The aim of this thesis was to compare the protein profile of surface proteins from different strains of Listeria monocytogenes in planktonic culture and biofilm and also to determine the role of flagellum in the adhesion of L. monocytogenes to abiotic surfaces. Within master thesis we used three strains from which we remove surface proteins and then analysing those proteins with two-dimensional polyacrilamide electrophoresis. Differentially expressed proteins were then identified with mass spectrometry. After analyzing images of surface proteins profiles, we detected small differences in planktonic culture and slightly higher in biofilm in the case of strain L. monocytogenes ŽM 603. Comparison of the profile of surface proteins of biofilm cells with the profile of surface proteins of planktonic cells showed differences in each strain. Amongst identified differentially expressed proteins were also moonlight proteins (MLP). Amongst all three strains, the highest number of expressed MLP in biofilm was observed in the L. monocyotgenes ŽM 603 strain. In all three strains, the level of the pyruvate dehydrogenase enzyme was increased in the biofilm culture. Despite of the defect and absence of flagellum, both strains, L. monocytogenes ŽM 603 and ŽM 600, formed biofilms, which indirectly indicates that flagellum does not contribute to adhesion and consequently in the process of forming the biofilm.
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