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Day 3, June 24(Tue.)
Room P (Maesato East, Foyer, Ocean Wing)
- 3P-PM-36
Investigation of the Antimicrobial Activity of Lactobacillus sp. SC-2001 Strain Isolated from Quercus serrata
(Sumitomo Chemical)
oYumi Komori, Naoya Ozawa, Hiroshi Kuwahara, Mikio Aoki
We have identified and characterized a novel ClassⅡ bacteriocin, lactobacin A, from Lactobacillus sp. SC-2001. The structure of lactobacin A was determined through a three-step purification, LC/MS/MS amino acid sequencing analysis and confirmation by RNA sequencing analysis of the coding gene. Lactobacin A was an entirely a novel non-pediocin-like, single-peptide bacteriocin with low similarity to known bacteriocins. Two genes adjacent to the lactobacin A gene encode ATP-binding cassette transporters, which might be involved in leader peptide cleavage/transport and self-immunity. Antibacterial assay of synthetic peptides suggested its N-terminal sequence involved in the activities. Lactobacin A showed remarkable stability over a wide range of pH levels, at elevated temperatures, and in oxidative environments. These results suggest that lactobacin A is a promising candidate for the development of new antimicrobial agents.