Mode of action of a novel anti-Listeria bacteriocin (CAMT2) produced by Bacillus amyloliquefaciens ZJHD3-06 from Epinephelus areolatus

Arch Microbiol. 2019 Jan;201(1):61-66. doi: 10.1007/s00203-018-1553-8. Epub 2018 Sep 10.

Abstract

Bacteriocin CAMT2, produced by Bacillus amyloliquefaciens ZJHD3-06, has been shown to exhibit protective activity against important food spoilage and food-borne bacterial pathogens. This study was conducted to investigate the mode of action of bacteriocin CAMT2 against highly pathogenic Listeria monocytogenes ATCC 19111. The addition of bacteriocin CAMT2 at 64 AU/ml inhibited L. monocytogenes ATCC 19111. An efflux of K+ ions, lactic acid dehydrogenase and an increase in extracellular electrical conductivity was observed in CAMT2-treated L. monocytogenes. Electron microscopy showed morphological alterations such as uneven cell surface, accumulation of cell debris and bacterial lysis. These results show that bacteriocin CAMT2 inhibit L. monocytogenes by increasing cell permeability and inducing membrane damage, hence it has the great application potentials in ensuring food safety.

Keywords: Bacteriocin CAMT2; Cytoplasmic membrane damage; Listeria monocytogenes; Mode of action.

MeSH terms

  • Animals
  • Anti-Bacterial Agents / metabolism
  • Anti-Bacterial Agents / pharmacology*
  • Bacillus amyloliquefaciens / metabolism*
  • Bacteriocins / metabolism
  • Bacteriocins / pharmacology*
  • Cell Membrane / drug effects*
  • Electric Conductivity
  • L-Lactate Dehydrogenase / metabolism
  • Listeria monocytogenes / drug effects*
  • Listeria monocytogenes / metabolism
  • Microbial Sensitivity Tests
  • Perciformes / microbiology*
  • Permeability / drug effects*
  • Potassium / metabolism
  • Protein Transport / drug effects

Substances

  • Anti-Bacterial Agents
  • Bacteriocins
  • L-Lactate Dehydrogenase
  • Potassium