Evidence map›Paper›PMID 24492359›Full record

ArticleAntimicrobial agents and chemotherapy2014

Fungicidal mechanisms of cathelicidins LL-37 and CATH-2 revealed by live-cell imaging.

Soledad R Ordonez, Ilham H Amarullah, Richard W Wubbolts, Edwin J A Veldhuizen, Henk P Haagsman

Open access · bronzeAbstract read
In one paragraph

Article in Antimicrobial agents and chemotherapy, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

45 citing papers in PubMed, 82 citations in OpenAlex.

  1. Review
  2. Article
  3. The Contribution of Human Antimicrobial Peptides to Fungi.International journal of molecular sciences · 2025
    Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Review
  9. Probing Cell-Surface Interactions in Fungal Cell Walls by High-ResolutionChemistry (Weinheim an der Bergstrasse, Germany) · 2023
    Article
  10. Review
  11. Article
  12. Review
  13. Antimicrobial Peptides with Anti-International journal of molecular sciences · 2022
    Review
  14. Antimicrobial nanomedicine for ocular bacterial and fungal infection.Drug delivery and translational research · 2021
    Review
  15. Article
  16. Article
  17. Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021
    Review
  18. Article
  19. Review
  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

5 authors at 1 institution in 1 country.

Soledad R OrdonezDepartment of Infectious Diseases and Immunology, Division Molecular Host Defense, Faculty of Veterinary Medicine, Utrecht University, Utrecht, The Netherlands.
Ilham H Amarullah
Richard W Wubbolts
Edwin J A Veldhuizen
Henk P Haagsman
Utrecht University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Antifungal mechanisms of action of two cathelicidins, chicken CATH-2 and human LL-37, were studied and compared with the mode of action of the salivary peptide histatin 5 (Hst5). Candida albicans was used as a model organism for fungal pathogens. Analysis by live-cell imaging showed that the peptides kill C. albicans rapidly. CATH-2 is the most active peptide and kills C. albicans within 5 min. Both cathelicidins induce cell membrane permeabilization and simultaneous vacuolar expansion. Minimal fungicidal concentrations (MFC) are in the same order of magnitude for all three peptides, but the mechanisms of antifungal activity are very different. The activity of cathelicidins is independent of the energy status of the fungal cell, unlike Hst5 activity. Live-cell imaging using fluorescently labeled peptides showed that both CATH-2 and LL-37 quickly localize to the C. albicans cell membrane, while Hst5 was mainly directed to the fungal vacuole. Small amounts of cathelicidins internalize at sub-MFCs, suggesting that intracellular activities of the peptide could contribute to the antifungal activity. Analysis by flow cytometry indicated that CATH-2 significantly decreases C. albicans cell size. Finally, electron microscopy showed that CATH-2 affects the integrity of the cell membrane and nuclear envelope. It is concluded that the general mechanisms of action of both cathelicidins are partially similar (but very different from that of Hst5). CATH-2 has unique features and possesses antifungal potential superior to that of LL-37.

Indexed as

Antifungal AgentsCandida albicansCathelicidinsMicrobial Sensitivity TestsMicroscopy, ElectronAntifungal AgentsCathelicidins

Identifiers

PMID24492359
PMCPMC4023799
OpenAlexW2140720134

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.