Thesis supervisor: László Norbert Galgóczi
Location of studies (in Hungarian): University of Szeged, Faculty of Science and Informatics, Department of Microbiology Abbreviation of location of studies: SzTE
Description of the research topic:
Presumably as a consequence of climate change the occurrence of resistant phyto-, pre- and postharvest pathogenic fungi and the number of mycotoxin contaminated feeds and foods are continuously increasing in Europe in the last years causing loss of billions of euros per year and posing severe risks to human and animal health. These facts urge the development of new, and more effective antifungal strategies. The highly stable, extracellular, cysteine-rich antifungal proteins from filamentous Ascomycetes (crAFPs) could offer an alternative, safely applicable solution. Our in silico investigations revealed that all isolated crAFPs contain an evolutionary conserved [GXC]-[X3-9]-[C] consensus γ-core motif. Our preliminary results demonstrated that the antifungal efficacy of crAFPs depends on the physical and chemical properties of the γ-core constituting amino acids. Based on this we hypothesize that the antifungal efficacy of crAFPs is improvable with rational design of the γ-core motif, and the improved crAFPs are applicable as biopesticides and crop preservatives in the agriculture and food industry. We will address this question by investigating different crAFPs produced by Neosartorya fischeri, their γ-core improved variants, and their γ-core peptides by antifungal susceptibility, haemolytic activity, cytotoxicity tests, plant and crop model experiments. The achievements in this project will allow further steps towards the biotechnological application of crAFPs, and open up a completely new avenue for the development of bioactive proteins and peptides with worldwide economic and societal impact on pest control and crop preservation.
Required language skills: English Recommended language skills (in Hungarian): German Further requirements: Basic knowledge in microbiological and protein works and methods.