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We purified three proline-rich antimicrobial peptides from elastase-treated extracts of sheep and goat leukocytes and subjected two of them, OaBac5α and ChBac5, to detailed analysis. OaBac5α and ChBac5 were homologous to each other and to bovine Bac5. Both exhibited potent, broad-spectrum antimicrobial activity under low-concentration salt conditions. While the peptides remained active againstEscherichia coli ,Pseudomonas aeruginosa ,Bacillus subtilis , andListeria monocytogenes in 100 mM NaCl, they lost activity againstStaphylococcus aureus andCandida albicans under these conditions. ChBac5 was shown to bind lipopolysaccharide, a property that could enhance its ability to kill gram-negative bacteria. Proline-rich Bac5 peptides are highly conserved in ruminants and may contribute significantly to their innate host defense mechanisms.

Purification and Properties of Proline-Rich Antimicrobial Peptides from Sheep and Goat Leukocytes