The Phosphoenolpyruvate: Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin SublancinDe Gonzalo, C. V. G., Denham, E. L., Mars, R. A. T., Stuelke, J., van der Donk, W. A. & van Dijl, J. M., Nov-2015, In : Antimicrobial Agents and Chemotherapy. 59, 11, p. 6844-6854 11 p.
Research output: Contribution to journal › Article › Academic › peer-review
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.
|Number of pages||11|
|Journal||Antimicrobial Agents and Chemotherapy|
|Publication status||Published - Nov-2015|
- CARBON CATABOLITE REPRESSION, S-LINKED GLYCOPEPTIDE, BACILLUS-SUBTILIS, LIPID-II, PHOSPHOCARRIER PROTEIN, STAPHYLOCOCCUS-AUREUS, RESISTANCE, EXPRESSION, GENES, HPR