Protozoal infection is a serious factor in the decline of reproductive health in humans and animals. The example of T. vaginalis shows how the parasite-host interaction is mediated. It is known that signaling between cells and parasites is carried out with the help of specific connections. These bonds can be represented by glycans and lectins. In this work, we examined the glycan profile of cells and lectin profile of exosomal vesicles of the intestinal trichomonad Tritrichomonas sp. in an intestinal epithelial model. The cytotoxicity of active trophozoites on cells of the CaCo-2 tumor cell line was shown, and the absence of cytotoxic effect of exosomal vesicles on cells was also demonstrated. We investigated the glycan profile of CaCo-2 cells by treatment with biotinylated lectins and found a high percentage of binding to the lectins RCA120, AAL, and UEA-1. These lectins bind galactose and fucose-containing glycans. When we determined the lectin profile of vesicles on glycan chips, we found vesicles bound to alpha-Gal beta-Gal and GalNAc, as well as Fuca1. We hypothesize that exosomal vesicles interact with the host cell through these glycan-lectin chains. By selecting blockers of these interactions, parasite adhesion can be inhibited. These mechanisms may form the basis of new antiprotozoal drugs.