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001-es BibID:	BIBFORM090877
035-os BibID:	(cikkazonosító)1183 (scopus)85099978064 (wos)000615359000001
Első szerző:	Czajlik András (gyógyszerész)
Cím:	Solution Structure, Dynamics, and New Antifungal Aspects of the Cysteine-Rich Miniprotein PAFC / András Czajlik, Jeanett Holzknecht, László Galgóczy, Liliána Tóth, Péter Poór, Attila Ördög, Györgyi Váradi, Alexander Kühbacher, Attila Borics, Gábor K. Tóth, Florentine Marx, Gyula Batta
Dátum:	2021
ISSN:	1661-6596 1422-0067
Megjegyzések:	The genome of Penicillium chrysogenum Q176 contains a gene coding for the 88-amino-acid (aa)-long glycine- and cysteine-rich P. chrysogenum antifungal protein C (PAFC). After maturation, the secreted antifungal miniprotein (MP) comprises 64 aa and shares 80% aa identity with the bubble protein (BP) from Penicillium brevicompactum, which has a published X-ray structure. Our team expressed isotope (15N, 13C)-labeled, recombinant PAFC in high yields, which allowed us to determine the solution structure and molecular dynamics by nuclear magnetic resonance (NMR) experiments. The primary structure of PAFC is dominated by 14 glycines, and therefore, whether the four disulfide bonds can stabilize the fold is challenging. Indeed, unlike the few published solution structures of other antifungal MPs from filamentous ascomycetes, the NMR data indicate that PAFC has shorter secondary structure elements and lacks the typical ??-barrel structure, though it has a positively charged cavity and a hydrophobic core around the disulfide bonds. Some parts within the two putative ??-core motifs exhibited enhanced dynamics according to a new disorder index presentation of 15N-NMR relaxation data. Furthermore, we also provided a more detailed insight into the antifungal spectrum of PAFC, with specific emphasis on fungal plant pathogens. Our results suggest that PAFC could be an effective candidate for the development of new antifungal strategies in agriculture.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Penicillium chrysogenum antifungal protein PAFC γ-core motif solution structure dynamics nuclear magnetic resonance plant protection
Megjelenés:	International Journal of Molecular Sciences. - 22 : 3 (2021), p. 1-23. -
További szerzők:	Holzknecht, Jeanett Galgóczy László (1950-) Tóth Liliána Poór Péter Ördög Attila Váradi Györgyi Kühbacher, Alexander Borics Attila Tóth Gábor K. Marx, Florentine Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:	NKFIH FK 134343 Egyéb NKFIH PD 134284 Egyéb GINOP-2.3.2-15-2016-00008 GINOP GINOP-2.3.3-15-2016-00004 GINOP
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001-es BibID:	BIBFORM086163
035-os BibID:	(cikkazonosító)183246
Cím:	Two small, cysteine-rich and cationic antifungal proteins from Penicillium chrysogenum : a comparative study of PAF and PAFB / A. Huber, L. Galgóczy, G. Váradi, J. Holzknecht, A. Kakar, N. Malanovic, R. Leber, J. Koch, M. A. Keller, G. Batta, G. K. Tóth, F. Marx
Dátum:	2020
ISSN:	0005-2736
Megjegyzések:	The filamentous fungus Penicillium chrysogenum Q176 secretes the antimicrobial proteins (AMPs) PAF and PAFB, which share a compact disulfide-bond mediated, beta-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.
Tárgyszavak:	Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk Antimicrobial proteins and peptides Penicillium chrysogenum beta-Fold structure gamma-Core Fungal membrane lipids Endocytosis Apoptosis
Megjelenés:	Biochimica et Biophysica Acta (BBA). Biomembranes. - 1862 : 8 (2020), p. 1-14. -
További szerzők:	Huber Anna Galgóczy László (1950-) Váradi Györgyi Holzknecht, Jeanett Kakar, A. Malanovic, N. Leber, R. Koch, J. Keller, M. A. Batta Gyula (1953-) (molekula-szerkezet kutató) Tóth Gábor K. Marx, Florentine
Pályázati támogatás:	GINOP-2.3.2-15-2016-00008 GINOP GINOP-2.3.3-15-2016-00004 GINOP GINOP-2.3.2-15-2016-00014 GINOP NKFI 20391-3/2018/FEKUSTRAT Egyéb TUDFO/47138-1/2019-ITM FIKP Egyéb
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