Evidence map›Paper›PMID 25755096›Full record

ArticleMicrobiologyOpen2015

The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells.

Oriane Mith, Asma Benhamdi, Teddy Castillo, Muriel Bergé, Colin W MacDiarmid, Janet Steffen, David J Eide, Véronique Perrier, Maeva Subileau, Françoise Gosti and 2 more

Open access · goldAbstract read
In one paragraph

Article in MicrobiologyOpen, 2015. 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
1.4field-weighted citation impact, top 20% 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, 31 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Review
  5. Candida albicans and Antifungal Peptides.Infectious diseases and therapy · 2023
    Article
  6. Review
  7. Overexpression of a Defensin-Like GeneFrontiers in plant science · 2020
    Article
  8. Article
  9. Review
  10. 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

12 authors at 6 institutions in 2 countries.

Oriane MithINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Asma BenhamdiINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Teddy CastilloINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Muriel BergéINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Colin W MacDiarmidDepartment of Nutritional Sciences, University of Wisconsin-Madison, Madison, Wisconsin, 53706.
Janet SteffenDepartment of Nutritional Sciences, University of Wisconsin-Madison, Madison, Wisconsin, 53706.
David J EideDepartment of Nutritional Sciences, University of Wisconsin-Madison, Madison, Wisconsin, 53706.
Véronique PerrierINRA/CIRAD UMR 1028 IATE Ingénierie des Agropolymères et Technologies Emergentes, Montpellier SupAgro/Université Montpellier 2, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Maeva SubileauINRA/CIRAD UMR 1028 IATE Ingénierie des Agropolymères et Technologies Emergentes, Montpellier SupAgro/Université Montpellier 2, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Françoise GostiINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Pierre BerthomieuINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Laurence MarquèsINRA/CNRS UMR B&PMP, Biochimie et Physiologie Moléculaire des Plantes, Montpellier SupAgro/Université Montpellier 2, Campus Montpellier SupAgro, 2 Place Viala, F-34060, Montpellier Cedex 2, France.
Université de Montpellier · FRUniversity of Wisconsin–Madison · USInstitut Agro Montpellier · FRInstitut des Sciences des Plantes de Montpellier · FRCentre National de la Recherche Scientifique · FRIngénierie des Agropolymères et Technologies Emergentes · FR

Funding

REGULATION OF CELLULAR ZINC HOMEOSTASISR01GM056285 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI EIDE, DAVID J · 1997 to 2022
$6.2M
NIGMS NIH HHS R01 GM056285NIGMS NIH HHS R01-GM56285
6 · The paper itself

Abstract

Antimicrobial peptides represent an expanding family of peptides involved in innate immunity of many living organisms. They show an amazing diversity in their sequence, structure, and mechanism of action. Among them, plant defensins are renowned for their antifungal activity but various side activities have also been described. Usually, a new biological role is reported along with the discovery of a new defensin and it is thus not clear if this multifunctionality exists at the family level or at the peptide level. We previously showed that the plant defensin AhPDF1.1b exhibits an unexpected role by conferring zinc tolerance to yeast and plant cells. In this paper, we further explored this activity using different yeast genetic backgrounds: especially the zrc1 mutant and an UPRE-GFP reporter yeast strain. We showed that AhPDF1.1b interferes with adaptive cell response in the endoplasmic reticulum to confer cellular zinc tolerance. We thus highlighted that, depending on its cellular localization, AhPDF1.1b exerts quite separate activities: when it is applied exogenously, it is a toxin against fungal and also root cells, but when it is expressed in yeast cells, it is a peptide that modulates the cellular adaptive response to zinc overload.

Indexed as

Gene ExpressionPlant ProteinsRecombinant ProteinsAntifungal AgentsAntimicrobial Cationic PeptidesArabidopsisBioreactorsDefensinsEndoplasmic ReticulumFermentationHydrogen PeroxideOxidation-ReductionPhenotypePlant RootsProtein FoldingVitamin K 3Antifungal AgentsAntimicrobial Cationic PeptidesDefensinsHydrogen PeroxidePlant ProteinsRecombinant ProteinsVitamin K 3ZincAntifungal proteincellular adaptive responsemultifunctionalityplant defensinzinc tolerance

Identifiers

PMID25755096
PMCPMC4475384
OpenAlexW1995718073

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.