Evidence map›Paper›PMID 33060695›Full record

ArticleScientific reports2020

The structure of the antimicrobial human cathelicidin LL-37 shows oligomerization and channel formation in the presence of membrane mimics.

Enea Sancho-Vaello, David Gil-Carton, Patrice François, Eve-Julie Bonetti, Mohamed Kreir, Karunakar Reddy Pothula, Ulrich Kleinekathöfer, Kornelius Zeth

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 73 papers.

0numbers the graph read from it
0cells of the map it votes in
73citing papers in PubMed
8.0field-weighted citation impact, top 2% 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

73 citing papers in PubMed, 116 citations in OpenAlex.

  1. Review
  2. Article
  3. β-Amyloid (Aβ) and Human Cathelicidin LL-37: Two Sides of the Same Coin?International journal of molecular sciences · 2026
    Review
  4. Article
  5. Serine protease HtrA promotesScience advances · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Review
  11. Review
  12. Review
  13. Review
  14. Extended-Spectrum β-Lactamase-ProducingAntibiotics (Basel, Switzerland) · 2025
    Review
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Review

13 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

8 authors at 6 institutions in 6 countries.

Enea Sancho-VaelloUnidad de Biofisica, Centro Mixto Consejo Superior de Investigaciones Cientificas-Universidad del País Vasco/Euskal Herriko Unibertsitatea (CSIC, UPV/EHU), Barrio Sarriena s/n, Leioa, Bizkaia, Spain.
David Gil-CartonStructural Biology Unit, CIC bioGUNE, Parque Tecnológico de Bizkaia Edificio 800, 48160, Derio, Spain.
Patrice FrançoisGenomic Research Laboratory, Department of Medical Specialities, Geneva University Hospitals, University of Geneva, Genève, Switzerland.ORCID 0000-0002-0540-750X
Eve-Julie BonettiGenomic Research Laboratory, Department of Medical Specialities, Geneva University Hospitals, University of Geneva, Genève, Switzerland.
Mohamed KreirNanion Technologies GmbH, Gabrielenstraße 9, 80636, Munich, Germany.
Karunakar Reddy PothulaDepartment of Physics and Earth Sciences, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.ORCID 0000-0003-0073-2511
Ulrich KleinekathöferDepartment of Physics and Earth Sciences, Jacobs University Bremen, Campus Ring 1, 28759, Bremen, Germany.ORCID 0000-0002-6114-7431
Kornelius ZethDepartment of Science and Environment, Roskilde University, Universitetsvej 1, 4000, Roskilde, Denmark. kzeth@ruc.dk.
Constructor University · DEUniversity of Geneva · CHCIC bioGUNE · ESConsejo Superior de Investigaciones Científicas · ESJanssen (Belgium) · BERoskilde University · DK

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The human cathelicidin LL-37 serves a critical role in the innate immune system defending bacterial infections. LL-37 can interact with molecules of the cell wall and perforate cytoplasmic membranes resulting in bacterial cell death. To test the interactions of LL-37 and bacterial cell wall components we crystallized LL-37 in the presence of detergents and obtained the structure of a narrow tetrameric channel with a strongly charged core. The formation of a tetramer was further studied by cross-linking in the presence of detergents and lipids. Using planar lipid membranes a small but defined conductivity of this channel could be demonstrated. Molecular dynamic simulations underline the stability of this channel in membranes and demonstrate pathways for the passage of water molecules. Time lapse studies of E. coli cells treated with LL-37 show membrane discontinuities in the outer membrane followed by cell wall damage and cell death. Collectively, our results open a venue to the understanding of a novel AMP killing mechanism and allows the rational design of LL-37 derivatives with enhanced bactericidal activity.

Indexed as

Molecular MimicryAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiopolymersCathelicidinsCell MembraneMolecular Dynamics SimulationProtein ConformationAnti-Bacterial AgentsAntimicrobial Cationic PeptidesBiopolymersCathelicidins

Identifiers

PMID33060695
PMCPMC7562864
OpenAlexW3093007566

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.