Protein palmitoylation plays an important role in Trichomonas vaginalis adherence

NIEVAS, YESICA R; VASHISHT, AJAY A; CORVI, MARIA M; METZ, SEBASTIAN; JOHNSON, PATRICIA J; WOHLSCHLEGEL, JAMES A; DE MIGUEL, NATALIA

MOLECULAR & CELLULAR PROTEOMICS

AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC

Año: 2018

1535-9476

The flagellated protozoan parasite Trichomonas vaginalis is the etiologic agent of trichomoniasis,the most common non-viral sexually transmitted infection worldwide. As an obligate extracellularpathogen, adherence to epithelial cells is critical for parasite survival within the human host and a betterunderstanding of this process is a prerequisite for the development of therapies to combat infection. In thissense, recent work has shown S-acylation as a key modification that regulates pathogenesis in differentprotozoan parasites. However, there are no reports indicating whether this post-translational modificationis a mechanism operating in T. vaginalis. In order to study the extent and function of S-acylation in T.vaginalis biology, we undertook a proteomic study to profile the full scope of S-acylated proteins in thisparasite and reported the identification of 363 proteins involved in a variety of biological processes such asprotein transport, pathogenesis related and signaling, among others. Importantly, treatment of parasites withthe palmitoylation inhibitor 2-bromopalmitate causes a significant decrease in parasite: parasite aggregationas well as adherence to host cells suggesting that palmitoylation could be modifying proteins that are keyregulators of Trichomonas vaginalis pathogenesis.