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Mol Cell Proteomics. 2018 Feb 14. pii: mcp.RA117.000018. doi: 10.1074/mcp.RA117.000018. [Epub ahead of print]

Protein palmitoylation plays an important role in Trichomonas vaginalis adherence.

Author information

1
IIB-INTECH, CONICET-UNSAM, Argentina.
2
Genomics Institute of the Novartis Research Foundation, United States of America.
3
UCLA.
4
University of California, Los Angeles, United States of America.
5
Laboratorio de ParĂ¡sitos Anaerobios, IIB-INTECH, CONICET-UNSAM, Argentina ndemiguel@intech.gov.ar.

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.

KEYWORDS:

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

PMID:
29444981
DOI:
10.1074/mcp.RA117.000018
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