Evidence map›Paper›PMID 17277210›Full record

ArticleApplied and environmental microbiology2007

The antifungal protein AFP from Aspergillus giganteus inhibits chitin synthesis in sensitive fungi.

Silke Hagen, Florentine Marx, Arthur F Ram, Vera Meyer

Open access · greenAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.

0numbers the graph read from it
0cells of the map it votes in
41citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

41 citing papers in PubMed, 98 citations in OpenAlex.

  1. Article
  2. Morphotype-specific susceptibility toMicrobiology spectrum · 2026
    Article
  3. Article
  4. Review
  5. Article
  6. The antifungal peptide AnAFP fromFrontiers in microbiology · 2024
    Article
  7. Review
  8. Antifungal peptides from living organisms.Frontiers in microbiology · 2024
    Review
  9. Article
  10. Article
  11. Article
  12. Potential Treatment of DermatophyteMolecules (Basel, Switzerland) · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021
    Review
  18. Article
  19. Article
  20. Review
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

4 authors at 3 institutions in 3 countries.

Silke HagenBerlin University of Technology, Institute of Biotechnology, Department Microbiology and Genetics, Gustav-Meyer-Allee 25, D-13355 Berlin, Germany.
Florentine Marx
Arthur F Ram
Vera Meyer
Technische Universität Berlin · DEInnsbruck Medical University · ATLeiden University · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The antifungal protein AFP from Aspergillus giganteus is highly effective in restricting the growth of major human- and plant-pathogenic filamentous fungi. However, a fundamental prerequisite for the use of AFP as an antifungal drug is a complete understanding of its mode of action. In this study, we performed several analyses focusing on the assumption that the chitin biosynthesis of sensitive fungi is targeted by AFP. Here we show that the N-terminal domain of AFP (amino acids 1 to 33) is sufficient for efficient binding of AFP to chitin but is not adequate for inhibition of the growth of sensitive fungi. AFP susceptibility tests and SYTOX Green uptake experiments with class III and class V chitin synthase mutants of Fusarium oxysporum and Aspergillus oryzae showed that deletions made the fungi less sensitive to AFP and its membrane permeabilization effect. In situ chitin synthase activity assays revealed that chitin synthesis is specifically inhibited by AFP in sensitive fungi, indicating that AFP causes cell wall stress and disturbs cell integrity. Further evidence that there was AFP-induced cell wall stress was obtained by using an Aspergillus niger reporter strain in which the cell wall integrity pathway was strongly induced by AFP.

Indexed as

Amino Acid SequenceAntifungal AgentsCell WallChitinChitin SynthaseFungal ProteinsFungiMolecular Sequence DataAntifungal Agentsantifungal protein, AspergillusChitinChitin SynthaseFungal Proteins

Identifiers

PMID17277210
PMCPMC1855660
OpenAlexW2062354669

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.