RESUMO
Trichomonas vaginalis causes trichomoniasis, the most common non-viral sexually transmitted disease worldwide. As an extracellular parasite, adhesion to host cells is essential for the development of infection. During attachment, the parasite changes its tear ovoid shape to a flat ameboid form, expanding the contact surface and migrating through tissues. Here, we have identified a novel structure formed at the posterior pole of adherent parasite strains, resembling the previously described uropod, which appears to play a pivotal role as an anchor during the attachment process. Moreover, our research demonstrates that the overexpression of the tetraspanin TSP5 protein (TvTSP5), localized on the parasite's cell surface, notably enhances the formation of this posterior anchor structure in adherent strains. Finally, we demonstrate parasites that overexpress TvTSP5 possess an increased ability of the parasite to adhere to host cells, enhanced parasite aggregation and reduced migration on agar plates. Overall, these findings unveil novel proteins and structures involved in the intricate mechanisms of Trichomonas vaginalis interactions with host cells.