Evidence map›Paper›PMID 38619888›Full record

ArticleMolecular plant pathology2024

Modes of action and potential as a peptide-based biofungicide of a plant defensin MtDef4.

Hui Li, Raviraj Kalunke, Meenakshi Tetorya, Kirk J Czymmek, Dilip M Shah

Open access · goldAbstract read
In one paragraph

Article in Molecular plant pathology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.

0numbers the graph read from it
0cells of the map it votes in
10citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

10 citing papers in PubMed, 17 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Antifungal Peptides SmAPAntibiotics (Basel, Switzerland) · 2025
    Article
  7. Article
  8. Review
  9. Article
  10. 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.

Hui LiDonald Danforth Plant Science Center, St. Louis, Missouri, USA.ORCID 0000-0002-2489-4905
Raviraj KalunkeDonald Danforth Plant Science Center, St. Louis, Missouri, USA.ORCID 0000-0003-0110-2888
Meenakshi TetoryaDonald Danforth Plant Science Center, St. Louis, Missouri, USA.ORCID 0000-0002-1529-3331
Kirk J CzymmekDonald Danforth Plant Science Center, St. Louis, Missouri, USA.ORCID 0000-0002-5471-7395
Dilip M ShahDonald Danforth Plant Science Center, St. Louis, Missouri, USA.ORCID 0000-0001-9503-4729
Donald Danforth Plant Science Center · US

Funding

National Science Foundation-EAGER grant IOS:1955461
6 · The paper itself

Abstract

Due to rapidly emerging resistance to single-site fungicides in fungal pathogens of plants, there is a burgeoning need for safe and multisite fungicides. Plant antifungal peptides with multisite modes of action (MoA) have potential as bioinspired fungicides. Medicago truncatula defensin MtDef4 was previously reported to exhibit potent antifungal activity against fungal pathogens. Its MoA involves plasma membrane disruption and binding to intracellular targets. However, specific biochemical processes inhibited by this defensin and causing cell death have not been determined. Here, we show that MtDef4 exhibited potent antifungal activity against Botrytis cinerea. It induced severe plasma membrane and organelle irregularities in the germlings of this pathogen. It bound to fungal ribosomes and inhibited protein translation in vitro. A MtDef4 variant lacking antifungal activity exhibited greatly reduced protein translation inhibitory activity. A cation-tolerant MtDef4 variant was generated that bound to β-glucan of the fungal cell wall with higher affinity than MtDef4. It also conferred a greater reduction in the grey mould disease symptoms than MtDef4 when applied exogenously on Nicotiana benthamiana plants, tomato fruits and rose petals. Our findings revealed inhibition of protein synthesis as a likely target of MtDef4 and the potential of its cation-tolerant variant as a peptide-based fungicide.

Indexed as

Antifungal AgentsFungicides, IndustrialBotrytisCationsDefensinsPeptidesPlant DiseasesPlantsAntifungal AgentsCationsDefensinsFungicides, IndustrialPeptidesantimicrobial peptidesBotrytis cinereafungal pathogenpeptide‐based fungicideribosome bindingtranslation inhibitiontransmission electron microscopy

Identifiers

PMID38619888
PMCPMC11018249
OpenAlexW4394824073

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.