Glycolipid and protein profiles of normal and Trypanosoma cruzi infected heart muscle cells.

Using Triton X-114, glycolipids and proteins were extracted from heart muscle cells (HMC) infected with Trypanosoma cruzi clone Dm28c and from uninfected HMC, and analysed by SDS-PAGE and high-performance thin-layer chromatography (HPTLC). Two major differences were observed: (a) two proteins with a molecular mass of 92 kDa and 69 kDa were present in the uninfected cells but absent from the infected cells and (b) a 70-90 kDa protein band was detected only in parasitized cells. These differences would seem to constitute alterations taking place during the process of cell recognition and/or parasite interiorization. No differences were observed in the respective glycolipid compositions, of control and infected cells analysed by HPTLC. A glycolipid with the same mobility as the neutral glycolipid isolated from epimastigotes of T. cruzi was detected in the uninfected cells. This finding may lend support to the previously described hypothesis that molecular mimicry is implicated in the cardioneuropathology of Chagas' disease.