The Phosphoenolpyruvate:Sugar Phosphotransferase system is involved in sensitivity to the glucosylated bacteriocin sublancin.
Antimicrob Agents Chemother. 2015 Aug 17;
Authors: Garcia De Gonzalo CV, Denham EL, Mars RA, Stülke J, van der Donk WA, van Dijl JM
The mode of action of a group of glycosylated antimicrobial peptides known as glycocins remains to be elucidated. In the current study on 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 an increased sensitivity, suggesting that sublancin has a distinct mechanism of action. Collectively, our present mutagenesis and genomic studies demonstrate that, in particular, the histidine-containing phosphocarrier protein (HPr) and domain A of enzyme II (PtsG) are critical determinants for the bacterial sensitivity to sublancin.
PMID: 26282429 [PubMed - as supplied by publisher]