The Experts below are selected from a list of 192 Experts worldwide ranked by ideXlab platform
Florentine Marx - One of the best experts on this subject based on the ideXlab platform.
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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, Florentine Marx, László Csernoch, Barbara Kovács, Valéria Tomori, Nak Jung Kwon, Tamás Emri, Gyula Batta, 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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Penicillium chrysogenum glucose oxidase -- a study on its antifungal effects.
Journal of applied microbiology, 2004Co-Authors: Éva Leiter, Florentine Marx, Tünde Pusztahelyi, Hubertus Haas, István PócsiAbstract:E´ .L EITER, F. MARX, T. PUSZTAHELYI, H. HAAS AND I. POCSI. 2004. Aims: Purification and characterization of the high molecular mass Candida albicans-killing protein secreted by Penicillium chrysogenum. Methods and Results: The protein was purified by a combination of ultrafiltration, chromatofocusing and gel filtration. Enzymological characteristics (relative molecular mass (Mr) ¼ 155 000, subunit structure a2 with Mr,a ¼ 76 000, isoelectric point (pI) ¼ 5AE4) were determined using SDS-PAGE and 2D-electrophoresis. N-terminal amino acid sequencing and homology search demonstrated that the antifungal protein was the glucose oxidase (GOX) of the fungus. The enzyme was cytotoxic for a series of bacteria, yeasts and filamentous fungi. Vitamin C (1AE 0m g ml )1 ) prevented oxidative cell injuries triggered by 0AE004 U GOX in Emericella nidulans cultures but bovine liver catalase was ineffective even at a GOX : catalase activity ratio of 0AE004 : 200 U. A secondary inhibition of growth in E. nidulans cultures by the oxygen-depleting GOX-catalase system was likely to replace the primary inhibition exerted by H2O2. Conclusions: Penicillium chrysogenum GOX possesses similar enzymological features to those described earlier for other Penicillium GOXs. Its cytotoxicity was dependent on the inherent antioxidant potential of the test micro-organisms. Significance and Impact of the Study: Penicillium chrysogenum GOX may find future applications in glucose biosensor production, the disinfection of medical implants or in the food industry as an antimicrobial and/or preservative agent.
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characterization of the Penicillium chrysogenum antifungal protein paf
Archives of Microbiology, 2003Co-Authors: Lydia Kaiserer, Éva Leiter, Christoph Oberparleiter, Renate Weilergorz, Wolfgang Burgstaller, Florentine MarxAbstract:The filamentous fungus Penicillium chrysogenum abundantly secretes the small, highly basic and cysteine-rich protein PAF (Penicillium antifungal protein). In this study, the antifungal activity of PAF is described. PAF inhibited the growth of a variety of filamentous fungi, including opportunistic human pathogenic and phytopathogenic fungi, whereas bacterial and yeast cells were unaffected. PAF reduced the conidial germination and hyphal extension rates in a dose-dependent manner and induced severe changes in cell morphology that resulted in crippled and distorted hyphae and atypical branching. Growth-affected hyphae suffered from oxidative stress, plasma membrane leakage, and metabolic inactivity, which points to an induction of multifactorial effects in sensitive fungi. In contrast to other known antifungal proteins, the effects of PAF were only partially antagonized by cations.
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Active Internalization of the Penicillium chrysogenum Antifungal Protein PAF in Sensitive Aspergilli
Antimicrobial agents and chemotherapy, 2003Co-Authors: Christoph Oberparleiter, Hubertus Haas, Lydia Kaiserer, Peter Ladurner, Manfred Andratsch, Florentine MarxAbstract:The Penicillium chrysogenum antifungal protein PAF inhibits the growth of various filamentous fungi. In this study, PAF was found to localize to the cytoplasm of sensitive aspergilli by indirect immunofluorescence staining. The internalization process required active metabolism and ATP and was prevented by latrunculin B, suggesting an endocytotic mechanism.
Arnold J. M. Driessen - One of the best experts on this subject based on the ideXlab platform.
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Synthetic control devices for gene regulation in Penicillium chrysogenum
2020Co-Authors: László Mózsik, Arnold J. M. Driessen, Zsófia Büttel, Roel A. L. Bovenberg, Yvonne NygårdAbstract:Synthetic biology aims at controlled gene regulation that can lead to increased production of chemicals and pharmaceuticals. In this work synthetic control devices were developed for Penicillium chrysogenum, a model filamentous fungus and industrially relevant cell factory.
