Fusion of fungicidal peptide dhvar4 to enterococcal peptide pheromone increases its bactericidal activity against Enterococcus faecalis.

Bacterial peptide pheromone has a high affinity to its membrane receptor. Fusion of these peptides to pore-forming antimicrobial peptide might enhance its bactericidal activity against pheromone-sensing bacteria. We constructed two chimeric peptides by fusing the pore-forming fungicidal peptide dhvar4 to the C-terminus of enterococcal peptide pheromones cCF10 and cOB1 individually. Comparison on the bactericidal activities against pheromone-sensing bacteria Enterococcus faecalis demonstrates that the chimeric peptides cCF10-dhvar4 and cOB1-dhvar4 are more potent than the parent peptide dhvar4. The LD(50)s of both chimeric peptides (1.0 microm) are 10 times lower than that of dhvar4 (10.8 microm). Free peptide pheromone could inhibit E. faecalis killing mediated by both chimeric peptides. As same as that of the parent peptide, both chimeric peptides kill bacteria by disrupting its cell membrane. These results indicate that fused enterococcal peptide pheromone increases the bactericidal activity of fungicidal peptide against E. faecalis by improving its ability to reach the cell membrane.