Bactericidal thurincin H causes unique morphological changes in Bacillus cereus F4552 without affecting membrane permeability.

@article{Wang2014BactericidalTH,
  title={Bactericidal thurincin H causes unique morphological changes in Bacillus cereus F4552 without affecting membrane permeability.},
  author={Gaoyan Wang and Guoping Feng and Abigail B Snyder and David C. Manns and John J Churey and Randy W Worobo},
  journal={FEMS microbiology letters},
  year={2014},
  volume={357 1},
  pages={69-76}
}
Thurincin H is an antilisterial bacteriocin produced by Bacillus thuringiensis SF361. It exhibits inhibitory activity against a wide range of Gram-positive foodborne pathogens and spoilage bacteria including Listeria monocytogenes, B. cereus, and B. subtilis. This hydrophobic, anionic bacteriocin folds into a hairpin structure maintained by four pairs of unique sulfur to α-carbon thioether bonds. As its hydrophobicity and structure are quite different from most archived bacteriocins, this study… CONTINUE READING