Evidence map›Paper›PMID 30385807›Full record

ArticleScientific reports2018

Hornerin contains a Linked Series of Ribosome-Targeting Peptide Antibiotics.

Ulrich Gerstel, Ties Latendorf, Joachim Bartels, Alexander Becker, Andreas Tholey, Jens-Michael Schröder

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
2.4field-weighted citation impact, top 11% 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

14 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. The Epidermal Transcriptome Analysis of a Novel c.639_642dupInternational journal of molecular sciences · 2023
    Article
  5. Article
  6. Review
  7. Article
  8. Antimicrobial Peptides: A New Hope in Biomedical and Pharmaceutical Fields.Frontiers in cellular and infection microbiology · 2021
    Review
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. 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

6 authors at 3 institutions in 1 country.

Ulrich GerstelDepartment of Dermatology, University-Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany.
Ties LatendorfDepartment of Dermatology, University-Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany.
Joachim BartelsDepartment of Dermatology, University-Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany.
Alexander BeckerInstitute for Experimental Medicine - AG Systematic Proteomics & Bioanalytics, Kiel University (CAU), Kiel, Germany.
Andreas TholeyInstitute for Experimental Medicine - AG Systematic Proteomics & Bioanalytics, Kiel University (CAU), Kiel, Germany.
Jens-Michael SchröderDepartment of Dermatology, University-Hospital Schleswig-Holstein, Campus Kiel, Kiel, Germany. jschroeder@dermatology.uni-kiel.de.
Kiel University · DEUniversity Hospital Schleswig-Holstein · DEUniversity of Lübeck · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cationic intrinsically disordered antimicrobial peptides (CIDAMPs) belong to a novel class of epithelial peptide antibiotics with microbicidal activity against various pathogens, including Pseudomonas aeruginosa, Escherichia coli, Staphylococcus aureus and Candida albicans. Here we show that treatment of distinct bacteria with different hornerin (HRNR)-derived CIDAMPs cause formation of unique cytoplasmic protein aggregates, suggesting a common intracellular mode of action. We further found that, unlike most amphipathic antimicrobial peptides, HRNR traverses bacterial membranes energy-dependently and accumulates within the cytoplasm. Strikingly, certain structurally different, HRNR-based CIDAMPs were found to bind to an identical panel of distinct bacterial ribosomal proteins, thereby manifesting features of several known classes of antibiotics. This may cause the formation of aberrant proteins and toxic protein aggregates in HRNR-treated pathogens which eventually may induce its death. Our study reveals evidence that structurally distinct CIDAMPs of an abundant body surface protein simultaneously target multiple sites of the bacterial protein synthesis machinery.

Indexed as

Antimicrobial Cationic PeptidesCalcium-Binding ProteinsCandida albicansCell MembraneEscherichia coliHumansIntermediate Filament ProteinsIntrinsically Disordered ProteinsPseudomonas aeruginosaRecombinant ProteinsRibosomesStaphylococcus aureusAntimicrobial Cationic PeptidesCalcium-Binding ProteinsHRNR protein, humanIntermediate Filament ProteinsIntrinsically Disordered ProteinsRecombinant Proteins

Identifiers

PMID30385807
PMCPMC6212518
OpenAlexW2898182372

What OpenQuestion holds

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LicenceCC BY
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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.