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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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DOI
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2.

001-es BibID:BIBFORM072198
035-os BibID:(Cikkazonosító)1751 (WOS)000423429800003 (Scopus)85041371349
Első szerző:Huber Anna
Cím:New Antimicrobial Potential and Structural Properties of PAFB: A Cationic, Cysteine-Rich Protein from Penicillium chrysogenum Q176 / Anna Huber, Dorottya Hajdu, Doris Bratschun-Khan, Zoltán Gáspári, Mihayl Varbanov, Stéphanie Philippot, Ádám Fizil, András Czajlik, Zoltán Kele, Christoph Sonderegger, László Galgóczy, Andrea Bodor, Florentine Marx, Gyula Batta
Dátum:2018
ISSN:2045-2322
Megjegyzések:Small, cysteine-rich and cationic proteins with antimicrobial activity are produced by diverse organisms of all kingdoms and represent promising molecules for drug development. The ancestor of all industrial penicillin producing strains, the ascomycete Penicillium chryosgenum Q176, secretes the extensively studied antifungal protein PAF. However, the genome of this strain harbours at least two more genes that code for other small, cysteine-rich and cationic proteins with potential antifungal activity. In this study, we characterized the pafB gene product that shows high similarity to PgAFP from P. chrysogenum R42C. Although abundant and timely regulated pafB gene transcripts were detected, we could not identify PAFB in the culture broth of P. chrysogenum Q176. Therefore, we applied a P. chrysogenum-based expression system to produce sufficient amounts of recombinant PAFB to address unanswered questions concerning the structure and antimicrobial function. Nuclear magnetic resonance (NMR)-based analyses revealed a compact [beta]-folded structure, comprising five [beta]-strands connected by four solvent exposed and flexible loops and an "abcabc" disulphide bond pattern. We identified PAFB as an inhibitor of growth of human pathogenic moulds and yeasts. Furthermore, we document for the first time an anti-viral activity for two members of the small, cysteine-rich and cationic protein group from ascomycetes.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Scientific Reports. - 8 : 1 (2018), p. 1751. -
További szerzők:Hajdu Dorottya (1987-) (biológus) Bratschun-Khan, Doris Gáspári Zoltán Varbanov, Mihayl Philippot, Stéphanie Fizil Ádám (1988-) (biológus) Czajlik András (1975-) (gyógyszerész) Kele Zoltán Sonderegger, Christoph Galgóczy László (1950-) Bodor Andrea Marx, Florentine Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:ANN 110821
OTKA
GINOP-2.3.2-15-2016-00008
GINOP
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3.

001-es BibID:BIBFORM109184
035-os BibID:(Scopus)85149121543 (WoS)000939526000001
Első szerző:Váradi Györgyi
Cím:Confirmation of the Disulfide Connectivity and Strategies for Chemical Synthesis of the Four-Disulfide-Bond-Stabilized Aspergillus giganteus Antifungal Protein, AFP / Györgyi Váradi, Gyula Batta, László Galgóczy, Dorottya Hajdu, Ádám Fizil, András Czajlik, Máté Virágh, Zoltán Kele, Vera Meyer, Sascha Jung, Florentine Marx, Gábor K. Tóth
Dátum:2023
ISSN:0163-3864 1520-6025
Megjegyzések:Emerging fungal infections require new, more efficient antifungal agents and therapies. AFP, a protein from Aspergillus giganteus with four disulfide bonds, is a promising candidate because it selectively inhibits the growth of filamentous fungi. In this work, the reduced form of AFP was prepared using native chemical ligation. The native protein was synthesized via oxidative folding with uniform protection for cysteine thiols. AFP's biological activity depends heavily on the pattern of natural disulfide bonds. Enzymatic digestion and MS analysis provide proof for interlocking disulfide topology (abcdabcd) that was previously assumed. With this knowledge, a semi-orthogonal thiol protection method was designed. By following this strategy, out of a possible 105, only 6 disulfide isomers formed and 1 of them proved to be identical with the native protein. This approach allows the synthesis of analogs for examining structure-activity relationships and, thus, preparing AFP variants with higher antifungal activity.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of Natural Products. - 86 : 4 (2023), p. 782-790. -
További szerzők:Batta Gyula (1953-) (molekula-szerkezet kutató) Galgóczy László (1950-) Hajdu Dorottya (1987-) (biológus) Fizil Ádám (1988-) (biológus) Czajlik András (1975-) (gyógyszerész) Virágh Máté Kele Zoltán Meyer, Vera Jung, Sascha Marx, Florentine Tóth Gábor K.
Pályázati támogatás:NKFIH TKP2021-EGA-32
Egyéb
NKFIH FK 134343
Egyéb
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4.

