Enhancement of the enterocin CRL35 activity by a synthetic peptide derived from the NH2-terminal sequence.

SAAVEDRA, M. L.; MINAHK, C; DE RUIZ HOLGADO, A.; SESMA, F.

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY

American Society for Microbiology

Año: 2004 vol. 48 p. 2778 - 2781

0066-4804

The enterocin CRL35 biosynthetic gene cluster was cloned and sequenced. The sequence was revealed to be highly identical to that of the mundticin KS gene cluster (S. Kawamoto, J. Shima, R. Sato, T. Eguchi, S. Ohmomo, J. Shibato, N. Horikoshi, K. Takeshita, and T. Sameshima, Appl. Environ. Microbiol. 68:3830-3840, 2002). Short synthetic peptides were designed based on the bacteriocin sequence and were evaluated in antimicrobial competitive assays. The peptide KYYGNGVSCNKKGCS produced an enhancement of enterocin CRL35 antimicrobial activity in a buffer system.