Protein Palmitoylation Plays an Important Role in Trichomonas vaginalis Adherence

Mol Cell Proteomics. 2018 Nov;17(11):2229-2241. doi: 10.1074/mcp.RA117.000018. Epub 2018 Feb 14.


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.

Keywords: Adherence; Cell adhesion; Host-Pathogen Interaction; Infectious disease; Microbiology; Palmitoylation; Parasite; Pathogens; Post-translational modifications; Protein Modification.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adhesiveness
  • Amino Acid Sequence
  • Gene Ontology
  • HeLa Cells
  • Humans
  • Lipoylation*
  • Protein Domains
  • Proteome / metabolism
  • Protozoan Proteins / chemistry
  • Protozoan Proteins / isolation & purification
  • Protozoan Proteins / metabolism*
  • Trichomonas vaginalis / metabolism*


  • Proteome
  • Protozoan Proteins