Evidence map›Paper›PMID 24566179›Full record

ArticleAntimicrobial agents and chemotherapy2014

Plant-derived decapeptide OSIP108 interferes with Candida albicans biofilm formation without affecting cell viability.

Nicolas Delattin, Katrijn De Brucker, David J Craik, Olivier Cheneval, Mirjam Fröhlich, Matija Veber, Lenart Girandon, Talya R Davis, Anne E Weeks, Carol A Kumamoto and 5 more

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 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
4.4field-weighted citation impact, top 6% 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

11 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Potential inhibitory activity of phytoconstituents against black fungus:Computational toxicology (Amsterdam, Netherlands) · 2022
    Article
  5. Bioactive Peptides Against Fungal Biofilms.Frontiers in microbiology · 2019
    Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. 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

15 authors at 7 institutions in 4 countries.

Nicolas DelattinCentre of Microbial and Plant Genetics (CMPG), KU Leuven, Leuven, Belgium.
Katrijn De Brucker
David J Craik
Olivier Cheneval
Mirjam Fröhlich
Matija Veber
Lenart Girandon
Talya R Davis
Anne E Weeks
Carol A Kumamoto
Paul Cos
Tom Coenye
Barbara De Coninck
Bruno P A Cammue
Karin Thevissen
KU Leuven · BEEducell · SITufts University · USUniversity of Queensland · AUGhent University · BEUniversity of Antwerp · BEVIB-UGent Center for Plant Systems Biology · BE

Funding

Contact sensing and C. albicans-host interactionR01AI081794 · NIAID · TUFTS UNIVERSITY BOSTON · PI KUMAMOTO, CAROL A. · 2010 to 2014
$2.2M
NIAID NIH HHS R01 AI081794
6 · The paper itself

Abstract

We previously identified a decapeptide from the model plant Arabidopsis thaliana, OSIP108, which is induced upon fungal pathogen infection. In this study, we demonstrated that OSIP108 interferes with biofilm formation of the fungal pathogen Candida albicans without affecting the viability or growth of C. albicans cells. OSIP108 displayed no cytotoxicity against various human cell lines. Furthermore, OSIP108 enhanced the activity of the antifungal agents amphotericin B and caspofungin in vitro and in vivo in a Caenorhabditis elegans-C. albicans biofilm infection model. These data point to the potential use of OSIP108 in combination therapy with conventional antifungal agents. In a first attempt to unravel its mode of action, we screened a library of 137 homozygous C. albicans mutants, affected in genes encoding cell wall proteins or transcription factors important for biofilm formation, for altered OSIP108 sensitivity. We identified 9 OSIP108-tolerant C. albicans mutants that were defective in either components important for cell wall integrity or the yeast-to-hypha transition. In line with these findings, we demonstrated that OSIP108 activates the C. albicans cell wall integrity pathway and that its antibiofilm activity can be blocked by compounds inhibiting the yeast-to-hypha transition. Furthermore, we found that OSIP108 is predominantly localized at the C. albicans cell surface. These data point to interference of OSIP108 with cell wall-related processes of C. albicans, resulting in impaired biofilm formation.

Indexed as

Antifungal AgentsBiofilmsCandida albicansOligopeptidesAntifungal AgentsOligopeptides

Identifiers

PMID24566179
PMCPMC3993227
OpenAlexW2147807911

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.