Trichomoniasis affects 170 million people worldwide, and 7.4 million in the USA. There is increasing focus on the role of cysteine proteases in Trichomonas vaginalis because of their role in virulence of other parasitic protozoa. Determining their location and function will provide insight about their role in the pathogenicity of T. vaginalis and their feasibility as a drug target. This study begins to characterize the first sequenced cysteine protease (CP1). E. coli and P. pastoris expression systems were developed to produce CP1 to generate antiserum, and to have enough active protein for biochemical characterization. Secondly, endogenous and epitope tagged CP1 were localized in T. vaginalis vesicles. These vesicles were confirmed to have alkaline phosphatase activity which is a characteristic of lysosomes. Lastly, deletion mutants of CP1 were created to determine the role of the prodomain in targeting CP1 to vesicles.
| Identifer | oai:union.ndltd.org:pacific.edu/oai:scholarlycommons.pacific.edu:uop_etds-1668 |
| Date | 01 January 2007 |
| Creators | Acquistapace, Bethany R. |
| Publisher | Scholarly Commons |
| Source Sets | University of the Pacific |
| Detected Language | English |
| Type | text |
| Format | application/pdf |
| Source | University of the Pacific Theses and Dissertations |
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