Fig. 1 Schematic model of Trypanosoma cruzi
Fig. 2 Life cycle of Trypanosoma cruzi
Trypanosoma cruzi is a species of parasitic euglenoids. Amongst the protozoa, the trypanosomes characteristically bore tissue in another organism and feed on blood (primarily) and also lymph. This behavior causes disease or the likelihood of disease that varies with the organism: Chagas disease in humans, dourine and surra in horses, and a brucellosis-like disease in cattle.
The Trypanosoma cruzi life cycle starts in an animal reservoir, usually mammals, wild or domestic, including humans. A triatomine insect serves as the vector. While taking a blood meal, it ingests T. cruzi. In the triatomine the parasite goes into the epimastigote stage, making it possible to reproduce. After reproducing through binary fission, the epimastigotes move onto the rectal cell wall, where they become infectious. Infectious T. cruzi are called metacyclic trypomastigotes. When the triatomine bug subsequently takes a blood meal from a human, it defecates. The trypomastigotes are in the feces and are capable of swimming into the host's cells using flagella, a characteristic swimming tail dominant in the Euglenoid class of protists. The trypomastigotes enter the human host through the bite wound or by crossing mucous membranes. The host cells contain macromolecules such as laminin, thrombospondin, heparin sulphate, and fibronectin that cover their surface. These macromolecules are essential for adhesion between parasite and host and for the process of host invasion by the parasite. The trypomastigotes must cross a network of proteins that line the exterior of the host cells in order to make contact and invade the host cells. The molecules and proteins on the cytoskeleton of the cell also bind to the surface of the parasite and initiate host invasion.
Comparisons of genes cloned from different T. cruzi strains and isolates showed that the sequence of the repeat units is almost identical, indicating that the repetitive domains of these antigens are highly conserved. For instance, antigens FRA, Ag1, JL7 and H49 are built up of repeats of 68 amino acids that are very conserved between strains and isolates of T. cruzi8. The high frequency with which antigens bearing repetitive domains are isolated could be explained by a high concentration of specific antibodies against repeats in sera from infected individuals and/or by the fact that such antibodies bind with high affinity. This strategy also allowed the identification of nonrepetitive T. cruzi antigens such as the ribosomal P protein JL5, the 24 kDa flagellar Ca2+-binding proteins (FCaBP, 1F8, Tc-24, Tc-28), A13, Tc40, heat-shock proteins, flagellum-associated membrane proteins (FL-160, CEA, CRP), and ubiquitin.
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