CDNA SEQUENCES OF 3 SHEEP MYELOID CATHELICIDINS

Several myeloid antimicrobial peptide precursors have been shown to co nsist of a N-terminal proregion similar to a protein named cathelin an d a structurally varied C-terminal antimicrobial domain. Proteins with these features have been named cathelicidins. In this paper me report the cDNA sequences of three ovine cathelicidins of 155, 160 and 190 r esidues, respectively, with cationic C-terminal sequences correspondin g to putative antimicrobial domains. These are structurally varied and include a Cys-rich sequence of 12 residues, which is similar to the b ovine antimicrobial cyclic dodecapeptide, a novel 29 residue sequence named SMAP-29 with a possible alpha-helical conformation, and a 60 res idue sequence named Bac7.5, which appears to be a new member of the Pr o- and Arg-rich group of mammalian antimicrobial peptides.