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Florentine Marx - One of the best experts on this subject based on the ideXlab platform.
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Nutrient Excess Triggers the Expression of the Penicillium chrysogenum Antifungal Protein PAFB
Microorganisms, 2019Co-Authors: Anna Huber, Hannah Lerchster, Florentine MarxAbstract:Nutrient limitation and nonfavorable growth conditions have been suggested to be major triggers for the expression of small, cysteine-rich antimicrobial Proteins (AMPs) of fungal origin, e.g., the Penicillium chrysogenum Antifungal Protein (PAF), the Aspergillus giganteus Antifungal Protein (AFP), the Aspergillus niger Antifungal Protein (AnAFP). Therefore, these AMPs have been considered to be fungal secondary metabolite products. In contrast, the present study revealed that the expression of the PAF-related AMP P. chrysogenum Antifungal Protein B (PAFB) is strongly induced under nutrient excess during the logarithmic growth phase, whereas PAFB remained under the detection level in the supernatant of cultures grown under nutrient limitation. The efficiency of the pafB-promoter to induce PAFB expression was compared with that of two P. chrysogenum promoters that are well established for recombinant Protein production: the paf-promoter and the xylose-inducible promoter of the xylanase gene, xylP. The inducibility of the pafB-promoter was superior to that of the xylP-promoter yielding comparable PAFB amounts as under the regulation of the paf-promoter. We conclude that (i) differences in the expression regulation of AMPs suggest distinct functional roles in the producer beyond their Antifungal activity; and (ii) the pafB-promoter is a promising tool for recombinant Protein production in P. chrysogenum, as it guarantees strong gene expression with the advantage of inducibility.
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Insight into the Antifungal mechanism of Neosartorya fischeri Antifungal Protein
Protein & cell, 2015Co-Authors: Máté Virágh, Florentine Marx, Csaba Vágvölgyi, Annamária Marton, Csaba Vizler, Liliána Tóth, László GalgóczyAbstract:Small, cysteine-rich, highly stable Antifungal Proteins secreted by filamentous Ascomycetes have great potential for the development of novel Antifungal strategies. However, their practical application is still limited due to their not fully clarified mode of action. The aim of this work was to provide a deep insight into the Antifungal mechanism of Neosartorya fischeri Antifungal Protein (NFAP), a novel representative of this Protein group. Within a short exposure time to NFAP, reduced cellular metabolism, apoptosis induction, changes in the actin distribution and chitin deposition at the hyphal tip were observed in NFAP-sensitive Aspergillus nidulans. NFAP did show neither a direct membrane disrupting-effect nor uptake by endocytosis. Investigation of A. nidulans signalling mutants revealed that NFAP activates the cAMP/Protein kinase A pathway via G-Protein signalling which leads to apoptosis and inhibition of polar growth. In contrast, NFAP does not have any influence on the cell wall integrity pathway, but an unknown cell wall integrity pathway-independent mitogen activated Protein kinase A-activated target is assumed to be involved in the cell death induction. Taken together, it was concluded that NFAP shows similarities, but also differences in its mode of Antifungal action compared to two most investigated NFAP-related Proteins from Aspergillus giganteus and Penicillium chrysogenum.
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the small molecular mass Antifungal Protein of penicillium chrysogenum a mechanism of action oriented review
Journal of Basic Microbiology, 2011Co-Authors: Éva Leiter, Barbara Kovacs, Valeria Tomori, Nak Jung Kwon, Tamas Emri, Florentine Marx, Gyula Batta, Nikoletta Hegedűs, Laszlo CsernochAbstract:The β-lactam producing filamentous fungus Penicillium chrysogenum secretes a 6.25 kDa small molecular mass Antifungal Protein, PAF, which has a highly stable, compact 3D structure and is effective against a wide spectrum of plant and zoo pathogenic fungi. Its precise physiological functions and mode of action need to be elucidated before considering possible biomedical, agricultural or food technological applications. According to some more recent experimental data, PAF plays an important role in the fine-tuning of conidiogenesis in Penicillium chrysogenum. PAF triggers apoptotic cell death in sensitive fungi, and cell death signaling may be transmitted through two-component systems, heterotrimeric G Protein coupled signal transduction and regulatory networks as well as via alteration of the Ca2+-homeostasis of the cells. Possible biotechnological applications of PAF are also outlined in the review. (© 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)
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The Aspergillus giganteus Antifungal Protein AFPNN5353 activates the cell wall integrity pathway and perturbs calcium homeostasis
BMC microbiology, 2011Co-Authors: Ulrike Binder, Mojca Benčina, Andrea Eigentler, Vera Meyer, Florentine MarxAbstract: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.
