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Chagas disease, which affects 12 million people living in the Latin American region, is caused by the parasite Trypanosoma cruzi. A major consequence of infection is the occurrence of long-term symptoms of chronic cardiomyopathy. Antibodies induced by the ribosomal protein P2 β from T. cruzi (TcP2β) crossreact with a specific epitope on the human β1-adrenergic receptor of cardiomyocytes, suggesting an autoimmune mechanism for this pathology. In order to characterise the phenomenon further, we are studying an anti-TcP2 β monoclonal antibody (mAb), 17.2, and its interaction with both the cognate and cross-reactive antigens. The monoclonal antibody 17.2, which was raised against the recombinant ribosomal protein, recognises an epitope at the Cterminus of the molecule. In addition, mAb 17.2 simulates rat cardiomyocytes, and cross-reacts with a peptide carrying the β1-adrenergic receptor epitope that is implicated in the cardiomyopathy of Chagas disease. We have determined the crystal structure of Fab 17.2 as a complex with a peptide containing the ribosomal epitope. Crystallisation trials of Fab 17.2 with TcP2 β and a peptide containing the β1-adrenergic receptor epitope are in progress to complement our initial structural results.

Structural studies of antibodies implicated in Chagas disease