ArticleBMC microbiology2011
The Aspergillus giganteus antifungal protein AFPNN5353 activates the cell wall integrity pathway and perturbs calcium homeostasis.
Article in BMC microbiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 54 citations in OpenAlex.
- The role of Npt1 in regulating antifungal protein activity in filamentous fungi.Nature communications · 2025Article
- The antifungal peptide AnAFP fromFrontiers in microbiology · 2024Article
- Navigating the fungal battlefield: cysteine-rich antifungal proteins and peptides from Eurotiales.Frontiers in fungal biology · 2024Review
- Novel findings about the mode of action of the antifungal protein PeAfpA against Saccharomyces cerevisiae.Applied microbiology and biotechnology · 2023Article
- Pharmacokinetic profile of sarcin and thionin from Aspergillus giganteus and in vitro validation against human fungal pathogen.Bioscience reports · 2022Article
- CaJournal of fungi (Basel, Switzerland) · 2022Article
- Fungal Infections as an Uprising Threat to Human Health: Chemosensitization of Fungal Pathogens With AFP FromFrontiers in cellular and infection microbiology · 2022Review
- Do Antimicrobial Proteins Contribute to Overcoming the Hidden Antifungal Crisis at the Dawn of a Post-Antibiotic Era?Microorganisms · 2019Article
- Inhibitory Effect of PgAFP and Protective Cultures onMicroorganisms · 2018Article
- Antifungal Peptides of the AFP Family Revisited: Are These Cannibal Toxins?Microorganisms · 2018Review
- Usage of the Heterologous Expression of the Antimicrobial GeneFrontiers in plant science · 2018Article
- Calcium binding of the antifungal protein PAF: Structure, dynamics and function aspects by NMR and MD simulations.PloS one · 2018Article
- Optimization and partial characterization of intracellular anticandidal protein from Aspergillus giganteus MTCC 8408 using taguchi DOE.Bioengineered · 2017Article
- Article
- NFAP2, a novel cysteine-rich anti-yeast protein from Neosartorya fischeri NRRL 181: isolation and characterization.AMB Express · 2016Article
- Insight into the antifungal mechanism of Neosartorya fischeri antifungal protein.Protein & cell · 2015Article
- Protein kinase A signaling and calcium ions are major players in PAF mediated toxicity against Aspergillus niger.FEBS letters · 2015Article
- Components of the calcium-calcineurin signaling pathway in fungal cells and their potential as antifungal targets.Eukaryotic cell · 2015Review
- Article
- Antifungal proteins: More than antimicrobials?Fungal biology reviews · 2013Article
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundThe 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.
resultsWe 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.
conclusionsThe 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.
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