15-MER PEPTIDE DERIVED FROM THE NH2-TERMINUS OF THE SUBCLASS IIA BACTERIOCIN ENTEROCIN CRL35 SHOWS ANTIMICROBIAL ACTIVITY

SALVUCCI E.; SESMA F.

Nantes, Francia

Simposio; First International Symposium on antimicrobial peptides. Food, Veterinary, and Medical Applications; 2006

Enitiaa, Nantes

A 15-mer peptide derived from the NH2-terminus of the subClass IIa bacteriocin enterocin CRL35 shows antimicrobial activity Salvucci E., Sesma F.* Centro de Referencia para Lactobacilos (CERELA-CONICET) Chacabuco 145, (T4000ILC) S.M. de Tucumán, Tucumán, Argentina. Key Words: Subclass IIa bacteriocins, enterocin CRL35, short peptide, Listeria. Subclass IIa bacteriocins produced by food grade lactic acid bacteria (LAB) have antilisterial activity and it is commonly accepted that they exert bactericidal activity by permeabilizing the cell membrane (2,5,8). The ecological function of these ribosomally synthesized antimicrobial peptides is not yet fully understood (7). These compounds share a YGNGVxCxxxxC consensus in the amino terminal; however, the C-terminal domains are somewhat more diverse which allows subclass IIa antimicrobials to be subdivided into three subgroups (2,6). In attempts to elucidate the structure-function of pediocin-like bacteriocins we examined the inhibitory activity of a short peptide derived from N-terminal sequence of enterocin CRL35, a class IIa bacteriocin produced by Enterococcus mundtii CRL35. The antimicrobial activity in complex and chemically defined mediums was also evaluated.