Fine and Performing Arts Honors
Date of Award
Thesis Professor Department
Cyclic-di-GMP, a common bacterial second messenger, has been thought to help develop virulence and biofilms in bacteria, most specifically in Salmonella Typhimurium. By being able to dysregulate cyclic-di-GMP production, virulence may be better combatted. STM1987, an L-arginine-responsive diguanylate cyclase with a periplasmic sensory domain, dimerizes and generates the bacterial second messenger cyclic-di-GMP in response to the amino acid L-arginine in a pathway that also requires the periplasmic L-arginine-binding protein ArtI. Their biochemical responses to L-arginine and when they dimerize could help clarify this pathway, so I sought to develop a periplasmic dimerization sensor to better monitor these biochemical interactions. Similar to STM1987, the ToxR transcriptional regulator from Vibrio cholera is also activated by dimerization. By switching out the periplasmic domain of ToxR for the periplasmic regions of interest, I can better evaluate the cyclic-di-GMP response to L-arginine. This research aims to find the specific responses in this pathway to be able to use this in combatting bacterial virulence. I was able to successfully show that the STM1987 periplasmic domain dimerizes in response to L-arginine, providing an important insight into this signaling pathway.
East Tennessee State University
Honors Thesis - Open Access
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This work is licensed under a Creative Commons Attribution-Noncommercial-No Derivative Works 3.0 License.
Mohseni, Deeba, "The Role of STM1987 and ArtI in Arginine Response of Salmonella Typhimurium" (2022). Undergraduate Honors Theses. Paper 667. https://dc.etsu.edu/honors/667
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