Publication

The Phosphoenolpyruvate: Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin

De 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 journalArticleAcademicpeer-review

APA

De Gonzalo, C. V. G., Denham, E. L., Mars, R. A. T., Stuelke, J., van der Donk, W. A., & van Dijl, J. M. (2015). The Phosphoenolpyruvate: Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin. Antimicrobial Agents and Chemotherapy, 59(11), 6844-6854. https://doi.org/10.1128/AAC.01519-15

Author

De Gonzalo, C. V. Garcia ; Denham, E. L. ; Mars, R. A. T. ; Stuelke, J. ; van der Donk, W. A. ; van Dijl, Jan Maarten. / The Phosphoenolpyruvate : Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin. In: Antimicrobial Agents and Chemotherapy. 2015 ; Vol. 59, No. 11. pp. 6844-6854.

Harvard

De Gonzalo, CVG, Denham, EL, Mars, RAT, Stuelke, J, van der Donk, WA & van Dijl, JM 2015, 'The Phosphoenolpyruvate: Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin' Antimicrobial Agents and Chemotherapy, vol. 59, no. 11, pp. 6844-6854. https://doi.org/10.1128/AAC.01519-15

Standard

The Phosphoenolpyruvate : Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin. / De Gonzalo, C. V. Garcia; Denham, E. L.; Mars, R. A. T.; Stuelke, J.; van der Donk, W. A.; van Dijl, Jan Maarten.

In: Antimicrobial Agents and Chemotherapy, Vol. 59, No. 11, 11.2015, p. 6844-6854.

Research output: Contribution to journalArticleAcademicpeer-review

Vancouver

De Gonzalo CVG, Denham EL, Mars RAT, Stuelke J, van der Donk WA, van Dijl JM. The Phosphoenolpyruvate: Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin. Antimicrobial Agents and Chemotherapy. 2015 Nov;59(11):6844-6854. https://doi.org/10.1128/AAC.01519-15


BibTeX

@article{155f717a683b45f8865f5f321be7eda4,
title = "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.",
keywords = "CARBON CATABOLITE REPRESSION, S-LINKED GLYCOPEPTIDE, BACILLUS-SUBTILIS, LIPID-II, PHOSPHOCARRIER PROTEIN, STAPHYLOCOCCUS-AUREUS, RESISTANCE, EXPRESSION, GENES, HPR",
author = "{De Gonzalo}, {C. V. Garcia} and Denham, {E. L.} and Mars, {R. A. T.} and J. Stuelke and {van der Donk}, {W. A.} and {van Dijl}, {Jan Maarten}",
note = "Copyright {\circledC} 2015, American Society for Microbiology. All Rights Reserved.",
year = "2015",
month = "11",
doi = "10.1128/AAC.01519-15",
language = "English",
volume = "59",
pages = "6844--6854",
journal = "Antimicrobial Agents and Chemotherapy",
issn = "1098-6596",
publisher = "AMER SOC MICROBIOLOGY",
number = "11",

}

RIS

TY - JOUR

T1 - The Phosphoenolpyruvate

T2 - Sugar Phosphotransferase System Is Involved in Sensitivity to the Glucosylated Bacteriocin Sublancin

AU - De Gonzalo, C. V. Garcia

AU - Denham, E. L.

AU - Mars, R. A. T.

AU - Stuelke, J.

AU - van der Donk, W. A.

AU - van Dijl, Jan Maarten

N1 - Copyright © 2015, American Society for Microbiology. All Rights Reserved.

PY - 2015/11

Y1 - 2015/11

N2 - 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.

AB - 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.

KW - CARBON CATABOLITE REPRESSION

KW - S-LINKED GLYCOPEPTIDE

KW - BACILLUS-SUBTILIS

KW - LIPID-II

KW - PHOSPHOCARRIER PROTEIN

KW - STAPHYLOCOCCUS-AUREUS

KW - RESISTANCE

KW - EXPRESSION

KW - GENES

KW - HPR

U2 - 10.1128/AAC.01519-15

DO - 10.1128/AAC.01519-15

M3 - Article

VL - 59

SP - 6844

EP - 6854

JO - Antimicrobial Agents and Chemotherapy

JF - Antimicrobial Agents and Chemotherapy

SN - 1098-6596

IS - 11

ER -

ID: 23336836