ABSTRACT
Trypanosoma cruzi, the etiologic agent of Chagas' disease, is represented by a set of parasites which circulate between man, vectors, domestic and wild animals. Recently, our group isolated from Triatoma vitticeps strains of T. cruzi that were characterized as belonging to the Z3 phylogenetic lineage. Since very little is known about the biological and/or biochemical markers of sylvatic Z3 isolates, we have studied the protein and protease profiles of distinct Z3 isolates designated as SMM10, SMM53, SMM88, and SMM98. By means of sodium dodecyl sulfate-polyacrylamide gel electrophoresis, both quantitative and qualitative differences were observed in the protein profiles of these strains. All strains produced an acidic cysteine protease of 45 kDa, resembling cruzipain activity. The strain SMM10 synthesized an additional 55 kDa metalloprotease. Using Western blotting and anti-cruzipain antibody to detect cruzipain-like molecules, a 40-kDa reactive molecule was identified in all strains; in the strain SMM10, an 80-kDa protein was also reacted. Studies about cruzipain isoforms from sylvatic parasites could be valuable tools in the comprehension of the genetic variability in the pathogenesis of Chagas' disease.