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The small molecular mass Antifungal Protein of Penicillium chrysogenum--a mechanism of action oriented review.
Journal of basic microbiology, 2011Co-Authors: Nikoletta Hegedüs, Éva Leiter, Barbara Kovacs, Valeria Tomori, Nak Jung Kwon, Tamas Emri, Florentine Marx, Gyula Batta, Laszlo Csernoch, Hubertus HaasAbstract:The β-lactam producing filamentous fungus Penicillium chrysogenum secretes a 6.25 kDa small molecular mass Antifungal Protein, PAF, which has a highly stable, compact 3D structure and is effective against a wide spectrum of plant and zoo pathogenic fungi. Its precise physiological functions and mode of action need to be elucidated before considering possible biomedical, agricultural or food technological applications. According to some more recent experimental data, PAF plays an important role in the fine-tuning of conidiogenesis in Penicillium chrysogenum. PAF triggers apoptotic cell death in sensitive fungi, and cell death signaling may be transmitted through two-component systems, heterotrimeric G Protein coupled signal transduction and regulatory networks as well as via alteration of the Ca(2+) -homeostasis of the cells. Possible biotechnological applications of PAF are also outlined in the review.
Gyula Batta - One of the best experts on this subject based on the ideXlab platform.
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calixarene mediated assembly of a small Antifungal Protein
IUCrJ, 2019Co-Authors: Jimi Marin Alex, Gyula Batta, Martin L Rennie, Sylvain Engilberge, Gabor Lehoczki, Hajdu Dorottya, Adam Fizil, Peter B CrowleyAbstract:Synthetic macrocycles such as calixarenes and cucurbiturils are increasingly applied as mediators of Protein assembly and crystallization. The macrocycle can facilitate assembly by providing a surface on which two or more Proteins bind simultaneously. This work explores the capacity of the sulfonato-calix[n]arene (sclxn) series to effect crystallization of PAF, a small, cationic Antifungal Protein. Co-crystallization with sclx4, sclx6 or sclx8 led to high-resolution crystal structures. In the absence of sclxn, diffraction-quality crystals of PAF were not obtained. Interestingly, all three sclxn were bound to a similar patch on PAF. The largest and most flexible variant, sclx8, yielded a dimer of PAF. Complex formation was evident in solution via NMR and ITC experiments, showing more pronounced effects with increasing macrocycle size. In agreement with the crystal structure, the ITC data suggested that sclx8 acts as a bidentate ligand. The contributions of calixarene size/conformation to Protein recognition and assembly are discussed. Finally, it is suggested that the conserved binding site for anionic calixarenes implicates this region of PAF in membrane binding, which is a prerequisite for Antifungal activity.
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the small molecular mass Antifungal Protein of penicillium chrysogenum a mechanism of action oriented review
Journal of Basic Microbiology, 2011Co-Authors: Éva Leiter, Barbara Kovacs, Valeria Tomori, Nak Jung Kwon, Tamas Emri, Florentine Marx, Gyula Batta, Nikoletta Hegedűs, Laszlo CsernochAbstract:The β-lactam producing filamentous fungus Penicillium chrysogenum secretes a 6.25 kDa small molecular mass Antifungal Protein, PAF, which has a highly stable, compact 3D structure and is effective against a wide spectrum of plant and zoo pathogenic fungi. Its precise physiological functions and mode of action need to be elucidated before considering possible biomedical, agricultural or food technological applications. According to some more recent experimental data, PAF plays an important role in the fine-tuning of conidiogenesis in Penicillium chrysogenum. PAF triggers apoptotic cell death in sensitive fungi, and cell death signaling may be transmitted through two-component systems, heterotrimeric G Protein coupled signal transduction and regulatory networks as well as via alteration of the Ca2+-homeostasis of the cells. Possible biotechnological applications of PAF are also outlined in the review. (© 2011 WILEY-VCH Verlag GmbH & Co. KGaA, Weinheim)
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The small molecular mass Antifungal Protein of Penicillium chrysogenum--a mechanism of action oriented review.