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genome editing in Penicillium chrysogenum using cas9 ribonucleoprotein particles
Methods of Molecular Biology, 2018Co-Authors: Carsten Pohl, Arnold J. M. Driessen, László Mózsik, Roel A. L. Bovenberg, Yvonne NygårdAbstract:Several CRISPR/Cas9 tools have been recently established for precise genome editing in a wide range of filamentous fungi. This genome editing platform offers high flexibility in target selection and the possibility of introducing genetic deletions without the introduction of transgenic sequences . This chapter describes an approach for the transformation of Penicillium chrysogenum protoplasts with preassembled ribonucleoprotein particles (RNPs) consisting of purified Cas9 protein and in vitro transcribed single guide RNA (sgRNA) for the deletion of genome sequences or their replacement with alternative sequences. This method is potentially transferable to all fungal strains where protoplasts can be obtained from.
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Identification of a Polyketide Synthase Involved in Sorbicillin Biosynthesis by Penicillium chrysogenum
Applied and environmental microbiology, 2016Co-Authors: Oleksandr Salo, Roel A. L. Bovenberg, Fernando Guzman-chavez, Marco Ries, Peter P. Lankhorst, Rob J. Vreeken, Arnold J. M. DriessenAbstract:ABSTRACT Secondary metabolism in Penicillium chrysogenum was intensively subjected to classical strain improvement (CSI), the resulting industrial strains producing high levels of β-lactams. During this process, the production of yellow pigments, including sorbicillinoids, was eliminated as part of a strategy to enable the rapid purification of β-lactams. Here we report the identification of the polyketide synthase (PKS) gene essential for sorbicillinoid biosynthesis in P. chrysogenum. We demonstrate that the production of polyketide precursors like sorbicillinol and dihydrosorbicillinol as well as their derivatives bisorbicillinoids requires the function of a highly reducing PKS encoded by the gene Pc21g05080 ( pks13 ). This gene belongs to the cluster that was mutated and transcriptionally silenced during the strain improvement program. Using an improved β-lactam-producing strain, repair of the mutation in pks13 led to the restoration of sorbicillinoid production. This now enables genetic studies on the mechanism of sorbicillinoid biosynthesis in P. chrysogenum and opens new perspectives for pathway engineering. IMPORTANCE Sorbicillinoids are secondary metabolites with antiviral, anti-inflammatory, and antimicrobial activities produced by filamentous fungi. This study identified the gene cluster responsible for sorbicillinoid formation in Penicillium chrysogenum, which now allows engineering of this diverse group of compounds.
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genome sequencing and analysis of the filamentous fungus Penicillium chrysogenum
Nature Biotechnology, 2008Co-Authors: Marco A Van Den Berg, Richard Albang, Kaj Albermann, Carlos Garciaestrada, Natalie D Fedorova, Diana M Harris, Jean-marc Daran, Jonathan H Badger, Arnold J. M. Driessen, Wilbert H M HeijneAbstract:Penicillins and derived β-lactam antibiotics are essential in healthcare. To gain more insight into penicillin synthesis van den Berg and colleagues sequence and analyze the genome and transcriptome of the filamentous fungus Penicillium chrysogenum.
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assessment of the microbody luminal ph in the filamentous fungus Penicillium chrysogenum
Biochimica et Biophysica Acta, 2002Co-Authors: Ted R Van Der Lende, P Breeuwer, Tjakko Abee, Wil N Konings, Arnold J. M. DriessenAbstract:The enzymes of the penicillin biosynthetic pathway in Penicillium chrysogenum are located in different subcellular compartments. Consequently, penicillin pathway precursors and the biologically active penicillins have to cross one or more membranes. The final enzymatic step that is mediated by acyltransferase takes place in a microbody. The pH of the microbody lumen in penicillin producing cells has been determined with fluorescent probes and mutants of the green fluorescent protein and found to be slightly alkaline.
Shi Xinyuan - One of the best experts on this subject based on the ideXlab platform.
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Separation of chitosan from Penicillium chrysogenum mycelium and its applications
Journal of Bioactive and Compatible Polymers, 2002Co-Authors: Tan Tian-wei, Wang Binwu, Shi XinyuanAbstract:A process to separate chitosan from Penicillium chrysogenum mycelium was developed. Alkaline treatment and acetic acid extraction were used for deacetylating chitin to chitosan. The molecular weight of the chitosan was 3.6 × 104 and the degree of deacetylation was 84%. Analysis indicated that the chitosan from Penicillium chrysogenum mycelium was similar to that obtained from shrimp. The chitosan from the mycelium was used to prepare microcapsules for controlled drug release. The chitosan microcapsules reached maximum release of vitamin D2 after 10 h which avoided the problem of instability in gastric juice; the chitosan microcapsules are suitable for adsorption of vitamin D2 in intestines.
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Separation of chitosan from Penicillium chrysogenum mycelium and its applications
Journal of Bioactive and Compatible Polymers, 2002Co-Authors: Tan Tian-wei, Wang Binwu, Shi XinyuanAbstract:A process to separate chitosan from Penicillium chrysogenum mycelium was developed. Alkaline treatment and acetic acid extraction were used for deacetylating chitin to chitosan. The molecular weigh...
