Characterization of the Mutant ProP Protein in Salmonella enterica serovar Typhimurium

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Florida Southern College
Mechanisms invoked by organisms to combat osmotic stress are ubiquitous. The information gained from analyzing osmotic adaptations can be broadly applied, to creating drought-resistant crops, understanding disease pathologies, and fighting bacterial infections. Salmonella enterica serovar Typhimurium (Salmonella typhimurium, hereafter) has a transport protein called ProP that undergoes post-translational modifications that allow it to uptake osmoprotectants in the face of osmotic stress. The nature of these post-translational modifications is not well understood since the protein has not been crystallized. The aim of my study was to further characterize 6 Salmonella typhimurium strains that have a mutant ProP protein that has conformational changes that mimic post-translationally modified wild-type proteins. I did so by running a sequence alignment between Salmonella typhimurium and 22 related species to gain an understanding of the importance of the regions of ProP needed for function and I modeled the mutated amino acid sequences on a related protein to gain a better understanding of how the mutations affect the confirmation of the protein. The regions where the mutations occurred in the mutants were found to play a significant role in ProP’s function based on their conservation among 22 ProP orthologs, and the majority of the mutations could significantly affect ProP’s function in a way that likely mimics the wildtype.
Honors Thesis Spring 2021
Salmonella enteritidis, Salmonella typhimurium, Disease (Pathology)