Journal of basic microbiology, 2011Co-Authors: Nikoletta Hegedüs, Éva Leiter, Barbara Kovacs, Valeria Tomori, Nak Jung Kwon, Tamas Emri, Florentine Marx, Gyula Batta, Laszlo Csernoch, Hubertus HaasAbstract:The β-lactam producing filamentous fungus Penicillium chrysogenum secretes a 6.25 kDa small molecular mass Antifungal Protein, PAF, which has a highly stable, compact 3D structure and is effective against a wide spectrum of plant and zoo pathogenic fungi. Its precise physiological functions and mode of action need to be elucidated before considering possible biomedical, agricultural or food technological applications. According to some more recent experimental data, PAF plays an important role in the fine-tuning of conidiogenesis in Penicillium chrysogenum. PAF triggers apoptotic cell death in sensitive fungi, and cell death signaling may be transmitted through two-component systems, heterotrimeric G Protein coupled signal transduction and regulatory networks as well as via alteration of the Ca(2+) -homeostasis of the cells. Possible biotechnological applications of PAF are also outlined in the review.
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functional aspects of the solution structure and dynamics of paf a highly stable Antifungal Protein from penicillium chrysogenum
FEBS Journal, 2009Co-Authors: Gyula Batta, Ulrike Binder, Lydia Kaiserer, Terez Barna, Zoltan Gaspari, Szabolcs Sandor, Katalin E Kover, Bettina Sarg, Anil Kumar Chhillar, Andrea EigentlerAbstract:Penicillium Antifungal Protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candidate against the often lethal Aspergillus infections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-Protein coupled signalling followed by apoptosis. In the present study, the solution structure of this small, cationic, Antifungal Protein from Penicillium chrysogenum is determined by NMR. We demonstrate that PAF belongs to the structural classification of Proteins fold class of its closest homologue Antifungal Protein from Aspergillus giganteus. PAF comprises five β-strands forming two orthogonally packed β-sheets that share a common interface. The ambiguity in the assignment of two disulfide bonds out of three was investigated by NMR dynamics, together with restrained molecular dynamics calculations. The clue could not be resolved: the two ensembles with different disulfide patterns and the one with no S–S bond exhibit essentially the same fold. 15N relaxation dispersion and interference experiments did not reveal disulfide bond rearrangements via slow exchange. The measured order parameters and the 3.0 ns correlation time are appropriate for a compact monomeric Protein of this size. Using site-directed mutagenesis, we demonstrate that the highly-conserved and positively-charged lysine-rich surface region enhances the toxicity of PAF. However, the binding capability of the oligosaccharide/oligonucleotide binding fold is reduced in PAF compared to Antifungal Protein as a result of less solvent-exposed aromatic regions, thus explaining the absence of chitobiose binding. The present study lends further support to the understanding of the documented substantial differences between the mode of action of two highly homologous Antifungal Proteins.
