Vesicle-Associated Membrane Proteins in Trichomonas vaginalis
Poster Number
5
Format
Poster Presentation
Faculty Mentor Name
Lisa Wrischnik
Additional Faculty Mentor Name
Kirkwood Land
Abstract/Artist Statement
Trichomonas vaginalis is an anaerobic, flagellated parasitic protozoan. It is the cause of trichomoniasis, which is the most prevalent protozoan infection in the industrial world. The mechanisms of Trichomonas' pathogenenicity are still not completely understood, but several studies have implicated cysteine proteases in this process. The protists undergo a change of morphology when bound to human cells, which includes a reorganization of vesicular membranes in the cell so· that vesicles are localized just under the surface that contacts the host cell. Cysteine protease 1 (CPl) appears to localize to vesicles in cultures of Trichomonas, and several other cysteine proteases are known to be secreted by the parasite. To better understand the protein sorting mechanisms of cysteine proteases, we have cloned and expressed a number of genes found in the Trichomonas genome that are known to produce proteins involved in vesicle membrane trafficking, exocytosis and endocytosis. We will use immunofluorescence microscopy to examine the localization of several tagged membrane compartment proteins. Similarly, we are using a fluorescent dye called Lysotracker to view acidic compartments in the cells. Acidic compartments are riormally associated with lysosome-like organelles as well as some types of secretory compartments. Co-localizing these proteins (CPl and proteins associated with exocytosis or endocytosis) through fluorescence microscopy will allow us to better understand whether the vesicles are acting to break down endocytosed materials, or fuse with the plasma membrane to exocytose internal materials, and this may help to answer how these CP !-containing vesicles may contribute to the pathogenicity mechanisms of Trichomonas:
Location
Wendell Phillips Center, 1st floor hallways
Start Date
3-5-2008 1:00 PM
End Date
3-5-2008 3:00 PM
Vesicle-Associated Membrane Proteins in Trichomonas vaginalis
Wendell Phillips Center, 1st floor hallways
Trichomonas vaginalis is an anaerobic, flagellated parasitic protozoan. It is the cause of trichomoniasis, which is the most prevalent protozoan infection in the industrial world. The mechanisms of Trichomonas' pathogenenicity are still not completely understood, but several studies have implicated cysteine proteases in this process. The protists undergo a change of morphology when bound to human cells, which includes a reorganization of vesicular membranes in the cell so· that vesicles are localized just under the surface that contacts the host cell. Cysteine protease 1 (CPl) appears to localize to vesicles in cultures of Trichomonas, and several other cysteine proteases are known to be secreted by the parasite. To better understand the protein sorting mechanisms of cysteine proteases, we have cloned and expressed a number of genes found in the Trichomonas genome that are known to produce proteins involved in vesicle membrane trafficking, exocytosis and endocytosis. We will use immunofluorescence microscopy to examine the localization of several tagged membrane compartment proteins. Similarly, we are using a fluorescent dye called Lysotracker to view acidic compartments in the cells. Acidic compartments are riormally associated with lysosome-like organelles as well as some types of secretory compartments. Co-localizing these proteins (CPl and proteins associated with exocytosis or endocytosis) through fluorescence microscopy will allow us to better understand whether the vesicles are acting to break down endocytosed materials, or fuse with the plasma membrane to exocytose internal materials, and this may help to answer how these CP !-containing vesicles may contribute to the pathogenicity mechanisms of Trichomonas: