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Few bacteriocins with antibacterial activity against  Shigella flexneri  have been reported. Here, a novel bacteriocin ( LFX01 ) produced by  Lactiplantibacillus plantarum  strain LF-8 from the intestine of tilapia was purified and extensively characterized.  LFX01  possesses a molecular weight of 1049.56 Da and an amino acid sequence of I-T-G-G-P-A-V-V-H-Q-A.  LFX01  significantly inhibited  S. flexneri  strain 14 ( S. flexneri _14) growth. Moreover, it exhibited excellent stability under heat and acid-base stress, and presented sensitivity to a variety of proteases, such as proteinase K, pepsin, and trypsin. The minimum inhibitory concentration (MIC) of  LFX01  against  S. flexneri _14 was 12.65 μg/mL, which was smaller than that of most of the previously found bacteriocins. Furthermore,  LFX01  significantly inhibited ( p  &amp;lt; 0.05)  S. flexneri _14 cells and decreased their cell viability. In addition,  LFX01  could significantly ( p  &amp;lt; 0.05) inhibit biofilm formation of  S. flexneri _14. Scanning electron microscopy analysis presented that the cell membrane permeability of  S. flexneri _14 was demolished by  LFX01 , leading to cytoplasmic contents leakage and cell rupture death. In summary, a novel bacteriocin of lactic acid bacteria (LAB) was found, which could effectively control  S. flexneri  in both planktonic and biofilm states.

frontiers in microbiology

A Novel Bacteriocin Against Shigella flexneri From Lactiplantibacillus plantarum Isolated From Tilapia Intestine: Purification, Antibacterial Properties and Antibiofilm Activity