During the Trypanosoma cruzi adhesion to the host extracellular matrix, protein phosphorylation/dephosphorylation of cytoskeletal protein is critical for the adhesion response. In addition to the constituents of the cytoskeleton proteins reported (tubulin and paraflagellar rod proteins), heat shock proteins and ERK 1/2 protein (modified in response to elements of the extracellular matrix: laminin and fibronectin), both located in flagellum, have also been modified by phosphorylation as a result of ECM adhesion. In different organisms, heat shock proteins (HSPs) may contribute to its infectivity and to cell differentiation. HSPs may have a constitutive or induced expression by environmental factors not only the temperature. Preliminary results from our laboratory also showed variation in phosphorylation levels of HSP85 during the parasite adhesion to host ECM, with flagellar localization and with a possible role in the adhesion and invasion to the host cell. Thus, we propose in this project develop monoclonal antibodies against protein HSP85 of Trypanosoma cruzi, evaluate its participation in adhesion and invasion events and identify the proteins anchored to HSP85 located in the flagellum.
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