Evidence map›Paper›PMID 30842543›Full record

ArticleScientific reports2019

Proteolytic Degradation of reduced Human Beta Defensin 1 generates a Novel Antibiotic Octapeptide.

Judith Wendler, Bjoern O Schroeder, Dirk Ehmann, Louis Koeninger, Daniela Mailänder-Sánchez, Christina Lemberg, Stephanie Wanner, Martin Schaller, Eduard F Stange, Nisar P Malek and 3 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

17 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Maintaining microbiota across diverse symbiotic organs inProceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  4. Article
  5. Review
  6. Human α-Defensin 5International journal of molecular sciences · 2023
    Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Article
  12. 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

13 authors at 4 institutions in 3 countries.

Judith WendlerDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany.
Bjoern O SchroederDr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology, Stuttgart and University of Tuebingen, Tuebingen, Germany.ORCID 0000-0002-6716-8284
Dirk EhmannDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany.
Louis KoeningerDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany.
Daniela Mailänder-SánchezDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany.
Christina LembergInstitute of Dermatology, University Hospital Tuebingen, Tuebingen, Germany.
Stephanie WannerInstitute of Dermatology, University Hospital Tuebingen, Tuebingen, Germany.
Martin SchallerInstitute of Dermatology, University Hospital Tuebingen, Tuebingen, Germany.
Eduard F StangeDr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology, Stuttgart and University of Tuebingen, Tuebingen, Germany.
Nisar P MalekDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany.
Christopher WeidenmaierInstitute of Medical Microbiology and Hygiene, University Hospital Tuebingen, Tuebingen, Germany.ORCID 0000-0003-4107-739X
Salomé LeibundGut-LandmannInstitute of Immunology, Vetsuisse Faculty, University of Zürich, Zurich, Switzerland.ORCID 0000-0002-5724-4837
Jan WehkampDepartment of Internal Medicine 1, University Hospital Tuebingen, Tuebingen, Germany. jan.wehkamp@med.uni-tuebingen.de.ORCID 0000-0001-6788-841X
University of Tübingen · DEDr. Margarete Fischer-Bosch-Institute of Clinical Pharmacology · DEInstitute of Medical Microbiology and Hygiene · DEUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Microbial resistance against clinical used antibiotics is on the rise. Accordingly, there is a high demand for new innovative antimicrobial strategies. The host-defense peptide human beta-defensin 1 (hBD-1) is produced continuously by epithelial cells and exhibits compelling antimicrobial activity after reduction of its disulphide bridges. Here we report that proteolysis of reduced hBD-1 by gastrointestinal proteases as well as human duodenal secretions produces an eight-amino acid carboxy-terminal fragment. The generated octapeptide retains antibiotic activity, yet with distinct characteristics differing from the full-length peptide. We modified the octapeptide by stabilizing its termini and by using non-natural D-amino acids. The native and modified peptide variants showed antibiotic activity against pathogenic as well as antibiotic-resistant microorganisms, including E. coli, P. aeruginosa and C. albicans. Moreover, in an in vitro C. albicans infection model the tested peptides demonstrated effective amelioration of C. albicans infection without showing cytotoxity on human cells. In summary, protease degradation of hBD-1 provides a yet unknown mechanism to broaden antimicrobial host defense, which could be used to develop defensin-derived therapeutic applications.

Indexed as

Anti-Bacterial AgentsBacteriabeta-DefensinsFungiHumansPeptide FragmentsProteolysisAnti-Bacterial Agentsbeta-DefensinsDEFB1 protein, humanPeptide Fragments

Identifiers

PMID30842543
PMCPMC6403363
OpenAlexW2918688055

What OpenQuestion holds

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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.