Pheromone-induced production of antimicrobial peptides in Lactobacillus.

Production of the bacteriocin sakacin P by Lactobacillus sake LTH673 is dependent on a secreted 19-residue peptide pheromone (IP-673). The gene encoding IP-673 (sppIP) was identified and sequenced. SppIP was shown to be co-transcribed with genes encoding a histidine kinase (sppK) and a response regulator (sppR) typical for signal transduction in bacteria. Further sequencing and transcription studies have shown that IP-673 induces transcription of its own gene and of what are often considered to be all genes necessary for bacteriocin production and immunity. Studies with a reporter gene showed that the promoter in front of the sakacin P structural gene (sppA) is strictly regulated. The promoter in front of sppIP turned out to be less strictly regulated, and low basal promoter activity could be detected in uninduced cells. Bacteriocin production in Bac isolates of L. plantarum C11 could be induced by the non-cognate IP-673 only after the introduction of sppK, indicating that sppK encodes the pheromone receptor. These results show that bacteriocin production in lactobacilli is regulated using a short, strain-specific peptide pheromone. Growth conditions were shown to have considerable effects on the functionality of this regulatory mechanism.