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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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2.

001-es BibID:BIBFORM077292
035-os BibID:(WoS)000466621200053 (Scopus)85061541042
Első szerző:Hajdu Dorottya (biológus)
Cím:Solution structure and novel insights into phylogeny and mode of action of the Neosartorya (Aspergillus) fischeri antifungal protein (NFAP) / Hajdu Dorottya, Huber Anna, Czajlik András, Tóth Liliána, Kele Zoltán, Kocsubé Sándor, Fizil Ádám, Marx Florentine, Galgóczy László, Batta Gyula
Dátum:2019
ISSN:0141-8130
Megjegyzések:Small, cysteine-rich and cationic antifungal proteins fromnatural sources are promising candidates for the development of novel treatment strategies to prevent and combat infections caused by drug-resistant fungi. However, limited information about their structure and antifungal mechanism hampers their future applications. In the present study, we determined the solution structure, dynamics and associated solvent areas of the Neosartorya (Aspergillus) fischeri antifungal protein NFAP. Genome mining within the genus revealed the presence of orthologous genes in N. fischeri and Neosartorya spathulata, and genes encoding closely related proteins can be found in Penicillium brasiliensis and Penicillium oxalicum. We show that the tertiary structure of these putative proteins can be resolved using the structure of NFAP as reliable template for in silico prediction. Localization studies with fluorescence-labelled protein pointed at an energy-dependent uptake mechanism of NFAP in the sensitive model fungus Neurospora crassa and subsequent cytoplasmic localization coincided with cell-death induction. The presented results contribute to a better understanding of the structure/function relationship of NFAP and related proteins and pave the way towards future antifungal drug development.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Neosartorya (Aspergillus) fischeri antifungal
protein (NFAP)
Nuclear magnetic resonance (NMR)
Antifungal mechanism
Megjelenés:International Journal of Biological Macromolecules. - 129 (2019), p. 511-522.
További szerzők:Huber Anna Czajlik András (1975-) (gyógyszerész) Tóth Liliána Kele Zoltán Kocsubé Sándor Fizil Ádám (1988-) (biológus) Marx, Florentine Galgóczy László (1950-) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:GINOP-2.3.2-15-2016-00008
GINOP
GINOP-2.3.3-15-2016-00004
GINOP
PD 120808
OTKA
ANN 122833
OTKA
ANN 110821
OTKA
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3.

001-es BibID:BIBFORM072756
035-os BibID:(cikkazonosító)393 (WOS)000426785800002 (Scopus)85043257197
Első szerző:Tóth Liliána
Cím:Anti-Candidal Activity and Functional Mapping of Recombinant and Synthetic Neosartorya fischeri Antifungal Protein 2 (NFAP2) / Tóth Liliána, Váradi Györgyi, Borics Attila, Batta Gyula, Kele Zoltán, Vendrinszky Ákos, Tóth Roberta, Ficze Hargita, Tóth Gábor K., Vágvölgyi Csaba, Marx Florentine, Galgóczy László
Dátum:2018
ISSN:1664-302X
Megjegyzések:The increasing number of life-threatening Candida infections caused by antifungal drug-resistant strains urges the development of new therapeutic strategies. The small, cysteine-rich, and cationic Neosartorya fischeri antifungal protein 2 (NFAP2) effectively inhibits the growth of Candida spp. Limiting factors of its future application, are the low-yield production by the native producer, unavailable information about potential clinical application, and the unsolved relationship between the structure and function. In the present study we adopted a Penicillium chrysogenum-based expression system for bulk production of recombinant NFAP2. Furthermore, solid-phase peptide synthesis and native chemical ligation were applied to produce synthetic NFAP2. The average yield of recombinant and synthetic NFAP2 was 40- and 16-times higher than in the native producer, respectively. Both proteins were correctly processed, folded, and proved to be heat-stable. They showed the same minimal inhibitory concentrations as the native NFAP2 against clinically relevant Candida spp. Minimal inhibitory concentrations were higher in RPMI 1640 mimicking the human inner fluid than in a low ionic strength medium. The recombinant NFAP2 interacted synergistically with fluconazole, the first-line Candida therapeutic agent and significantly decreased its effective in vitro concentrations in RPMI 1640. Functional mapping with synthetic peptide fragments of NFAP2 revealed that not the evolutionary conserved antimicrobial ?-core motif, but the mid-N-terminal part of the protein influences the antifungal activity that does not depend on the primary structure of this region. Preliminary nucleic magnetic resonance measurements signed that the produced recombinant NFAP2 is suitable for further structural investigations.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Neosartorya fischeri antifungal protein 2
recombinant protein
protein synthesis
anti-candidal activity
protein structure
functional mapping
Megjelenés:Frontiers in Microbiology. - 9 : 393 (2018), p. 1-12. -
További szerzők:Váradi Györgyi Borics Attila Batta Gyula (1953-) (molekula-szerkezet kutató) Kele Zoltán Vendrinszky Ákos Tóth Roberta Ficze Hargita Tóth Gábor K. Vágvölgyi Csaba Marx, Florentine Galgóczy László (1950-)
Pályázati támogatás:PD 120808, ANN 122833, ANN 110821
OTKA
GINOP-2.3.2-15-2016-00008
GINOP
GINOP-2.3.2-15-2016-00014
GINOP
GINOP-2.3.2-15-2016-00035
GINOP
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