Evidence map›Paper›PMID 24566173›Full record

ArticleAntimicrobial agents and chemotherapy2014

Agp2p, the plasma membrane transregulator of polyamine uptake, regulates the antifungal activities of the plant defensin NaD1 and other cationic peptides.

Mark R Bleackley, Jennifer L Wiltshire, Francine Perrine-Walker, Shaily Vasa, Rhiannon L Burns, Nicole L van der Weerden, Marilyn A Anderson

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 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
2.2field-weighted citation impact, top 14% 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

19 citing papers in PubMed, 29 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Article
  5. Review
  6. Membrane-Interacting Antifungal Peptides.Frontiers in cell and developmental biology · 2021
    Review
  7. Frontiers in microbiology · 2020
    Article
  8. Article
  9. Screening theAntimicrobial agents and chemotherapy · 2019
    Article
  10. Article
  11. Extracellular vesicles secreted byCommunications biology · 2019
    Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. 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

7 authors at 1 institution in 1 country.

Mark R BleackleyLa Trobe Institute for Molecular Science, Melbourne, Victoria, Australia.
Jennifer L Wiltshire
Francine Perrine-Walker
Shaily Vasa
Rhiannon L Burns
Nicole L van der Weerden
Marilyn A Anderson
La Trobe University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cationic antifungal peptides (AFPs) act through a variety of mechanisms but share the common feature of interacting with the fungal cell surface. NaD1, a defensin from Nicotiana alata, has potent antifungal activity against a variety of fungi of both hyphal and yeast morphologies. The mechanism of action of NaD1 occurs via three steps: binding to the fungal cell surface, permeabilization of the plasma membrane, and internalization and interaction with intracellular targets to induce fungal cell death. The targets at each of these three stages have yet to be defined. In this study, the screening of a Saccharomyces cerevisiae deletion collection led to the identification of Agp2p as a regulator of the potency of NaD1. Agp2p is a plasma membrane protein that regulates the transport of polyamines and other molecules, many of which carry a positive charge. Cells lacking the agp2 gene were more resistant to NaD1, and this resistance was accompanied by a decreased uptake of defensin. Agp2p senses and regulates the uptake of the polyamine spermidine, and competitive inhibition of the antifungal activity of NaD1 by spermidine was observed in both S. cerevisiae and the plant pathogen Fusarium oxysporum. The resistance of agp2Δ cells to other cationic antifungal peptides and decreased binding of the cationic protein cytochrome c to agp2Δ cells compared to that of wild-type cells have led to a proposed mechanism of resistance whereby the deletion of agp2 leads to an increase in positively charged molecules at the cell surface that repels cationic antifungal peptides.

Indexed as

Antifungal AgentsCell MembraneFlow CytometryFusariumNADH DehydrogenasePeptidesPlant ProteinsPolyaminesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsAntifungal AgentsNADH DehydrogenasePeptidesPlant ProteinsPolyaminesSaccharomyces cerevisiae Proteins

Identifiers

PMID24566173
PMCPMC3993230
OpenAlexW2062172099

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.