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Functional aspects of the solution structure and dynamics of PAF – a highly‐stable Antifungal Protein from Penicillium chrysogenum
The FEBS journal, 2009Co-Authors: Gyula Batta, Ulrike Binder, Lydia Kaiserer, Terez Barna, Zoltan Gaspari, Szabolcs Sandor, Katalin E Kover, Bettina Sarg, Anil Kumar Chhillar, Andrea EigentlerAbstract:Penicillium Antifungal Protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candidate against the often lethal Aspergillus infections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-Protein coupled signalling followed by apoptosis. In the present study, the solution structure of this small, cationic, Antifungal Protein from Penicillium chrysogenum is determined by NMR. We demonstrate that PAF belongs to the structural classification of Proteins fold class of its closest homologue Antifungal Protein from Aspergillus giganteus. PAF comprises five β-strands forming two orthogonally packed β-sheets that share a common interface. The ambiguity in the assignment of two disulfide bonds out of three was investigated by NMR dynamics, together with restrained molecular dynamics calculations. The clue could not be resolved: the two ensembles with different disulfide patterns and the one with no S–S bond exhibit essentially the same fold. 15N relaxation dispersion and interference experiments did not reveal disulfide bond rearrangements via slow exchange. The measured order parameters and the 3.0 ns correlation time are appropriate for a compact monomeric Protein of this size. Using site-directed mutagenesis, we demonstrate that the highly-conserved and positively-charged lysine-rich surface region enhances the toxicity of PAF. However, the binding capability of the oligosaccharide/oligonucleotide binding fold is reduced in PAF compared to Antifungal Protein as a result of less solvent-exposed aromatic regions, thus explaining the absence of chitobiose binding. The present study lends further support to the understanding of the documented substantial differences between the mode of action of two highly homologous Antifungal Proteins.
Andrea Eigentler - One of the best experts on this subject based on the ideXlab platform.
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The Aspergillus giganteus Antifungal Protein AFPNN5353 activates the cell wall integrity pathway and perturbs calcium homeostasis
BMC microbiology, 2011Co-Authors: Ulrike Binder, Mojca Benčina, Andrea Eigentler, Vera Meyer, Florentine MarxAbstract: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.
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functional aspects of the solution structure and dynamics of paf a highly stable Antifungal Protein from penicillium chrysogenum
FEBS Journal, 2009Co-Authors: Gyula Batta, Ulrike Binder, Lydia Kaiserer, Terez Barna, Zoltan Gaspari, Szabolcs Sandor, Katalin E Kover, Bettina Sarg, Anil Kumar Chhillar, Andrea EigentlerAbstract:Penicillium Antifungal Protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candidate against the often lethal Aspergillus infections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-Protein coupled signalling followed by apoptosis. In the present study, the solution structure of this small, cationic, Antifungal Protein from Penicillium chrysogenum is determined by NMR. We demonstrate that PAF belongs to the structural classification of Proteins fold class of its closest homologue Antifungal Protein from Aspergillus giganteus. PAF comprises five β-strands forming two orthogonally packed β-sheets that share a common interface. The ambiguity in the assignment of two disulfide bonds out of three was investigated by NMR dynamics, together with restrained molecular dynamics calculations. The clue could not be resolved: the two ensembles with different disulfide patterns and the one with no S–S bond exhibit essentially the same fold. 15N relaxation dispersion and interference experiments did not reveal disulfide bond rearrangements via slow exchange. The measured order parameters and the 3.0 ns correlation time are appropriate for a compact monomeric Protein of this size. Using site-directed mutagenesis, we demonstrate that the highly-conserved and positively-charged lysine-rich surface region enhances the toxicity of PAF. However, the binding capability of the oligosaccharide/oligonucleotide binding fold is reduced in PAF compared to Antifungal Protein as a result of less solvent-exposed aromatic regions, thus explaining the absence of chitobiose binding. The present study lends further support to the understanding of the documented substantial differences between the mode of action of two highly homologous Antifungal Proteins.
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Functional aspects of the solution structure and dynamics of PAF – a highly‐stable Antifungal Protein from Penicillium chrysogenum
The FEBS journal, 2009Co-Authors: Gyula Batta, Ulrike Binder, Lydia Kaiserer, Terez Barna, Zoltan Gaspari, Szabolcs Sandor, Katalin E Kover, Bettina Sarg, Anil Kumar Chhillar, Andrea EigentlerAbstract:Penicillium Antifungal Protein (PAF) is a promising antimycotic without toxic effects on mammalian cells and therefore may represent a drug candidate against the often lethal Aspergillus infections that occur in humans. The pathogenesis of PAF on sensitive fungi involves G-Protein coupled signalling followed by apoptosis. In the present study, the solution structure of this small, cationic, Antifungal Protein from Penicillium chrysogenum is determined by NMR. We demonstrate that PAF belongs to the structural classification of Proteins fold class of its closest homologue Antifungal Protein from Aspergillus giganteus. PAF comprises five β-strands forming two orthogonally packed β-sheets that share a common interface. The ambiguity in the assignment of two disulfide bonds out of three was investigated by NMR dynamics, together with restrained molecular dynamics calculations. The clue could not be resolved: the two ensembles with different disulfide patterns and the one with no S–S bond exhibit essentially the same fold. 15N relaxation dispersion and interference experiments did not reveal disulfide bond rearrangements via slow exchange. The measured order parameters and the 3.0 ns correlation time are appropriate for a compact monomeric Protein of this size. Using site-directed mutagenesis, we demonstrate that the highly-conserved and positively-charged lysine-rich surface region enhances the toxicity of PAF. However, the binding capability of the oligosaccharide/oligonucleotide binding fold is reduced in PAF compared to Antifungal Protein as a result of less solvent-exposed aromatic regions, thus explaining the absence of chitobiose binding. The present study lends further support to the understanding of the documented substantial differences between the mode of action of two highly homologous Antifungal Proteins.
