Characterization of the Mutant ProP Protein in Salmonella enterica serovar Typhimurium
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)