PROTEIN S-ACYLATION IN Trichomonas vaginalis

NIEVAS, RY; CORVI, MM; DE MIGUEL, N

Cordoba

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

Sociedad Argentina de Investigación en Bioquímica y Biología Molecular

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. A better understanding of this processis a prerequisite for the development of therapies to combat infection. In thissense, recent work has shown S-acylation as a key modification that regulatesinvasion and motility in different protozoan parasites, such as Plasmodium spp, Trypanosoma ssp, Giardia sspand T. gondii. However, up todate there are no reports indicating whether this post-translationalmodification is a mechanism operating in T.vaginalis. In order to study the extent and function of S-acylation in T. vaginalis biology, we undertook aproteomic study to profile the full scope of s-acylated proteins in thisparasite and here we report the identification of 504 proteins involved in avariety of biological processes including protein transport, attachment andsignaling, among others. Importantly, treatment of parasites with thepalmitoylation inhibitor 2-bromopalmitate caused a significant decrease in theadherence to host cells, suggesting that palmitoylation could be modifyingproteins that are key players in adherence and concomitant pathogenesis of Trichomonas vaginalis.