Frans Borremans - One of the best experts on this subject based on the ideXlab platform.
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determination of the three dimensional solution structure of raphanus sativus Antifungal Protein 1 by 1h nmr
Journal of Molecular Biology, 1998Co-Authors: Franky Fant, Wim F Vranken, Willem F. Broekaert, Frans BorremansAbstract:Abstract Raphanus sativus Antifungal Protein 1 (Rs-AFP1) is a 51 amino acid residue plant defensin isolated from radish ( Raphanus sativus L.) seeds. The three-dimensional structure in aqueous solution has been determined from two-dimensional 1 H NMR data recorded at 500 MHz using the DIANA/REDAC calculation protocols. Experimental constraints consisted of 787 interproton distances extracted from NOE cross-peaks, 89 torsional constraints from 106 vicinal interproton coupling constants and 32 stereospecific assignments of prochiral protons. Further refinement by simulated annealing resulted in a set of 20 structures having pairwise root-mean-square differences of 1.35(±0.35) A over the backbone heavy atoms and 2.11(±0.46) A over all heavy atoms. The molecule adopts a compact globular fold comprising an α-helix from Asn18 till Leu28 and a triple-stranded β-sheet (β1=Lys2-Arg6, β2=His33-Tyr38 and β3=His43-Pro50). The central strand of this β-sheet is connected by two disulfide bridges (Cys21–Cys45 and Cys25–Cys47) to the α-helix. The connection between β-strand 2 and 3 is formed by a type VIa β-turn. Even the loop (Pro7 to Asn17) between β-strand 1 and the α-helix is relatively well defined. The structure of Raphanus sativus Antifungal Protein 1 features all the characteristics of the “cysteine stabilized αβ motif”. A comparison of the complete structure and of the regions important for interaction with the fungal receptor according to a mutational study, is made with the structure of γ-thionin, a plant defensin that has no Antifungal activity. It is concluded that this interaction is both electrostatic and specific, and some possible scenarios for the mode of action are given.
Félix Núñez - One of the best experts on this subject based on the ideXlab platform.
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Increased chitin biosynthesis contributes to the resistance of Penicillium polonicum against the Antifungal Protein PgAFP.
Applied microbiology and biotechnology, 2015Co-Authors: Josué Delgado, Rebecca A. Owens, Sean Doyle, Miguel A. Asensio, Félix NúñezAbstract:Antifungal Proteins from molds have been proposed as a valuable tool against unwanted molds, but the resistance of some fungi limits their use. Resistance to antimicrobial peptides has been suggested to be due to lack of interaction with the mold or to a successful response. The Antifungal Protein PgAFP produced by Penicillium chrysogenum inhibits the growth of various ascomycetes, but not Penicillium polonicum. To study the basis for resistance to this Antifungal Protein, localization of PgAFP and metabolic, structural, and morphological changes were investigated in P. polonicum. PgAFP bound the outer layer of P. polonicum but not regenerated chitin, suggesting an interaction with specific molecules. Comparative two-dimensional gel electrophoresis (2D-PAGE) and comparative quantitative proteomics revealed changes in the relative abundance of several Proteins from ribosome, spliceosome, metabolic, and biosynthesis of secondary metabolite pathways. The proteome changes and an altered permeability reveal an active reaction of P. polonicum to PgAFP. The successful response of the resistant mold seems to be based on the higher abundance of Protein Rho GTPase Rho1 that would lead to the increased chitin deposition via cell wall integrity (CWI) signaling pathway. Thus, combined treatment with chitinases could provide a complementary means to combat resistance to Antifungal Proteins.
