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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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