Abstract
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.
- Parasite
- Palmitoylation
- Adherence
- Cell adhesion*
- Host-Pathogen Interaction
- Infectious disease
- Microbiology
- Parasite
- Pathogens
- Post-translational modifications*
- Protein Modification*
Footnotes
Author contributions: Y.R.N., M.M.C., and N.d.M. designed research; Y.R.N., A.A.V., and J.A.W. performed research; Y.R.N., A.A.V., S.M., P.J.J., J.A.W., and N.d.M. analyzed data; Y.R.N., J.A.W., and N.d.M. wrote the paper; M.M.C., S.M., P.J.J., and N.d.M. contributed new reagents/analytic tools.
- Received May 31, 2017.
- Revision received January 3, 2018.
- Accepted February 14, 2018.
- Published under license by The American Society for Biochemistry and Molecular Biology, Inc.