ArticleMicrobial cell factories2016
A Penicillium chrysogenum-based expression system for the production of small, cysteine-rich antifungal proteins for structural and functional analyses.
Article in Microbial cell factories, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 50 papers.
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50 citing papers in PubMed, 81 citations in OpenAlex.
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- Engineering Penicillium expansum antifungal proteins unveils new clues about their mode of action.Applied microbiology and biotechnology · 2026Article
- High yield production of the antifungal proteins PeAfpA and PdAfpB by vacuole targeting in a TMV-based expression vector.Plant biotechnology journal · 2026Article
- The Biocontrol and Growth-Promoting Potential ofPlants (Basel, Switzerland) · 2025Article
- Increasing the efficiency of CRISPR/Cas9-mediated genome editing in the citrus postharvest pathogen Penicillium digitatum.Fungal biology and biotechnology · 2024Article
- Fighting pathogenic yeasts with plant defensins and anti-fungal proteins from fungi.Applied microbiology and biotechnology · 2024Review
- 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
- Heterologous protein production in filamentous fungi.Applied microbiology and biotechnology · 2023Review
- Transcriptomic Profile of Penicillium digitatum Reveals Novel Aspects of the Mode of Action of the Antifungal Protein AfpB.Microbiology spectrum · 2023Article
- An efficient Agrobacterium-mediated system based on the pyrG auxotrophic marker for recombinant expression in the filamentous fungus Penicillium rubens.Biotechnology letters · 2023Article
- Confirmation of the Disulfide Connectivity and Strategies for Chemical Synthesis of the Four-Disulfide-Bond-StabilizedJournal of natural products · 2023Article
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- Acetylcholine Esterase Inhibitory Effect, Antimicrobial, Antioxidant, Metabolomic Profiling, and an In Silico Study of Non-Polar Extract of The Halotolerant Marine FungusMicroorganisms · 2023Article
- DMSO-Induced Unfolding of the Antifungal Disulfide Protein PAF and Its Inactive Variant: A Combined NMR and DSC Study.International journal of molecular sciences · 2023Article
- FungalBraid 2.0: expanding the synthetic biology toolbox for the biotechnological exploitation of filamentous fungi.Frontiers in bioengineering and biotechnology · 2023Article
- Article
- TheJournal of fungi (Basel, Switzerland) · 2022Article
- Small, Cationic Antifungal Proteins from Filamentous Fungi InhibitMicrobiology spectrum · 2022Article
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Authors and funding
11 authors at 4 institutions in 3 countries.
Funding
Abstract
backgroundSmall, cysteine-rich and cationic antifungal proteins (APs) from filamentous ascomycetes, such as NFAP from Neosartorya fischeri and PAF from Penicillium chrysogenum, are promising candidates for novel drug development. A prerequisite for their application is a detailed knowledge about their structure-function relation and mode of action, which would allow protein modelling to enhance their toxicity and specificity. Technologies for structure analyses, such as electronic circular dichroism (ECD) or NMR spectroscopy, require highly purified samples and in case of NMR milligrams of uniformly
resultsThe APs PAF, PAF mutants and NFAP were expressed in a P. chrysogenum ∆paf mutant strain that served as perfect microbial expression factory. This strain lacks the paf-gene coding for the endogenous antifungal PAF and is resistant towards several APs from other ascomycetes. The expression of the recombinant proteins was under the regulation of the strong paf promoter, and the presence of a paf-specific pre-pro sequence warranted the secretion of processed proteins into the supernatant. The use of defined minimal medium allowed a single-step purification of the recombinant proteins. The expression system could be extended to express PAF in the related fungus Penicillium digitatum, which does not produce detectable amounts of APs, demonstrating the versatility of the approach. The molecular masses, folded structures and antifungal activity of the recombinant proteins were analysed by ESI-MS, ECD and NMR spectroscopy and growth inhibition assays.
conclusionThis study demonstrates the implementation of a paf promoter driven expression cassettes for the production of cysteine-rich, cationic, APs in different Penicillium species. The system is a perfect tool for the generation of correctly folded proteins with high quality for structure-function analyses.
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