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

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 activit...

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Autores principales: Mith, Oriane, Benhamdi, Asma, Castillo, Teddy, Bergé, Muriel, MacDiarmid, Colin W, Steffen, Janet, Eide, David J, Perrier, Véronique, Subileau, Maeva, Gosti, Françoise, Berthomieu, Pierre, Marquès, Laurence
Formato: Online Artículo Texto
Lenguaje:English
Publicado: BlackWell Publishing Ltd 2015
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4475384/
https://www.ncbi.nlm.nih.gov/pubmed/25755096
http://dx.doi.org/10.1002/mbo3.248
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author Mith, Oriane
Benhamdi, Asma
Castillo, Teddy
Bergé, Muriel
MacDiarmid, Colin W
Steffen, Janet
Eide, David J
Perrier, Véronique
Subileau, Maeva
Gosti, Françoise
Berthomieu, Pierre
Marquès, Laurence
author_facet Mith, Oriane
Benhamdi, Asma
Castillo, Teddy
Bergé, Muriel
MacDiarmid, Colin W
Steffen, Janet
Eide, David J
Perrier, Véronique
Subileau, Maeva
Gosti, Françoise
Berthomieu, Pierre
Marquès, Laurence
author_sort Mith, Oriane
collection PubMed
description 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.
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spelling pubmed-44753842015-06-26 The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells Mith, Oriane Benhamdi, Asma Castillo, Teddy Bergé, Muriel MacDiarmid, Colin W Steffen, Janet Eide, David J Perrier, Véronique Subileau, Maeva Gosti, Françoise Berthomieu, Pierre Marquès, Laurence Microbiologyopen Original Research 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. BlackWell Publishing Ltd 2015-06 2015-03-08 /pmc/articles/PMC4475384/ /pubmed/25755096 http://dx.doi.org/10.1002/mbo3.248 Text en © 2015 The Authors. MicrobiologyOpen published by John Wiley & Sons Ltd. http://creativecommons.org/licenses/by/4.0/ This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.
spellingShingle Original Research
Mith, Oriane
Benhamdi, Asma
Castillo, Teddy
Bergé, Muriel
MacDiarmid, Colin W
Steffen, Janet
Eide, David J
Perrier, Véronique
Subileau, Maeva
Gosti, Françoise
Berthomieu, Pierre
Marquès, Laurence
The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
title The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
title_full The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
title_fullStr The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
title_full_unstemmed The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
title_short The antifungal plant defensin AhPDF1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
title_sort antifungal plant defensin ahpdf1.1b is a beneficial factor involved in adaptive response to zinc overload when it is expressed in yeast cells
topic Original Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4475384/
https://www.ncbi.nlm.nih.gov/pubmed/25755096
http://dx.doi.org/10.1002/mbo3.248
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