Perforins are proteins that have a large biotechnological potential in biopharmaceutical, analytic and agronomical fields because of their pore forming abilities. There is already a wide spectre of known perforins and protein couples that jointly form pores, but their wide spectre of potential use calls for new research. Analysis of molecular mechanisms that effect their biological function as well as their potential applications is crucial. In this thesis we decided to discover potential of entomopathogenic fungi Beauveria bassiana, its aegerolylin and protein with MACPF domain with a goal of discovering their interaction in formulation of pores. We selected two genes, for which there was a plausibility, that they are enabling fungi its entomopathogenic activity, with formation of pores into insect cuticle. During the research we successfully cloned and expressed both proteins from recombinant bacterium and successfully isolated aegerolysin in a pure form. On this protein we than preceded to conduct analytical methods, that confirmed, that we most likely gained it in its native form. Sedimentation test and SPR showed strong bonds of aegerolysin to lipid combination of ceramide phosphoethanolamine and sphingomyelin which matches predicted biological function. For exact determination of biological functions of both proteins and final discovery of their potential use as pesticide and other applications further research is needed.
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