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Applied and Environmental Microbiology, September 2001, p. 4041-4047, Vol. 67, No. 9
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.9.4041-4047.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Identification of a New Plasmid-Encoded sec-Dependent Bacteriocin Produced by Listeria innocua 743

M. L. Kalmokoff,1,* S. K. Banerjee,1 T. Cyr,2 M. A. Hefford,2 and T. Gleeson3

Microbiology Research Division, Bureau of Microbial Hazards, Food Directorate, Health Protection Branch, 1 Research Services Division, Bureau of Biologics and Radiopharmaceuticals, Biologics and Genetics Directorate, Health Products and Foods Branch,2 and National Laboratory for HIV Genetics,3 Health Canada, Banting Research Centre, Tunney's Pasture, Ottawa, Ontario, Canada K1A 0L2

Received 26 January 2001/Accepted 15 June 2001

Listeria innocua 743 produces an inhibitory activity demonstrating broad-spectrum inhibition of Listeria monocytogenes isolates. Gel-electrophoretic analysis of culture supernatants indicated that two inhibitors with different molecular weights were produced by this strain. Insertion of Tn917 into a 2.9 Kb plasmid (pHC743) generated mutants with either an impaired ability or a loss in ability to produce one of the inhibitors. Sequence analysis of the transposon insertion regions revealed the presence of two continuous open reading frames, the first encoding a new pediocin-like bacteriocin (lisA) and the second encoding a protein homologous with genes involved in immunity toward other bacteriocins (lisB). Translation of the bacteriocin gene (lisA) initiates from a noncanonical start codon and encodes a 71-amino-acid prebacteriocin which lacked the double glycine leader peptidase processing site common in other type II bacteriocins. Alignment of the sequence with the processed N termini of related bacteriocins suggests that the mature bacteriocin consists of 43 amino acids, with a predicted molecular mass of 4,484 Da. Mutants containing insertions into lisA were sensitive to the inhibitor, indicating that lisAB forms a single operon and that lisB represents the immunity protein. Cloning of an amplicon containing the lisAB operon into Escherichia coli resulted in expression and export of the bacteriocin. This finding confirms that the phenotype is dependent on the structural and immunity gene only and that export of this bacteriocin is sec dependent. This is the first confirmation of bacteriocin production in a Listeria spp., and it is of interest that this bacteriocin is closely related to the pediocin family of bacteriocins produced by lactic acid bacteria.

* Corresponding author. Mailing address: Microbiology Research Division, Bureau of Microbial Hazards, Food Directorate, Health Protection Branch, Health Canada, Banting Research Centre, Tunney's Pasture, Ottawa, Ontario, Canada K1A 0L2. Phone: (613) 957-0903. Fax: (613) 941-0280. E-mail: Martin_Kalmokof{at}hc-sc.gc.ca.

Applied and Environmental Microbiology, September 2001, p. 4041-4047, Vol. 67, No. 9
0099-2240/01/$04.00+0   DOI: 10.1128/AEM.67.9.4041-4047.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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