Protein S-acylation in Trichomonas vaginalis

NIEVAS Y. R; CORVI M.M; DE MIGUEL N

CORDOBA

Congreso; Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular; 2016

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB)

The flagellatedprotozoan parasite Trichomonas vaginalisis the etiologic agent of trichomoniasis, the most common non-viral sexuallytransmitted infection worldwide. Since T.vaginalis is an obligate extracellular pathogen, adherence to epithelialcells is critical for parasite survival within the human host. A betterunderstanding of this process is a prerequisite for the development oftherapies to combat infection. In this sense, recent work has shown S-acylationas a key modification that regulates invasion and motility in differentprotozoan parasites, such as Plasmodiumspp, Trypanosoma ssp, Giardia ssp and T. gondii. However, up to date there are no reports indicating whetherthis post-translational modification is a mechanism operating in T. vaginalis. In order to study theextent and function of S-acylation in T.vaginalis biology, we undertook a proteomic study to profile the full scopeof s-acylated proteins in this parasite and here we report the identificationof 504 proteins involved in a variety of biological processes including proteintransport, attachment and signaling, among others. Importantly, treatment ofparasites with the palmitoylation inhibitor 2-bromopalmitate caused asignificant decrease in the adherence to host cells, suggesting thatpalmitoylation could be modifying proteins that are key players in adherenceand concomitant pathogenesis of Trichomonasvaginalis.