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Antimicrobial Agents and Chemotherapy, July 2004, p. 2778-2781, Vol. 48, No. 7
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.7.2778-2781.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

Enhancement of the Enterocin CRL35 Activity by a Synthetic Peptide Derived from the NH2-Terminal Sequence

Lucila Saavedra,1 Carlos Minahk,2 Aída P. de Ruiz Holgado,1 and Fernando Sesma1*

Centro de Referencia para Lactobacilos (CERELA-CONICET), S.M. de Tucumán (4000),1 Instituto Superior de Investigaciones Biológicas, Instituto de Química Biológica "Dr. Bernabé Bloj," Facultad de Bioquímica, Química y Farmacia (UNT-CONICET), Tucumán, Argentina2

Received 4 November 2003/ Returned for modification 22 December 2003/ Accepted 8 March 2004

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.

* Corresponding author. Mailing address: Centro de Referencia para Lactobacilos (CERELA-CONICET), S.M. de Tucumán (4000), Chacabuco 145, Tucumán, Argentina. Phone: 54-381-431-1720. Fax: 54-381-400-5600. E-mail: fsesma{at}cerela.org.ar.

Antimicrobial Agents and Chemotherapy, July 2004, p. 2778-2781, Vol. 48, No. 7
0066-4804/04/$08.00+0     DOI: 10.1128/AAC.48.7.2778-2781.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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