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Please use this identifier to cite or link to this item: http://hdl.handle.net/11375/14165
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dc.contributor.advisorBurrows, Lorien_US
dc.contributor.authorShimkoff, Anthony E.en_US
dc.date.accessioned2014-06-18T17:06:33Z-
dc.date.available2014-06-18T17:06:33Z-
dc.date.created2014-05-14en_US
dc.date.issued2011-08en_US
dc.identifier.otheropendissertations/8993en_US
dc.identifier.other10081en_US
dc.identifier.other5580535en_US
dc.identifier.urihttp://hdl.handle.net/11375/14165-
dc.description.abstract<p>lmmunocompromised, burned, and cystic fibrosis patients are highly susceptible to severe and chronic <em>Pseudomonas</em> infections. Extracellular virulence factors, such as type IV pili (T4P), contribute to the establishment and maintenance of infection in these hosts. T4P are hairlike appendages involved in attachment to and colonization of biotic and abiotic surfaces, DNA uptake, biofilm formation, virulence and twitching motility. In<em> Pseudomonas aeruginosa</em>, the pilus fibre-primarily composed of PilA-is directed by the inner membrane subcomplex PilM/N/O/P to PilQ, the secretin pore. FimV is an inner membrane protein that contains a periplasmic region that binds peptidoglycan and a cytoplasmic region containing tetratricopeptide repeat (TPR) protein-protein interaction domains. FimV is essential for twitching motility in <em>P. aeruginosa</em>, but its exact function is not well understood. Here we investigate the role of the cytoplasmic region of FimV in the T4P system. Co-purification studies revealed that PilM and PilG, a protein proposed to be involved in T4P chemotaxis, interact with the cytoplasmic region of FimV. Fluoresence microscopy was used to test the role of FimV in the localization of a functional PilG-YFP fusion. In the wild type, PilG is polarly localized, while in a <em>fimV</em> mutant, PilG becomes diffuse. The interactions between FimV with PilG and PilM may play a pivotal role in twitching motility as <em>fimV</em> mutants lacking the cytoplasmic region are incapable of twitching. In this study, we have shown that FimV is interacting with components of the T4P chemotaxis system, which may be important for cAMP regulation.</p>en_US
dc.subjectextracellular virulence factorsen_US
dc.subjecttype IV pilien_US
dc.subjectinfectionen_US
dc.subjectfluoresence microscopyen_US
dc.subjectBiochemistryen_US
dc.subjectBiochemistry, Biophysics, and Structural Biologyen_US
dc.subjectLife Sciencesen_US
dc.subjectMedical Biochemistryen_US
dc.subjectMedical Sciencesen_US
dc.subjectBiochemistryen_US
dc.titleFimV is Involved in the Function and Regulation of the Type IV Pllus System in Pseudomonas aeruginosaen_US
dc.typethesisen_US
dc.contributor.departmentBiochemistry and Biomedical Sciencesen_US
dc.description.degreeMaster of Science (MSc)en_US
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