Myosin-like protein (M(r) 175,000) in Gregarina blaberae.

A myosin-like protein (M(r) 175,000) was detected in the parasitic protozoan Gregarina blaberae, by both immunofluorescence and immunoblotting of one- and two-dimensional electrophoresis gels using anti-myosin antibodies. This protein was present in the trophozoite ghost but not in the cytoplasmic extract, nor in extract from the sexual stage, suggesting a protein-stage-dependent expression. The protein tightly bound to the cortical membranes was insoluble at low ionic strength, or in detergent solutions, but could be extracted from Gregarina ghosts by 6 M urea in high ionic strength solution (0.5 M NaCl) and in the presence of reducing agents (20 mM DTT). The protein was localized by indirect immunofluorescence in the cortex of the epimerite, in the fibrillar disc (the so-called septum) separating the proto- and the deutomerite segments, in the contractile ring or sphincter at the top of the protomerite, and as longitudinal lines underlying the G. blaberae epicyte folds. The presence of both actin-like and myosin-like proteins would be consistent with a role in gliding and other cell motility processes of this parasite.