Abstract
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 language | English |
---|---|
Pages (from-to) | 6844-6854 |
Number of pages | 11 |
Journal | Antimicrobial Agents and Chemotherapy |
Volume | 59 |
Issue number | 11 |
DOIs | |
Publication status | Published - Nov 2015 |
Bibliographical note
Copyright © 2015, American Society for Microbiology. All Rights Reserved.Keywords
- Bacillus/drug effects
- Bacteriocins/pharmacology
- Glycopeptides/pharmacology
- Microbial Sensitivity Tests
- Phosphoenolpyruvate Sugar Phosphotransferase System/genetics
- Polymorphism, Single Nucleotide/genetics