NFAP2, a novel cysteine-rich anti-yeast protein from Neosartorya fischeri NRRL 181: isolation and characterization

Liliána Tóth, Zoltán Kele, Attila Borics, László G. Nagy, Györgyi Váradi, Máté Virágh, Miklós Takó, Csaba Vágvölgyi, László Galgóczy

Research output: Contribution to journalArticle

22 Citations (Scopus)

Abstract

The increasing incidence of fungal infections and damages due to drug-resistant fungi urges the development of new antifungal strategies. The cysteine-rich antifungal proteins from filamentous ascomycetes provide a feasible base for protection against molds due to their potent antifungal activity on them. In contrast to this, they show no or weak activity on yeasts, hence their applicability against this group of fungi is questionable. In the present study a 5.6 kDa anti-yeast protein (NFAP2) is isolated, identified and characterized from the ferment broth of Neosartorya fischeri NRRL 181. Based on a phylogenetic analysis, NFAP2 and its putative homologs represent a new group of ascomycetous cysteine-rich antifungal proteins. NFAP2 proved to be highly effective against tested yeasts involving clinically relevant Candida species. NFAP2 did not cause metabolic inactivity and apoptosis induction, but its plasma membrane disruption ability was observed on Saccharomyces cerevisiae. The antifungal activity was maintained after high temperature treatment presumably due to the in silico predicted stable tertiary structure. The disulfide bond-stabilized, heat-resistant folded structure of NFAP2 was experimentally proved. After further investigations of antifungal mechanism, structure and toxicity, NFAP2 could be applicable as a potent antifungal agent against yeasts.

Original languageEnglish
Article number75
JournalAMB Express
Volume6
Issue number1
DOIs
Publication statusPublished - Dec 1 2016

Keywords

  • Anti-yeast activity
  • Candida spp
  • Cysteine-rich antifungal protein
  • Neosartorya fischeri
  • Protein isolation
  • Protein structure

ASJC Scopus subject areas

  • Biophysics
  • Applied Microbiology and Biotechnology

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