Evidence map›Paper›PMID 26169420›Full record

ArticleAntimicrobial agents and chemotherapy2015

Influence of the yjiL-mdtM Gene Cluster on the Antibacterial Activity of Proline-Rich Antimicrobial Peptides Overcoming Escherichia coli Resistance Induced by the Missing SbmA Transporter System.

Andor Krizsan, Daniel Knappe, Ralf Hoffmann

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 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
4.6field-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

46 citing papers in PubMed, 77 citations in OpenAlex.

  1. Article
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  3. Article
  4. Article
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  6. Article
  7. Proline-Rich Antimicrobial Peptides from Invertebrates.Molecules (Basel, Switzerland) · 2024
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Bactericidal Properties of Proline-RichLife (Basel, Switzerland) · 2022
    Article
  17. Review
  18. Article
  19. Article
  20. Article
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 1 institution in 1 country.

Andor KrizsanInstitute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, Universität Leipzig, Leipzig, Germany Center for Biotechnology and Biomedicine, Universität Leipzig, Leipzig, Germany.
Daniel KnappeInstitute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, Universität Leipzig, Leipzig, Germany Center for Biotechnology and Biomedicine, Universität Leipzig, Leipzig, Germany.
Ralf HoffmannInstitute of Bioanalytical Chemistry, Faculty of Chemistry and Mineralogy, Universität Leipzig, Leipzig, Germany Center for Biotechnology and Biomedicine, Universität Leipzig, Leipzig, Germany hoffmann@chemie.uni-leipzig.de.
Leipzig University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In view of increasing health threats from multiresistant pathogens, antimicrobial peptides (AMPs) and, specifically, proline-rich AMPs (PrAMPs) have been investigated in animal models. PrAMPs enter bacteria via the ABC transporter SbmA and inhibit intracellular targets. We used phage transduction (Tn10 insertion) to screen by random mutagenesis for alternative uptake mechanisms for analogs of apidaecin 1b, a honeybee-derived PrAMP. All 24 apidaecin-resistant mutants had the Tn10 insertion in the sbmA gene. These sbmA::Tn10 insertion mutants and the Escherichia coli BW25113 ΔsbmA (JW0368) strain were still susceptible to the bactenecin PrAMP Bac7(1-35) and oncocin PrAMPs Onc18 and Onc112, as well as to Chex1-Arg20, despite significantly reduced internalizations. In a second round of random mutagenesis, the remaining susceptibility was linked to the yjiL-mdtM gene cluster. E. coli BW25113 and its ΔyjiL null mutant (JW5785) were equally susceptible to all PrAMPs tested, whereas the BW25113 ΔmdtM mutant was less susceptible to oncocins. The JW0368 yjiL::Tn10 transposon mutant (BS2) was resistant to all short PrAMPs and susceptible only to full-length Bac7 and A3-APO. Interestingly, PrAMPs appear to enter bacteria via MdtM, a multidrug resistance transporter (drug/H(+) antiporter) of the major facilitator superfamily (MFS) that can efflux antibiotics, biocides, and bile salts. In conclusion, PrAMPs enter bacteria via ABC and MFS transporters that efflux antibiotics and cytotoxic compounds from the cytoplasm to the periplasm.

Indexed as

Gene Expression Regulation, BacterialAnimalsAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntiportersATP-Binding Cassette TransportersBeesBiological TransportColiphagesCytoplasmDNA Transposable ElementsDrug Resistance, BacterialEscherichia coliEscherichia coli ProteinsMembrane Transport ProteinsMultigene FamilyAnti-Bacterial AgentsAntimicrobial Cationic PeptidesAntiportersapidaecinATP-Binding Cassette TransportersbactenecinDNA Transposable ElementsEscherichia coli ProteinsMdtM protein, E coliMembrane Transport ProteinsoncocinPeptides, CyclicSbmA protein, E coli

Identifiers

PMID26169420
PMCPMC4576061
OpenAlexW1939757033

What OpenQuestion holds

Textmetadata
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Registered trials

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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.