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Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum: A comparative study of PAF and PAFB.
Huber, A; Galgóczy, L; Váradi, G; Holzknecht, J; Kakar, A; Malanovic, N; Leber, R; Koch, J; Keller, M A; Batta, G; Tóth, G K; Marx, F.
Afiliación
  • Huber A; Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
  • Galgóczy L; Institute of Plant Biology, Biological Research Centre, 6726 Szeged, Hungary; Department of Biotechnology, Faculty of Science and Informatics, University of Szeged, 6726 Szeged, Hungary.
  • Váradi G; Department of Medical Chemistry, Faculty of Medicine, University of Szeged, 6720 Szeged, Hungary.
  • Holzknecht J; Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
  • Kakar A; Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria.
  • Malanovic N; Institute of Molecular Biosciences, Biophysics Division, University of Graz, Graz, Austria.
  • Leber R; Institute of Molecular Biosciences, Biophysics Division, University of Graz, Graz, Austria.
  • Koch J; Institute of Human Genetics, Medical University of Innsbruck, Austria.
  • Keller MA; Institute of Human Genetics, Medical University of Innsbruck, Austria.
  • Batta G; Department of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, 4032 Debrecen, Hungary.
  • Tóth GK; Department of Medical Chemistry, Faculty of Medicine, University of Szeged, 6720 Szeged, Hungary; MTA-SZTE Biomimetic Systems Research Group, University of Szeged, 6720 Szeged, Hungary.
  • Marx F; Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, 6020 Innsbruck, Austria. Electronic address: florentine.marx@i-med.ac.at.
Biochim Biophys Acta Biomembr ; 1862(8): 183246, 2020 08 01.
Article en En | MEDLINE | ID: mdl-32142818
The filamentous fungus Penicillium chrysogenum Q176 secretes the antimicrobial proteins (AMPs) PAF and PAFB, which share a compact disulfide-bond mediated, ß-fold structure rendering them highly stable. These two AMPs effectively inhibit the growth of human pathogenic fungi in micromolar concentrations and exhibit antiviral potential without causing cytotoxic effects on mammalian cells in vitro and in vivo. The antifungal mechanism of action of both AMPs is closely linked to - but not solely dependent on - the lipid composition of the fungal cell membrane and requires a strictly regulated protein uptake into the cell, indicating that PAF and PAFB are not canonical membrane active proteins. Variations in their antifungal spectrum and their killing dynamics point towards a divergent mode of action related to their physicochemical properties and surface charge distribution. In this review, we relate characteristic features of PAF and PAFB to the current knowledge about other AMPs of different sources. In addition, we present original data that have never been published before to substantiate our assumptions and provide evidences that help to explain and understand better the mechanistic function of PAF and PAFB. Finally, we underline the promising potential of PAF and PAFB as future antifungal therapeutics.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Fúngicas / Péptidos Catiónicos Antimicrobianos / Micosis / Antifúngicos Límite: Humans Idioma: En Revista: Biochim Biophys Acta Biomembr Año: 2020 Tipo del documento: Article País de afiliación: Austria Pais de publicación: Países Bajos
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Proteínas Fúngicas / Péptidos Catiónicos Antimicrobianos / Micosis / Antifúngicos Límite: Humans Idioma: En Revista: Biochim Biophys Acta Biomembr Año: 2020 Tipo del documento: Article País de afiliación: Austria Pais de publicación: Países Bajos