Title

Biochemical Characterization of a Cysteine Protease from Trichomonas vaginalis

Poster Number

1

Format

Poster Presentation

Faculty Mentor Name

Lisa Wrischnik

Additional Faculty Mentor Name

Kirkwood Land

Additional Faculty Mentor Name

Conor R. Caffrey (UCSF) and James H. McKerrow (UCSF)

Abstract/Artist Statement

Trichomonas vagina/is is a protozoal parasite that infects human urogenital tracts and causes a sexually transmitted disease known as trichomoniasis. While men are usually asymptomatic, women display symptoms of vaginitis. With infection come a number of adverse complications with pregnancy and greater risk for HIV. The current form of treatment is metronidazole and only recently, tinidazole. Because there is a rise in metronidazole-resistance cases, alternative forms of chemotherapy are necessary. T. vagina/is have at least four distinct cysteine protease genes which encode enzymes that have been shown to degrade the host's extracellular matrix while evading the immune system. Thus far, there is no proven role for cysteine proteases in T. vagina/is other than for infection. Because they seem to play a large role in virulence, they make for great drug targets. The focus of my research is on the purification and characterization of cysteine protease-! (CPl). CPl is -39 kD in size and is thought be contained in lysosome-like compartments. The possible major residues in the active site are Cys-25, His-163, Asn-187. The work presented here will describe our current efforts to express, purify, and characterize the biochemical properties CPl. A better understanding of cysteine proteases may shed light on alternative chemotherapies for this important human sexually transmitted pathogen.

Location

Wendell Phillips Center, 1st floor hallways

Start Date

3-5-2008 1:00 PM

End Date

3-5-2008 3:00 PM

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May 3rd, 1:00 PM May 3rd, 3:00 PM

Biochemical Characterization of a Cysteine Protease from Trichomonas vaginalis

Wendell Phillips Center, 1st floor hallways

Trichomonas vagina/is is a protozoal parasite that infects human urogenital tracts and causes a sexually transmitted disease known as trichomoniasis. While men are usually asymptomatic, women display symptoms of vaginitis. With infection come a number of adverse complications with pregnancy and greater risk for HIV. The current form of treatment is metronidazole and only recently, tinidazole. Because there is a rise in metronidazole-resistance cases, alternative forms of chemotherapy are necessary. T. vagina/is have at least four distinct cysteine protease genes which encode enzymes that have been shown to degrade the host's extracellular matrix while evading the immune system. Thus far, there is no proven role for cysteine proteases in T. vagina/is other than for infection. Because they seem to play a large role in virulence, they make for great drug targets. The focus of my research is on the purification and characterization of cysteine protease-! (CPl). CPl is -39 kD in size and is thought be contained in lysosome-like compartments. The possible major residues in the active site are Cys-25, His-163, Asn-187. The work presented here will describe our current efforts to express, purify, and characterize the biochemical properties CPl. A better understanding of cysteine proteases may shed light on alternative chemotherapies for this important human sexually transmitted pathogen.