Protein palmitoylation plays an important role in Trichomonas vaginalis adherence.
Nievas, Y. R., Vashisht, A. A., Corvi, M. M., Metz, S., Johnson, P. J., Wohlschlegel, J. A. and de Miguel, N.
Genomics Institute of the Novartis Research Foundation, United States of America.
University of California, Los Angeles, United States of America.
Laboratorio de Parasitos Anaerobios, IIB-INTECH, CONICET-UNSAM, Argentina
The flagellated protozoan parasite Trichomonas vaginalis is the etiologic agent of trichomoniasis, the most common non-viral sexually transmitted infection worldwide. As an obligate extracellular pathogen, adherence to epithelial cells is critical for parasite survival within the human host and a better understanding of this process is a prerequisite for the development of therapies to combat infection. In this sense, recent work has shown S-acylation as a key modification that regulates pathogenesis in different protozoan parasites. However, there are no reports indicating whether this post-translational modification is 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 this parasite and reported the identification of 363 proteins involved in a variety of biological processes such as protein transport, pathogenesis related and signaling, among others. Importantly, treatment of parasites with the palmitoylation inhibitor 2-bromopalmitate causes a significant decrease in parasite: parasite aggregation as well as adherence to host cells suggesting that palmitoylation could be modifying proteins that are key regulators of Trichomonas vaginalis pathogenesis.
Molecular and Cellular Proteomics : en prensa (2018)