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Applied and Environmental Microbiology, December 2000, p. 5213-5220, Vol. 66, No. 12
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.

Biochemical and Genetic Characterization of Coagulin, a New Antilisterial Bacteriocin in the Pediocin Family of Bacteriocins, Produced by Bacillus coagulans I4

Claire Le Marrec,1,* Bertrand Hyronimus,1 Philippe Bressollier,2,3 Bernard Verneuil,3 and Maria C. Urdaci2

Unité Sécurité Microbiologique des Aliments, ISTAB, Université Bordeaux I, F-33405 Talence,1 Laboratoire de Microbiologie et de Biochimie Appliquées, ENITA de Bordeaux, F-33175 Gradignan,2 and Laboratoire de Génie Enzymatique et Biovalorisation, IUT, Département Génie Biologique F-87000, Limoges,3 France

Received 20 March 2000/Accepted 14 September 2000

A plasmid-linked antimicrobial peptide, named coagulin, produced by Bacillus coagulans I4 has recently been reported (B. Hyronimus, C. Le Marrec and M. C. Urdaci, J. Appl. Microbiol. 85:42-50, 1998). In the present study, the complete, unambiguous primary amino acid sequence of the peptide was obtained by a combination of both N-terminal sequencing of purified peptide and the complete sequence deduced from the structural gene harbored by plasmid I4. Data revealed that this peptide of 44 residues has an amino acid sequence similar to that described for pediocins AcH and PA-1, produced by different Pediococcus acidilactici strains and 100% identical. Coagulin and pediocin differed only by a single amino acid at their C terminus. Analysis of the genetic determinants revealed the presence, on the pI4 DNA, of the entire 3.5-kb operon of four genes described for pediocin AcH and PA-1 production. No extended homology was observed between pSMB74 from P. acidilactici and pI4 when analyzing the regions upstream and downstream of the operon. An oppositely oriented gene immediately dowstream of the bacteriocin operon specifies a 474-amino-acid protein which shows homology to Mob-Pre (plasmid recombination enzyme) proteins encoded by several small plasmids extracted from gram-positive bacteria. This is the first report of a pediocin-like peptide appearing naturally in a non-lactic acid bacterium genus.

* Corresponding author. Mailing address: Unité Sécurité Microbiologique des Aliments, ISTAB, Université Bordeaux I, Avenue des Facultés, F-33405 Talence, France. Phone: (33) 556 848 902. Fax: (33) 556 848 919. E-mail: lemarrec{at}istab.u-bordeaux.fr.

Applied and Environmental Microbiology, December 2000, p. 5213-5220, Vol. 66, No. 12
0099-2240/00/$04.00+0
Copyright © 2000, American Society for Microbiology. All rights reserved.


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