Please use this identifier to cite or link to this item: http://dx.doi.org/10.14279/depositonce-6920
Main Title: The Aspergillus giganteus antifungal protein AFPNN5353activates the cell wall integrity pathway and perturbs calcium homeostasis
Author(s): Binder, Ulrike
Bencina, Mojca
Eigentler, Andrea
Meyer, Vera
Marx, Florentine
Type: Article
Language Code: en
Abstract: Background The antifungal protein AFPNN5353 is a defensin-like protein of Aspergillus giganteus. It belongs to a group of secretory proteins with low molecular mass, cationic character and a high content of cysteine residues. The protein inhibits the germination and growth of filamentous ascomycetes, including important human and plant pathogens and the model organsims Aspergillus nidulans and Aspergillus niger. Results We determined an AFPNN5353 hypersensitive phenotype of non-functional A. nidulans mutants in the protein kinase C (Pkc)/mitogen-activated protein kinase (Mpk) signalling pathway and the induction of the α-glucan synthase A (agsA) promoter in a transgenic A. niger strain which point at the activation of the cell wall integrity pathway (CWIP) and the remodelling of the cell wall in response to AFPNN5353. The activation of the CWIP by AFPNN5353, however, operates independently from RhoA which is the central regulator of CWIP signal transduction in fungi. Furthermore, we provide evidence that calcium (Ca2+) signalling plays an important role in the mechanistic function of this antifungal protein. AFPNN5353 increased about 2-fold the cytosolic free Ca2+ ([Ca2+]c) of a transgenic A. niger strain expressing codon optimized aequorin. Supplementation of the growth medium with CaCl2 counteracted AFPNN5353 toxicity, ameliorated the perturbation of the [Ca2+]c resting level and prevented protein uptake into Aspergillus sp. cells. Conclusions The present study contributes new insights into the molecular mechanisms of action of the A. giganteus antifungal protein AFPNN5353. We identified its antifungal activity, initiated the investigation of pathways that determine protein toxicity, namely the CWIP and the Ca2+ signalling cascade, and studied in detail the cellular uptake mechanism in sensitive target fungi. This knowledge contributes to define new potential targets for the development of novel antifungal strategies to prevent and combat infections of filamentous fungi which have severe negative impact in medicine and agriculture.
URI: https://depositonce.tu-berlin.de//handle/11303/7742
http://dx.doi.org/10.14279/depositonce-6920
Issue Date: 23-Sep-2011
Date Available: 3-May-2018
DDC Class: 570 Biowissenschaften; Biologie
Subject(s): Caspofungin
BAPTA
antifungal protein
mechanical perturbation
sensitive fungus
Sponsor/Funder: FWF, P19970-B11, Characterization of the toxicity of PAF
License: https://creativecommons.org/licenses/by/2.0/
Journal Title: BMC Microbiology
Publisher: BioMed Central
Publisher Place: London
Volume: 11
Article Number: 209
Publisher DOI: 10.1186/1471-2180-11-209
ISSN: 1471-2180
Appears in Collections:FG Angewandte und Molekulare Mikrobiologie » Publications

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