Presence of ATPase on the vesicular membrane of Cysticercus cellulosae. A high resolution cytochemical study.
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Porphyrins and activities of heme biosynthetic enzymes in Taenia solium cysticerci from porcine and human hosts, were examined in order to clarify the possible step where heme synthesis is interrupted. Porphyrins in the vesicular fluid of the parasite were predominantly coproporphyrin, followed by penta-carboxylated porphyrin, which together accounted for 90% of the accumulated porphyrins. Coproporphyrin and penta-carboxylated porphyrin were both type I and III isomers. Small amounts of protoporphyrin and uroporphyrin, and trace amounts of tri-, hexa- and hepta-carboxylated porphyrins were also detected. Fluorescence and phosphorescence spectra and lifetime studies revealed that at least 75% of the porphyrins were bound to metal, probably Zn, while the rest was free. Reverse phase high performance liquid chromatography monitored at an excitation wavelength of 417 nm and at an emission wavelength of 585 nm demonstrated that approximately 90% of these porphyrins were Zn-coproporphyrin. A fluorescence excitation peak at 283 nm with an emission peak at 585 nm and 625 nm indicated that some of the porphyrins were associated with proteins in the vesicular fluid of the parasite. Low levels of delta-aminolevulinic acid dehydratase, porphobilinogen deaminase and uroporphyrinogen decarboxylase activities, and heme concentrations were found in the extract of the parasite walls and scolex, but not in the vesicular fluid. The porphyrin accumulation pattern in this parasite can best be explained by postulating a deficiency of coproporphyrinogen oxidase activity, similar to that in human patients with hereditary coproporphyria. A parasite dissected from a human host was considerably less porphyric than those from pigs, but the pattern of accumulated porphyrins was quite similar in both. In view of their porphyrin contents, T. solium cysticerci could be light sensitive.
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Fractions of Taenia solium cysticerci were isolated using preparative isoelectric focusing. A fraction isoelectric between pH 7.8 and 10.0 was found to be most effective as an antigen in an enzyme-linked immunosorbent assay (ELISA) for anti-cyst antibodies. The efficacy of this fraction and of a total homogenate of the cysticerci to detect cases of neurocysticercosis by ELISA was compared. The partially purified fraction showed a sensitivity of 80% and specificity of 99.5%. The total homogenate had a sensitivity of 75% and a specificity of 99%. Cross-reactions occurred with sera from patients with hydatid disease. In patients with other parasitic infections the specificity of the isolated fraction (3/120) was considerably better than that of the total homogenate (16/120). Cysticercosis in man is caused by infection with the larval stage of the zoonotic pork tapeworm Taenia solium. The disease is largely one of developing countries and is prevalent in Latin America, Eastern Europe, the Far East and large parts of Africa. In the Republic of South Africa the prevalence of cysticercosis has been estimated as 8.5% amongst rural blacks, and in certain high incidence areas over 20%.