Enhancement of the Enterocin CRL35 Activity by a Synthetic Peptide

LUCILA SAAVEDRA,1 CARLOS MINAHK,2 AÍDA P. DE RUIZ HOLGADO,1 AND FERNANDO SESMA1*

ANTIMICROBIAL AGENTS AND CHEMOTHERAPY

Año: 2004 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