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Analysis of a trichomonas vaginalis cysteine protease

Author

Bethany R. Acquistapace, University of the Pacific

Date of Award

2007

Document Type

Thesis - Pacific Access Restricted

Degree Name

Master of Science (M.S.)

Department

Biological Sciences

First Advisor

Kirkwood Land

First Committee Member

Gregg Jongeward

Second Committee Member

Craig Vierra

Third Committee Member

Lisa A. Wrischnik

Abstract

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.

Pages

91

Recommended Citation

Acquistapace, Bethany R.. (2007). Analysis of a trichomonas vaginalis cysteine protease. University of the Pacific, Thesis - Pacific Access Restricted. https://scholarlycommons.pacific.edu/uop_etds/669