Trichomonas vaginalis is the protist parasite that causes the most common, non-viral sexually transmitted infection called trichomonosis. Enolase is a moonlighting protein that apart from its canonical function as a glycolytic enzyme, serves as a plasminogen receptor on the cell surface of T. vaginalis and, in consequence, it has been stablished as a virulence factor in this parasite. In the Trichomonas vaginalis sequence database there are nine genes annotated as enolase. In this work, we analyzed these genes as well as their products. We found that seven out of nine genes might indeed perform enolase activity, whereas two genes might have been equivocally identified, or they might be pseudogenes. Furthermore, a combination of qRT-PCR and proteomic approaches was used to assess, for the first time, the expression of these genes in the highly virulent mexican isolate of T. vaginalis CNCD-147 at different iron concentrations. We could find peptides corresponding to enolases encoded by genes TVAG_464170, TVAG_043500 and TVAG_329460. Moreover, we identified two distinctive characteristics within enolases from Trichomonas vaginalis. One of them corresponds to three key substitutions within one of the loops of the active site, compared to host enolase. The other, is a unique N-terminal motif, composed of 15 to 18 residues, on all the potentially active enolases, whose function still has to be stablished. Both differential features merit further studies as potential drug and vaccine targets as well as diagnosis markers. These findings offer new possibilities to fight trichomonosis.
Keywords: Enolase; Gene expression; Glycolytic enzyme; Moonlighting protein; Trichomonas vaginalis.
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