Xu-li Tang - One of the best experts on this subject based on the ideXlab platform.
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Two new compounds from the marine sponge derived fungus Penicillium chrysogenum.
Natural product research, 2019Co-Authors: Xiao Han, Xiangchao Luo, Dan Qiao, Xu-li TangAbstract:Two new compounds (1 and 2) were isolated from the marine sponge derived fungus Penicillium chrysogenum by using various column chromatography techniques. Their structures were elucidated by extens...
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Two new compounds from the marine sponge derived fungus Penicillium chrysogenum
2019Co-Authors: Xiao Han, Xiangchao Luo, Dan Qiao, Xu-li TangAbstract:Two new compounds (1 and 2) were isolated from the marine sponge derived fungus Penicillium chrysogenum by using various column chromatography techniques. Their structures were elucidated by extensive analysis of spectroscopic data and quantum chemical calculation. Compound 1 exhibited moderate activity against PTP1B with 2.95 ± 0.97% at the concentration of 30 μmol·L−1.
Éva Leiter - One of the best experts on this subject based on the ideXlab platform.
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Application of a low molecular weight antifungal protein from Penicillium chrysogenum (PAF) to treat pulmonary aspergillosis in mice.
Emerging microbes & infections, 2016Co-Authors: Zoltán Palicz, Éva Leiter, István Pócsi, Tamás Gáll, Sándor Kollár, Ilona Kovács, Kornél Miszti-blasius, László Csernoch, Péter SzentesiAbstract:Application of a low molecular weight antifungal protein from Penicillium chrysogenum (PAF) to treat pulmonary aspergillosis in mice
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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, Florentine Marx, László Csernoch, Barbara Kovács, Valéria Tomori, Nak Jung Kwon, Tamás Emri, Gyula Batta, 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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Penicillium chrysogenum glucose oxidase -- a study on its antifungal effects.
Journal of applied microbiology, 2004Co-Authors: Éva Leiter, Florentine Marx, Tünde Pusztahelyi, Hubertus Haas, István PócsiAbstract:E´ .L EITER, F. MARX, T. PUSZTAHELYI, H. HAAS AND I. POCSI. 2004. Aims: Purification and characterization of the high molecular mass Candida albicans-killing protein secreted by Penicillium chrysogenum. Methods and Results: The protein was purified by a combination of ultrafiltration, chromatofocusing and gel filtration. Enzymological characteristics (relative molecular mass (Mr) ¼ 155 000, subunit structure a2 with Mr,a ¼ 76 000, isoelectric point (pI) ¼ 5AE4) were determined using SDS-PAGE and 2D-electrophoresis. N-terminal amino acid sequencing and homology search demonstrated that the antifungal protein was the glucose oxidase (GOX) of the fungus. The enzyme was cytotoxic for a series of bacteria, yeasts and filamentous fungi. Vitamin C (1AE 0m g ml )1 ) prevented oxidative cell injuries triggered by 0AE004 U GOX in Emericella nidulans cultures but bovine liver catalase was ineffective even at a GOX : catalase activity ratio of 0AE004 : 200 U. A secondary inhibition of growth in E. nidulans cultures by the oxygen-depleting GOX-catalase system was likely to replace the primary inhibition exerted by H2O2. Conclusions: Penicillium chrysogenum GOX possesses similar enzymological features to those described earlier for other Penicillium GOXs. Its cytotoxicity was dependent on the inherent antioxidant potential of the test micro-organisms. Significance and Impact of the Study: Penicillium chrysogenum GOX may find future applications in glucose biosensor production, the disinfection of medical implants or in the food industry as an antimicrobial and/or preservative agent.
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characterization of the Penicillium chrysogenum antifungal protein paf
Archives of Microbiology, 2003Co-Authors: Lydia Kaiserer, Éva Leiter, Christoph Oberparleiter, Renate Weilergorz, Wolfgang Burgstaller, Florentine MarxAbstract:The filamentous fungus Penicillium chrysogenum abundantly secretes the small, highly basic and cysteine-rich protein PAF (Penicillium antifungal protein). In this study, the antifungal activity of PAF is described. PAF inhibited the growth of a variety of filamentous fungi, including opportunistic human pathogenic and phytopathogenic fungi, whereas bacterial and yeast cells were unaffected. PAF reduced the conidial germination and hyphal extension rates in a dose-dependent manner and induced severe changes in cell morphology that resulted in crippled and distorted hyphae and atypical branching. Growth-affected hyphae suffered from oxidative stress, plasma membrane leakage, and metabolic inactivity, which points to an induction of multifactorial effects in sensitive fungi. In contrast to other known antifungal proteins, the effects of PAF were only partially antagonized by cations.