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- W132221223 abstract "Three novel potential pathogenicity factors from the opportunistic pathogen Pseudomonas aeruginosa were characterized functionally and biochemically. The P. aeruginosa mutant 41D3 carries a transposon integration in the Pa5349 gene coding for a rubredoxin reductase. This mutant shows an increased sensitivity towards reactive oxigen species. It could be demonstrated that Pa5349 is an essential component in an electron transfer chain playing a central role in the detoxification of superoxide. Furthermore, evidence for the presence of a superoxide reductase in Pseudomonas aeruginosa could be accumulated, a class of enzymes previously known only from anaerobic and microaerophilic bacteria. Another mutant carried a transposon integration in the Pa0740 gene and lost the ability to reduce the amount of the Quorum Sensing molecule acyl-homoserin lactone. The Pa0740 protein was investigated for a acyl-homoserin lactone degrading activity which could not be demonstrated. The protein Pa1572 that was identified in a third mutant is annotated as conserved hypothetical protein and contains a conserved domain with homology to the ATP-NAD-kinase family. It could be demonstrated that this protein is a NADPH-dependend oxidoreductase with an yet to be identified acceptor.New methodologies for the proteome-wide investigation of interactions were introduced. These methods were aimed to elucidate the protein interactions within the pathogen in order to understand the role of the novel pathogenicity factors in the context of the infection. To this end, proteins were displayed on the cell surface of E. coli cells via fusion to the outer membrane protein intimin and possibilities and limitations of this system for the detection of protein protein interactions were investigated. It was demonstrated that a cell surface exposition requires the passage of the passenger protein through the outer membrane in an unfolded state. In order the expose proteins with a tendency to fold in the cytoplasm or periplasm on the cell surface, a novel methodology was developed which relies on the release of the passenger protein via partial lysis of a clonal population. As a model experiment, the interaction of the P. aeruginosa protein pair PcrV/PcrG could be demonstrated, providing the groundwork for the proteome-wide screening of protein interaction in pathogenic microorganisms." @default.
- W132221223 created "2016-06-24" @default.
- W132221223 creator A5013178949 @default.
- W132221223 date "2022-02-20" @default.
- W132221223 modified "2023-09-25" @default.
- W132221223 title "Funktionelle Charakterisierung potentieller Pathogenitätsfaktoren aus Pseudomonas aeruginosa mittels biochemischer und evolutiver Methoden" @default.
- W132221223 doi "https://doi.org/10.53846/goediss-488" @default.
- W132221223 hasPublicationYear "2022" @default.
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