Evidence map›Paper›PMID 21078927›Full record

ArticleAntimicrobial agents and chemotherapy2011

Peptide antibiotic sensing and detoxification modules of Bacillus subtilis.

Anna Staroń, Dora Elisabeth Finkeisen, Thorsten Mascher

Open access · greenAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.9field-weighted citation impact, top 5% 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

68 citing papers in PubMed, 114 citations in OpenAlex.

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  4. Discovery of Coerumycin, a Cinnamycin-like Lantibiotic fromAntibiotics (Basel, Switzerland) · 2026
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  5. Proteolytically activated antibacterial toxins inhibit the growth of diverse gram-positive bacteria.Proceedings of the National Academy of Sciences of the United States of America · 2025
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  6. Emerging antibiotic resistance by various novel proteins/enzymes.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025
    Review
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  8. The extracellular domain ofFrontiers in microbiology · 2025
    Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Application of a Bacillus subtilis Whole-Cell Biosensor (PMethods in molecular biology (Clifton, N.J.) · 2023
    Article
  18. Article
  19. Review
  20. Article

8 more citing papers are in PubMed but not listed here.

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

3 authors at 2 institutions in 1 country.

Anna StarońLudwig-Maximilians-University, Department Biology I, Microbiology, Munich, Germany.
Dora Elisabeth Finkeisen
Thorsten Mascher
Ludwig-Maximilians-Universität München · DEUniversity of Göttingen · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Peptide antibiotics are produced by a wide range of microorganisms. Most of them target the cell envelope, often by inhibiting cell wall synthesis. One of the resistance mechanisms against antimicrobial peptides is a detoxification module consisting of a two-component system and an ABC transporter. Upon the detection of such a compound, the two-component system induces the expression of the ABC transporter, which in turn removes the antibiotic from its site of action, mediating the resistance of the cell. Three such peptide antibiotic-sensing and detoxification modules are present in Bacillus subtilis. Here we show that each of these modules responds to a number of peptides and confers resistance against them. BceRS-BceAB (BceRS-AB) responds to bacitracin, plectasin, mersacidin, and actagardine. YxdJK-LM is induced by a cationic antimicrobial peptide, LL-37. The PsdRS-AB (formerly YvcPQ-RS) system responds primarily to lipid II-binding lantibiotics such as nisin and gallidermin. We characterized the psdRS-AB operon and defined the regulatory sequences within the P(psdA) promoter. Mutation analysis demonstrated that P(psdA) expression is fully PsdR dependent. The features of both the P(bceA) and P(psdA) promoters make them promising candidates as novel whole-cell biosensors that can easily be adjusted for high-throughput screening.

Indexed as

Drug Resistance, BacterialSignal TransductionAnti-Bacterial AgentsAntimicrobial Cationic PeptidesATP-Binding Cassette TransportersBacillus subtilisBacitracinBacterial ProteinsBacteriocinsBiosensing TechniquesCathelicidinsGene Expression Regulation, BacterialOperonPeptidesAnti-Bacterial AgentsAntimicrobial Cationic PeptidesATP-Binding Cassette TransportersBacitracinBacterial ProteinsBacteriocinsCathelicidinsmersacidinPeptidesplectasin

Identifiers

PMID21078927
PMCPMC3028804
OpenAlexW2098965059

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.