New antimicrobial potential and structural properties of PAFB: a cationic, cysteine-rich protein from Penicillium chrysogenum Q176

Huber Anna; Hajdu Dorottya Zsuzsanna; Bratschun-Khan Doris; Gáspári Zoltán; Varbanov Mihayl; Philippot Stéphanie; Fizil Ádám; Czajlik András; Kele Zoltán; Sonderegger Christoph; Galgóczi László Norbert; Bodor Andrea; Marx Florentine; Batta Gyula: New antimicrobial potential and structural properties of PAFB: a cationic, cysteine-rich protein from Penicillium chrysogenum Q176.
SCIENTIFIC REPORTS, 8. ISSN 2045-2322 (2018)

[thumbnail of Newantimicrobialpotential.pdf] Szöveg
Newantimicrobialpotential.pdf - Megjelent verzió

Download (4MB)
Mű típusa: Folyóiratcikk
Szerző azonosítók:
NévORCIDMTMT szerző azonosító
Huber Anna
Hajdu Dorottya Zsuzsanna10048215
Bratschun-Khan Doris
Gáspári Zoltán10001271
Varbanov Mihayl
Philippot Stéphanie
Fizil Ádám0000-0002-4815-574410032847
Czajlik András10017084
Kele Zoltán0000-0002-4401-030210021901
Sonderegger Christoph
Galgóczi László Norbert0000-0002-6976-891010002102
Bodor Andrea0000-0002-7422-298X10013303
Marx Florentine
Batta Gyula0000-0002-0442-182810007156
Absztrakt (kivonat): 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.
Folyóirat/kiadvány címe: SCIENTIFIC REPORTS
Évszám: 2018
Kötet: 8
ISSN: 2045-2322
Intézmény: Pázmány Péter Katolikus Egyetem
Kar: Információs Technológiai és Bionikai Kar (2013.07.-)
Nyelv: angol
Kulcsszavak: multidiszciplináris tudomány
MTMT rekordazonosító: 3324997
Dátum: 2024. Okt. 25. 09:14
Utolsó módosítás: 2024. Okt. 25. 09:14
URI: https://publikacio.ppke.hu/id/eprint/1506

Actions (login required)

Tétel nézet Tétel nézet