Date of Award:
8-2019
Document Type:
Thesis
Degree Name:
Master of Science (MS)
Department:
Chemistry and Biochemistry
Department name when degree awarded
Biochemistry
Committee Chair(s)
Nicholas E. Dickenson
Committee
Nicholas E. Dickenson
Committee
Lisa M. Berreau
Committee
Joan M. Hevel
Abstract
Several bacterial pathogens including Shigella (shigellosis), Escherichia coli (urinary tract infections), Pseudomonas (lung infections), Salmonella (food poisoning), and Yersinia (plague) critically rely on a complex type three secretion system (T3SS) for infection. With the rise in multi-antibiotic resistant strains of several of these pathogens, we turn to the T3SS as a promising target for the development of novel therapeutics. The Dickenson lab at Utah State University has been the first to identify and characterize the ATPase Spa47, the energy source of the Shigella infection system. We show that Spa47 is necessary for proper T3SS formation and function, being ultimately responsible for overall Shigella virulence. We find that proper ATPase function and in turn T3SS apparatus formation can be affected by something as simple as a single mutation to the removal of a non-catalytic domain. The insights gained from this work expands our understanding of the powerhouse that fuels these infection systems and brings us a step closer to developing novel therapeutics to combat infection.
Checksum
0b82c1831720a329ec027fbdc48bb1cd
Recommended Citation
Burgess, Jamie L., "Biophysical and Structural Characterization of Shigella ATPase Spa47 Oligomerization Provides Insight into Type Three Secretion System Activation and Virulence" (2019). All Graduate Theses and Dissertations, Spring 1920 to Summer 2023. 7605.
https://digitalcommons.usu.edu/etd/7605
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