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

Antimicrob Agents Chemother. 2015 Nov;59(11):6844-54. doi: 10.1128/AAC.01519-15. Epub 2015 Aug 17.


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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

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


  • Bacteriocins
  • Glycopeptides
  • Phosphoenolpyruvate Sugar Phosphotransferase System
  • phosphoenolpyruvate-glucose phosphotransferase