Short peptides derived from NH2-terminus of subClass IIa bacteriocin enterocin CRL35 show antimicrobial activity.

SALVUCCI E.; SAAVEDRA L; SESMA F.

JOURNAL OF ANTIMICROBIAL CHEMOTHERAPY

Oxford University Press

Año: 2007 vol. 59 p. 1102 - 1108

0305-7453

Enterocin CRL35 is a 43-aa heat stable peptide with antilisterial activity. It belongs tosubclass IIa bacteriocins characterized by a hydrophilic N-terminal domain which shares anYGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Short syntheticpeptides derived from the N-terminal half of divercin V41, enterocin A and enterocin CRL35were evaluated for antimicrobial properties. A 15-mer peptide fragment derived fromenterocin CRL35 inhibited the growth of Listeria innocua and Listeria monocytogenes insinthetical/minimal media and dissipated the membrane potential of sensitive cells.