001-es BibID:BIBFORM056390
Első szerző:Váradi Györgyi
Cím:Synthesis of PAF, an Antifungal Protein from P. chrysogenum, by Native Chemical Ligation : Native Disulfide Pattern and Fold Obtained upon Oxidative Refolding / Györgyi Váradi, Gábor K. Tóth, Zoltán Kele, László Galgóczy, Ádám Fizil, Gyula Batta
Dátum:2013
ISSN:0947-6539
Megjegyzések:The folding of disulfide proteins is of considerable interest because knowledge of this may influence our present understanding of protein folding. However, sometimes even the disulfide pattern cannot be unequivocally determined by the available experimental techniques. For example, the structures of a few small antifungal proteins (PAF, AFP) have been disclosed recently using NMR spectroscopy but with some ambiguity in the actual disulfide pattern. For this reason, we carried out the chemical synthesis of PAF. Probing different approaches, the oxidative folding of the synthetic linear PAF yielded a folded protein that has identical structure and antifungal activity as the native PAF. In contrast, unfolded linear PAF was inactive, a result that may have implications concerning its redox state in the mode of action.
Tárgyszavak:Természettudományok Kémiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
antifungal agents
NMR spectroscopy
peptides
protein folding
solid-phase synthesis
Molekulatudomány
Megjelenés:Chemistry-A European Journal 19 : 38 (2013), p. 12684-12692. -
További szerzők:Tóth Gábor K. Kele Zoltán Galgóczy László (1950-) Fizil Ádám (1988-) (biológus) Batta Gyula (1953-) (molekula-szerkezet kutató)
Pályázati támogatás:TÁMOP-4.2.1/B-09/1/KONV-2010-0005
TÁMOP
TÁMOP-4.2.1/B-09/1/KONV-2010-0007
TÁMOP
Szerkezeti biológia és molekuláris felismerés
TÁMOP-4.2.2.A-11/1/KONV-2012-0035
TÁMOP
CK 77515, K 105459, PD83355
OTKA
OMAA 83öu7 - Austrian-Hungarian Action
Egyéb
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5.

001-es BibID:BIBFORM049587
Első szerző:Virágh Máté
Cím:Production of a defensin-like antifungal protein NFAP from Neosartorya fischeri in Pichia pastoris and its antifungal activity against filamentous fungal isolates from human infections / Máté Virágh, Dóra Vörös, Zoltán Kele, Laura Kovács, Ádám Fizil, Gergely Lakatos, Gergely Maróti, Gyula Batta, Csaba Vágvölgyi, László Galgóczy
Dátum:2014
ISSN:1046-5928
Megjegyzések:Neosartorya fischeri NRRL 181 isolate secretes a defensin-like antifungal protein (NFAP) which has a remarkable antifungal effect against ascomycetous filamentous fungi. This protein is a promising antifungal agent of biotechnological value; however in spite of the available knowledge of the nature of its 50-upstream transcriptional regulation elements, the bulk production of NFAP has not been resolved yet. In this study we carried out its heterologous expression in the yeast Pichia pastoris and investigated the growth inhibition effect exerted by the heterologous NFAP (hNFAP) on filamentous fungal isolates from human infections compared with what was caused by the native NFAP. P. pastoris KM71H transformant strain harboring the pPICZalphaA plasmid with the mature NFAP encoding gene produced the protein. The final yield of the hNFAP was sixfold compared to the NFAP produced by N. fischeri NRRL 181. Based on the signal dispersion of the amide region, it was proven that the hNFAP exists in folded state. The purified hNFAP effectively inhibited the growth of fungal isolates belonging to the Aspergillus and to the Fusarium genus, but all investigated zygomycetous strain proved to be insusceptible. There was no significant difference between the growth inhibition effect exerted by the native and the heterologous NFAP. These data indicated that P. pastoris KM71H can produce the NFAP in an antifungally active folded state. Our results provide a base for further research, e.g., investigation the connection between the protein structure and the antifungal activity using site directed mutagenesis.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
Neosartorya fischeri antifungal protein
Pichia pastoris
Antimicrobial susceptibility
Clinical fungal isolates
Ascomycetes
Zygomycetes
Megjelenés:Protein Expression and Purification 94 (2014), p. 79-84. -
További szerzők:Vörös Dóra Kele Zoltán Kovács Laura Fizil Ádám (1988-) (biológus) Lakatos Gergely Maróti Gergely Batta Gyula (1953-) (molekula-szerkezet kutató) Vágvölgyi Csaba Galgóczy László (1950-)
Pályázati támogatás:TÁMOP-4.2.4.A/2-11-1-2012-0001
TÁMOP
PD 83355
OTKA
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DOI
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