ABSTRACT
Tc-85 is an 85-kDa surface glycoprotein specific for the trypomastigote stage of Tripanosoma cruzi which has been implicated in the invasion of host cells by the parasite. Tc-85 has a half-life of 3.5-4 h and is synthesized as a 95-kDa precursor. Processing of the 95-kDa precursor is inhibited by N-p-tosyl-L-lysine chloromethyl ketone, p-chloromercuriphenylsulfonic acid, iodoacetamide or N-ethylmaleimide, but not by aprotinin, antipain or phenylmethylsulfonil fluoride. Tc-85, but not the precursor, is rapidly shed into the medium, allowing a correlation between the decrease of Tc-85 in trypomastigotes and its increase in the culture medium. The shedding of Tc-85 was inhibited 50 per cent by 1 muM tunicamycin, but not by 10 muM swainsonine or 10 muM 1-deoxynojirimycin under the experimental conditions employed. This suggests that N-linked oligosaccharides are important for the shedding phenomenon, although it appears that they do not have to be fully processed for shedding to occur.