Literature DB >> 17449885

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

Emiliano Salvucci1, Lucila Saavedra, Fernando Sesma.   

Abstract

OBJECTIVES: Subclass IIa bacteriocins are characterized by a hydrophilic N-terminal domain that shares a YGNGVxCxxxxC consensus and a variable hydrophobic C-terminus. Enterocin CRL35 is a 43-amino-acid heat stable peptide with antilisterial activity. Short synthetic peptides derived from the N-terminal half of enterocin CRL35 and other subclass IIa bacteriocins were evaluated for antimicrobial properties.
METHODS: In vitro activities of synthetic peptides were evaluated in complex, chemically defined and minimal media. MIC assays were performed by the agar well-diffusion method. Fluorescence assays to evaluate the dissipation of membrane potentials in intact cells were carried out. Time-kill kinetics of Listeria innocua cells with the active peptide were performed. RESULTS AND
CONCLUSIONS: A 15-mer peptide derived from enterocin CRL35 inhibited the growth of L. innocua and Listeria monocytogenes in synthetic/minimal media and dissipated the membrane potential of sensitive cells, with MICs of 10 and 50 microM, respectively. 15-mer derivatives from other class IIa bacteriocins (mesentericin Y105, pediocin PA-1 and piscicolin 126) also showed antimicrobial activities.

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Year:  2007        PMID: 17449885     DOI: 10.1093/jac/dkm096

Source DB:  PubMed          Journal:  J Antimicrob Chemother        ISSN: 0305-7453            Impact factor:   5.790


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