Evidence map›Paper›PMID 27573545›Full record

ArticleScientific reports2016

The antifungal plant defensin AtPDF2.3 from Arabidopsis thaliana blocks potassium channels.

Kim Vriens, Steve Peigneur, Barbara De Coninck, Jan Tytgat, Bruno P A Cammue, Karin Thevissen

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed, 1 pooled it
4.1field-weighted citation impact, top 7% 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

22 citing papers in PubMed, 1 synthesis or guideline pooled it, 45 citations in OpenAlex.

  1. Pooled it
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  5. Review
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021
    Review
  14. Modulation of Lymphocyte Potassium Channel KACS pharmacology & translational science · 2020
    Article
  15. Overexpression of a Defensin-Like GeneFrontiers in plant science · 2020
    Article
  16. Article
  17. Article
  18. Review
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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

6 authors at 1 institution in 1 country.

Kim VriensCentre of Microbial and Plant Genetics, KU Leuven, Kasteelpark Arenberg 20, 3001 Heverlee, Belgium.
Steve PeigneurToxicology and Pharmacology, University of Leuven, O&N 2, Herestraat 49, P.O. Box 922, 3000, Leuven, Belgium.
Barbara De ConinckCentre of Microbial and Plant Genetics, KU Leuven, Kasteelpark Arenberg 20, 3001 Heverlee, Belgium.
Jan TytgatToxicology and Pharmacology, University of Leuven, O&N 2, Herestraat 49, P.O. Box 922, 3000, Leuven, Belgium.
Bruno P A CammueCentre of Microbial and Plant Genetics, KU Leuven, Kasteelpark Arenberg 20, 3001 Heverlee, Belgium.
Karin ThevissenCentre of Microbial and Plant Genetics, KU Leuven, Kasteelpark Arenberg 20, 3001 Heverlee, Belgium.
KU Leuven · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Scorpion toxins that block potassium channels and antimicrobial plant defensins share a common structural CSαβ-motif. These toxins contain a toxin signature (K-C4-X-N) in their amino acid sequence, and based on in silico analysis of 18 plant defensin sequences, we noted the presence of a toxin signature (K-C5-R-G) in the amino acid sequence of the Arabidopsis thaliana defensin AtPDF2.3. We found that recombinant (r)AtPDF2.3 blocks Kv1.2 and Kv1.6 potassium channels, akin to the interaction between scorpion toxins and potassium channels. Moreover, rAtPDF2.3[G36N], a variant with a KCXN toxin signature (K-C5-R-N), is more potent in blocking Kv1.2 and Kv1.6 channels than rAtPDF2.3, whereas rAtPDF2.3[K33A], devoid of the toxin signature, is characterized by reduced Kv channel blocking activity. These findings highlight the importance of the KCXN scorpion toxin signature in the plant defensin sequence for blocking potassium channels. In addition, we found that rAtPDF2.3 inhibits the growth of Saccharomyces cerevisiae and that pathways regulating potassium transport and/or homeostasis confer tolerance of this yeast to rAtPDF2.3, indicating a role for potassium homeostasis in the fungal defence response towards rAtPDF2.3. Nevertheless, no differences in antifungal potency were observed between the rAtPDF2.3 variants, suggesting that antifungal activity and Kv channel inhibitory function are not linked.

Indexed as

Antifungal AgentsArabidopsis ProteinsHomeodomain ProteinsHumansKv1.2 Potassium ChannelKv1.6 Potassium ChannelPotassium Channel BlockersRecombinant ProteinsSaccharomyces cerevisiaeShaker Superfamily of Potassium ChannelsAntifungal AgentsArabidopsis ProteinsHomeodomain ProteinsKCNA6 protein, humanKv1.2 Potassium ChannelKv1.6 Potassium ChannelPDF2 protein, ArabidopsisPotassium Channel BlockersRecombinant ProteinsShaker Superfamily of Potassium Channels

Identifiers

PMID27573545
PMCPMC5004176
OpenAlexW2509035076

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.