| dc.description.abstract | Endospore formation by Clostridium difficile is a vital part of the life cycle for this Gram-positive bacterium. During this process, the mothercell packages proteins into the developing endospore. However, the mechanisms by which many of these proteins are secreted into the spore cortex layer is unknown. Using an endolysin as a reporter protein to translationally fuse to potential sporulation secretion substrates would help determine if the secreted proteins is destined for the cortex layer or if it remains in the outer coat. This thesis uses a bioinformatics approach to identify potential endolysins that could be used as a reporter protein in the future. By searching primary literature and online databases, a variety of naturally-produced endolysins derived from several C. difficile strains, similar bacteria species and phages were identified. From this list, these proteins were fed into Basic Local Alignment Tool (BLAST) to determine which of these were present in multiple organisms. Next, the potential cellular location of these candidate proteins was determined using the PSORT-algorithm. While PSORT was unable to determine where many of the putative reporter proteins were located, it did give results for some that could be of use. These new, potential reporter proteins would give new insight on the process of sporulation, allowing for the study of the secretion process that occur during C. difficile spore formation. | en |
