A Novel C-Terminal Truncated Bacteriocin Found by Comparison between Leuconostoc mesenteroides 406 and 213M0 Isolated from Mongolian Traditional Fermented Milk, Airag

Author:

Hasiqimuge 12,Hano Chihiro1,Arakawa Kensuke1,Yoshida Saki1,Zhao Junliang13,Toh Hidehiro4,Morita Hidetoshi1,Miyamoto Taku1567

Affiliation:

1. Graduate School of Environmental and Life Science, Okayama University, Okayama 7008530, Japan

2. Department of Grassland Ecology, Animal Husbandry and Veterinary, Xilingol Vocational College, Xilinhot 026000, China

3. Faculty of Agriculture, Kagawa University, Kagawa 7610795, Japan

4. Advanced Genomics Center, National Institute of Genetics, Mishima 4118540, Japan

5. Faculty of Food Culture, Kurashiki Sakuyo University, Okayama 7100292, Japan

6. Microbial Fermentation Research Center, Minori Co., Ltd., Okayama 7011221, Japan

7. Functional Food Creation Research Institute Co., Ltd., Okayama 7161241, Japan

Abstract

Bacteriocins produced by lactic acid bacteria are known to be useful tools for food biopreservation and fermentation control. Leuconostoc mesenteroides subsp. mesenteroides 406 and 213M0 isolated from different samples of Mongolian traditional fermented milk, airag, had been reported to produce listericidal bacteriocin-like inhibitory substances with similar but slightly different properties. In this study, the antibacterial properties and the related gene sequences of both strains were compared, and then their bacteriocins were purified and identified. Strain 406 was superior to strain 213M0 in cell growth and antibacterial activity against many strains. However, the activity of 213M0 was stronger than that of 406 against a few strains. DNA sequencing revealed two and three plasmids in 406 and 213M0, respectively, and each one of them harbored an almost identical mesentericin Y105–B105 gene cluster. Removal of these plasmids resulted in a complete loss of activity, indicating that the antibacterial activity of both strains was generated by bacteriocins encoded on the plasmids. Mesentericins Y105 and B105 were purified from both cultures, and another novel bacteriocin, named mesentericin M, was identified from the 213M0 culture only. Its structural gene was coded on a 213M0 plasmid and, surprisingly, its C-terminal three amino acid residues were post-translationally cleaved. To our knowledge, this is the first report of a C-terminal truncated bacteriocin. In conclusion, the novel bacteriocin should be mainly responsible for the difference in antibacterial properties between the two strains.

Funder

JSPS KAKENHI

Laboratory of Animal Applied Microbiology, Faculty of Agriculture, Okayama University

Publisher

MDPI AG

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