The phosphoenolpyruvate:sugar phosphotransferase system is involved in sensitivity to the glucosylated bacteriocin sublancin

C V Garcia De Gonzalo, E L Denham, R A T Mars, J Stülke, W A van der Donk, J M van Dijl

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The mode of action of a group of glycosylated antimicrobial peptides known as glycocins remains to be elucidated. In the current study of one glycocin, sublancin, we identified the phosphoenolpyruvate:sugar phosphotransferase system (PTS) of Bacillus species as a key player in bacterial sensitivity. Sublancin kills several Gram-positive bacteria, such as Bacillus species and Staphylococcus aureus, including methicillin-resistant S. aureus (MRSA). Unlike other classes of bacteriocins for which the PTS is involved in their mechanism of action, we show that the addition of PTS-requiring sugars leads to increased resistance rather than increased sensitivity, suggesting that sublancin has a distinct mechanism of action. Collectively, our present mutagenesis and genomic studies demonstrate that the histidine-containing phosphocarrier protein (HPr) and domain A of enzyme II (PtsG) in particular are critical determinants for bacterial sensitivity to sublancin.

Original languageEnglish
Pages (from-to)6844-6854
Number of pages11
JournalAntimicrobial Agents and Chemotherapy
Issue number11
Publication statusPublished - Nov 2015


  • Bacillus/drug effects
  • Bacteriocins/pharmacology
  • Glycopeptides/pharmacology
  • Microbial Sensitivity Tests
  • Phosphoenolpyruvate Sugar Phosphotransferase System/genetics
  • Polymorphism, Single Nucleotide/genetics

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