Project description:Trichomonas vaginalis, a common sexually transmitted parasite that colonizes the human urogenital tract, secretes extracellular vesicles (TvEVs) that are taken up by human cells and are speculated to be taken up by parasites as well. While the crosstalk between TvEVs and human cells has led to insight into host:parasite interactions, the role of TvEVs in infection have largely been one-sided, with little known about the effect of TvEV uptake by T. vaginalis. Approximately 11% of infections are found to be co-infections of multiple T. vaginalis strains. Clinical isolates often differ in their adherence to and cytolysis of host cells, underscoring the importance of understanding the effects of TvEV uptake within the parasite population. To address this question our lab observed the effects of EV uptake by T. vaginalis on parasite gene expression. Using RNA-seq, we showed that TvEVs upregulate expression of predicted parasite membrane proteins and identified a novel adherence factor, heteropolysaccharide binding protein (HPB2).
Project description:The sexually transmitted parasite Trichomonas vaginalis secretes extracellular vesicles (TvEVs) that are internalized by human host cells. The goal of this experiment was to identify the effects of TvEV uptake on host cell gene expression.
Project description:The sexually transmitted parasite Trichomonas vaginalis is often found in symbiosis with the obligate intracellular pathogen Mycoplasma hominis. M. hominis is itself an opportunistic pathogen of the female reproductive tract associated with bacterial vaginosis. The goal of this experiment was to identify the effects of each pathogen individually and in symbiosis on host cell gene expression.
Project description:Trichomonas vaginalis is a sexually transmitted infection that causes vaginitis and increases the risk of HIV transmission. We are interested in the secreted and membrane glycoproteins of Trichomonas because they are likely involved in pathogenesis and may include novel vaccine targets. Four mass spectrometric methods (identification of all parasite proteins, glycoprotein enrichment with the plant lectin Concanavalin A, peptide:N-glycanase treatment to identify occupied N-glycans sites, and analysis of N-terminal peptides) were used to identify >300 Trichomonas secreted and membrane proteins. The first group of these proteins, which were present in multiple genome copies and had homologs in diverse eukaryotes, included 1) those involved in the N-glycan-dependent quality control protein folding in the ER lumen, 2) metalloproteases, serine proteases, cysteine proteases, and other lysosomal enzymes, and 3) transporters and membrane-associated cyclases. The second group of secreted and membrane proteins were, for the most part, encoded by single copy genes, unique to Trichomonas, and missing N-terminal signal peptides. The latter observation is despite evidence that the signal peptide peptidase functions normally in Trichomonas. As the unique secreted and membrane proteins of Trichomonas were often large and lacked features that make it easy to choose vaccine candidates, alternative strategies for vaccination and/or therapy are discussed.
