Further characterization of Trypanosoma cruzi GP57/51 as the major antigen expressed by differentiating epimastigotes.

Study of Trypanosoma cruzi metacyclogenesis under chemically defined conditions showed that the expression of a group of acidic polypeptides with a molecular weight of 45-50 kDa is markedly increased on adhesion of epimastigotes to the culture vessels. Immunochemical analysis revealed that these developmentally regulated polypeptides are structurally related to, and possibly homologous with, a major T. cruzi antigen, namely, GP57/51, a glycoprotein that has recently been characterized as a cysteine proteinase. The differentiation of epimastigotes into metacyclic trypomastigotes is accompanied by a 2- to 5-fold reduction in the concentration of GP57/51 antigen as determined by radioimmunoassays using monoclonal antibodies. Two-dimensional polyacrylamide gel electrophoretic analysis of metabolically labelled parasites indicated that this antigen is synthesized as a precursor with a molecular weight of 60 kDa, which is then processed to a level of 45-50 kDa via the formation of at least one intermediate processing product. The observation that expression of GP57/51-related products increases during epimastigote differentiation suggests an important role for this proteinase during the life cycle of T. cruzi.