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Impact of the Antifungal Protein PgAFP from Penicillium chrysogenum on the Protein profile in Aspergillus flavus
Applied microbiology and biotechnology, 2015Co-Authors: Josué Delgado, Rebecca A. Owens, Sean Doyle, Miguel A. Asensio, Félix NúñezAbstract:Antifungal Proteins produced by molds are generally small, highly basic, and cysteine-rich. The best known effects of these Proteins include morphological changes, metabolic inactivation, and membrane perturbation on sensitive fungi. Reactive oxygen species (ROS) generation leads to apoptosis, with G -Protein playing a key role in transduction of cell death signals. The Antifungal Protein PgAFP from Penicillium chrysogenum inhibits growth of some toxigenic molds. Here we analyzed the effect of the Antifungal Protein PgAFP on the growth of Aspergillus flavus. For this, comparative proteomic analysis was used to identify the whole Protein profile and Protein change in abundance after PgAFP treatment. PgAFP provoked metabolic changes related to reduced energy metabolism, cell wall integrity alteration, and increased stress response due to higher levels of ROS. The observed changes in Protein abundance, favoring a higher glutathione concentration as well as the increased abundance in heat shock Proteins, do not seem to be enough to avoid necrosis. The decreased chitin deposition observed in PgAFP-treated A. flavus is attributed to a lower relative quantity of Rho1. The reduced relative abundance of a β subunit of G -Protein seems to be the underlying reason for modulation of apoptosis in PgAFP-treated A. flavus hyphae. We propose Rho1 and G -Protein subunit β CpcB to be the main factors in the mode of action of PgAFP in A. flavus. Additionally, enzymes essential for the biosynthesis of aflatoxin were no longer detectable in A. flavus hyphae at 24 h, following treatment with PgAFP. This presents a promising effect of PgAFP, which may prevent A. flavus from producing mycotoxins. However, the impact of PgAFP on actual aflatoxin production requires further study.
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characterization of the novel Antifungal Protein pgafp and the encoding gene of penicillium chrysogenum
Peptides, 2010Co-Authors: Andrea Rodriguezmartin, Félix Núñez, Raquel Acosta, Susan Liddell, Ma Jose Benito, Miguel A. AsensioAbstract:Abstract The strain RP42C from Penicillium chrysogenum produces a small Protein PgAFP that inhibits the growth of some toxigenic molds. The molecular mass of the Protein determined by electrospray ionization mass spectrometry (ESI-MS) was 6 494 Da. PgAFP showed a cationic character with an estimated pI value of 9.22. Upon chemical and enzymatic treatments of PgAFP, no evidence for N- or O-glycosylations was obtained. Five partial sequences of PgAFP were obtained by Edman degradation and by ESI-MS/MS after trypsin and chymotrypsin digestions. Using degenerate primers from these peptide sequences, a segment of 70 bp was amplified by PCR from pgafp gene. 5′- and 3′-ends of pgafp were obtained by RACE-PCR with gene-specific primers designed from the 70 bp segment. The complete pgafp sequence of 404 bp was obtained using primers designed from 5′- and 3′-ends. Comparison of genomic and cDNA sequences revealed a 279 bp coding region interrupted by two introns of 63 and 62 bp. The precursor of the Antifungal Protein consists of 92 amino acids and appears to be processed to the mature 58 amino acids PgAFP. The deduced amino acid sequence of the mature Protein shares 79% identity to the Antifungal Protein Anafp from Aspergillus niger . PgAFP is a new Protein that belongs to the group of small, cysteine-rich, and basic Proteins with Antifungal activity produced by ascomycetes. Given that P. chrysogenum is regarded as safe mold commonly found in foods, PgAFP may be useful to prevent growth of toxigenic molds in food and agricultural products.