TY  - JOUR
SP  - Azonosító: 183246
AV  - public
EP  - Terjedelem: 14 p
UR  - http://doi.org/10.1016/j.bbamem.2020.183246
A1  -  Huber Anna
A1  -  Galgóczi László Norbert
A1  -  Váradi Györgyi
A1  -  Holzknecht Jeanett
A1  -  Kakar A.
A1  -  Malanovic Nermina
A1  -  Leber Regina
A1  -  Koch Jakob
A1  -  Keller Markus Andreas
A1  -  Batta Gyula
A1  -  Tóth Gábor
A1  -  Marx Florentine
SN  - 0005-2736
IS  - 8
VL  - 1862
TI  - Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum : A comparative study of PAF and PAFB
ID  - publicatio19541
N1  - Funding Agency and Grant Number: Hungarian National Research, Development and Innovation (NKFI) Office [ANN 131341, GINOP-2.3.2-15-2016-00014, 20391-3/2018/FEKUSTRAT]; New National Excellence Program of the Ministry for Innovation and Technology [UNKP-19-4]; Janos Bolyai Research Scholarship of the Hungarian Academy of SciencesHungarian Academy of Sciences; European Regional Development FundEuropean Union (EU) [GINOP-2.3.2-15-2016-00008, GINOP-2.3.3-15-2016-00004]; Ministry for Innovation and Technology (ITM) [TUDFO/47138-1/2019-ITM FIKP]; Austrian Science FundAustrian Science Fund (FWF) [FWF P25894-B20, I1644-B20, I3132-B21]; EUEuropean Union (EU);  [PD 131340]
            Funding text: The authors want to thank Karl Lohner for the helpful discussion and Sandor Kocsube for advices in the phylogenetic analysis. Research has been funded to F.M. by the Austrian Science Fund (FWF P25894-B20, I1644-B20, I3132-B21), and to L.G. by the Postdoctoral Excellence Program (PD 131340), the bilateral Austrian-Hungarian Joint Research Project (ANN 131341) of the Hungarian National Research, Development and Innovation (NKFI) Office. Present work of L.G. is supported by UNKP-19-4 New National Excellence Program of the Ministry for Innovation and Technology. L.G. has been supported by the Janos Bolyai Research Scholarship of the Hungarian Academy of Sciences. Structural research was supported by the EU and co-financed by the European Regional Development Fund under the projects GINOP-2.3.2-15-2016-00008 to G.B. and GINOP-2.3.3-15-2016-00004 (access to 700 MHz NMR facilities). Synthetic work was supported by GINOP-2.3.2-15-2016-00014 and 20391-3/2018/FEKUSTRAT of the Hungarian National Research, Development and Innovation (NKFI) Office, and by TUDFO/47138-1/2019-ITM FIKP of the Ministry for Innovation and Technology (ITM).
Institute of Molecular Biology, Biocenter, Medical University of Innsbruck, Innsbruck, 6020, Austria            
            Institute of Plant Biology, Biological Research Centre, Szeged, 6726, Hungary            
            Department of Biotechnology, Faculty of Science and Informatics, University of Szeged, Szeged, 6726, Hungary            
            Department of Medical Chemistry, Faculty of Medicine, University of Szeged, Szeged, 6720, Hungary            
            Institute of Molecular Biosciences, Biophysics Division, University of Graz, Graz, Austria            
            Institute of Human Genetics, Medical University of Innsbruck, Austria            
            Department of Organic Chemistry, Faculty of Science and Technology, University of Debrecen, Debrecen, 4032, Hungary            
            MTA-SZTE Biomimetic Systems Research Group, University of Szeged, Szeged, 6720, Hungary            
            Export Date: 16 July 2020            
            CODEN: BBBMB            
            Correspondence Address: Marx, F.; Institute of Molecular Biology, Biocenter, Medical University of InnsbruckAustria; email: florentine.marx@i-med.ac.at
JF  - BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
N2  - The filamentous fungus Penicillium chrysogenum Q176 secretes the antimicrobial proteins (AMPs) PAF and PAFB, which share a compact disulfide-bond mediated, ?-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.
Y1  - 2020///
ER  -