Evidence map›Paper›PMID 26282429›Full record

ArticleAntimicrobial agents and chemotherapy2015

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

C V Garcia De Gonzalo, E L Denham, R A T Mars, J Stülke, W A van der Donk, J M van Dijl

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
6.8field-weighted citation impact, top 4% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
  2. AJournal of bacteriology · 2025
    Article
  3. Characterization of a novel glycocin from a thermophile.bioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Transporters of glucose and other carbohydrates in bacteria.Pflugers Archiv : European journal of physiology · 2020
    Review
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
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4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 3 institutions in 4 countries.

C V Garcia De GonzaloHoward Hughes Medical Institute and Roger Adams Laboratory, Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, Illinois, USA.
E L DenhamDivision 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.
R A T MarsDepartment of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands.
J StülkeInstitut für Mikrobiologie und Genetik, Abteilung für Allgemeine Mikrobiologie, Göttingen, Germany.
W A van der DonkHoward 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.ORCID http://orcid.org/0000-0002-5467-7071
J M van DijlDepartment of Medical Microbiology, University of Groningen, University Medical Center Groningen, Groningen, the Netherlands vddonk@illinois.edu j.m.van.dijl01@umcg.nl.
University Medical Center Groningen · NLHoward Hughes Medical Institute · USInstitut für Medizinische Informatik, Biometrie und Epidemiologie · DE

Funding

Training Program in Chemistry-Interface with BiologyT32GM070421 · NIGMS · UNIVERSITY OF ILLINOIS URBANA-CHAMPAIGN · PI HERGENROTHER, PAUL · 2005 to 2019
$5.4M
Howard Hughes Medical InstituteNIGMS NIH HHS 5T32-GM070421NIGMS NIH HHS T32 GM070421
6 · The paper itself

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.

Indexed as

BacillusBacteriocinsGlycopeptidesMicrobial Sensitivity TestsPhosphoenolpyruvate Sugar Phosphotransferase SystemPolymorphism, Single NucleotideBacteriocinsGlycopeptidesphosphoenolpyruvate-glucose phosphotransferasePhosphoenolpyruvate Sugar Phosphotransferase System

Identifiers

PMID26282429
PMCPMC4604375
OpenAlexW1841236368

What OpenQuestion holds

Textmetadata
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Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.