Streptococcus pneumoniae (pneumococcus), a gram-positive bacterium, is commensal to the human nasopharynx. It is also a common cause of respiratory tract infections and multiple invasive diseases worldwide. Pneumococci attach to the nasopharynx, lung, and vascular endothelial cells, which contributes to colonization as well as to the development of pneumonia, bacteremia, and meningitis. Choline binding proteins (CBPs) are a unique set of cell wall proteins conserved within pneumococci. CBPs bind noncovalently to the phosphocholine of the cell wall through choline binding domains. The choline binding domains of the CBPs are highly conserved; however, they are diverse in their affinities and functions due to differences in their functional domains. Several of the CBPs are predicted to play a role in adherence and colonization, though direct evidence of binding to epithelial receptors is lacking. This project focuses on the ability to express and purify some of the lesser characterized CBPs which are predicted to serve as adhesins and to identify their cognate ligand proteins on host cells with the hope of identifying novel bacterial-host interactions that contribute to colonization.
| Identifer | oai:union.ndltd.org:MSSTATE/oai:scholarsjunction.msstate.edu:td-7201 |
| Date | 10 May 2024 |
| Creators | Tvarkunas, Milisen |
| Publisher | Scholars Junction |
| Source Sets | Mississippi State University |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | Theses and Dissertations |
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