Format

Send to

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

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

Author information

1
Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
2
Division of Translational and Systems Medicine, Unit of Microbiology and Infection, Warwick Medical School, University of Warwick, Coventry, United Kingdom Department of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
3
Department of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
4
Institut für Mikrobiologie und Genetik, Abteilung für Allgemeine Mikrobiologie, Göttingen, Germany.
5
Howard Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA vddonk@illinois.edu j.m.van.dijl01@umcg.nl.
6
Department of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands vddonk@illinois.edu j.m.van.dijl01@umcg.nl.

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.

PMID:
26282429
PMCID:
PMC4604375
DOI:
10.1128/AAC.01519-15
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for HighWire Icon for PubMed Central
Loading ...
Support Center