-terminal portion of precursors and are released by proteolytic cleavage of a signal sequence and, in the case of BD-1 (36 a.a.), a propeptide region. ß-defensins contain a six-cysteine motif that forms three intra-molecular disulfide bonds. ß-Defensins are 3-5 kDa peptides ranging in size from 33-47 amino acid residues.