Unknown

Dataset Information

0

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


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.

SUBMITTER: Garcia De Gonzalo CV 

PROVIDER: S-EPMC4604375 | biostudies-literature | 2015 Nov

REPOSITORIES: biostudies-literature

altmetric image

Publications

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

Garcia De Gonzalo C V CV   Denham E L EL   Mars R A T RA   Stülke J J   van der Donk W A WA   van Dijl J M JM  

Antimicrobial agents and chemotherapy 20150817 11


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 th  ...[more]

Similar Datasets

| S-EPMC1618308 | biostudies-literature
| S-EPMC1471863 | biostudies-literature
| S-EPMC9671846 | biostudies-literature
| S-EPMC3724859 | biostudies-literature
| S-EPMC97224 | biostudies-literature
| S-EPMC2785159 | biostudies-literature
| S-EPMC3911062 | biostudies-literature
| S-EPMC2222622 | biostudies-literature
| S-EPMC2479611 | biostudies-literature
| S-EPMC6372417 | biostudies-literature