Some aspects of the presence of surface--associated acid mucosubstances on larval Taenia saginata infecting suitable and unsuitable hosts.

The coat of acid mucosubstances occurring on the bladder surface was studied in Cysticercus bovis (larvae of Taenia saginata) developing in specific (cattle) and nonspecific (some other ruminants) intermediate hosts. In cysticerci developing in nonspecific intermediate hosts, this coat is absent or poorly developed even at the time when it is completely formed on the bladder surface of C. bovis from cattle. If the cysticercus develops up to the infective stage in a nonspecific intermediate host, it is usually localized outside the muscles: in the brain, lungs or liver. Its bladder is then also covered by a coat of acid mucosubstances. The absence or insufficient development of the protective coat on larvae in nonspecific intermediate hosts is explained by their early and strong tissue reaction.

[Free amino acid components of cystic fluid of Cysticercus cellulosae].

The free amino acids in the cystic fluid of Cysticercus cellulosae were determined quantitatively by using automatic amino acid analyzer. The cystic fluids of both subcutaneous-muscular Cysticercus cellulosae from 14 pigs and cerebral Cysticercus cellulosae from 10 pigs were detected. Among the 18 amino acids detected, alanine was found to be the predominant amino acid in both of the cystic fluids. The quantities of glycine and proline were higher than other amino acids in subcutaneous-muscular Cysticercus cellulosae, while threonine was higher than the rest in the cerebral Cysticercus cellulosae. A comparison was made between the quantities of amino acids in the fluids of both subcutaneous-muscular and cerebral Cysticercus cellulosae of 7 pigs by the T-test method. The results showed that the quantities of 12 out of 15 amino acids were significantly different, with particular reference to threonine, alanine, serine, and valine, suggesting that the difference in the metabolism of amino acids in Cysticercus may be related to the parasite's location in their respective hosts.

Biochemical characterization of Taenia hydatigena cysticerci from goats and pigs.

Analysis of the major biochemical components of Taenia hydatigena cysticerci collected from goats and pigs showed marked differences, particularly in glycogen, protein, lipid and DNA levels. Differences were also detected in the levels of cholesterol, triglycerides, free fatty acids and phospholipids. Furthermore, the profile of phospholipid fractions revealed quantitative differences between the two species. It is concluded that the cysticerci of goat and pig origin probably represent two different strains and possibly follow the same pattern of speciation as reported in the related taeniid, Echinococcus granulosus.

Porphyrin content of the cysticercus of Taenia solium.

The strong red fluorescence of the cysticercus of Taenia solium depends on the presence of several porphyrins in the vesicular fluid of the parasite: probably protoporphyrin IX, coproporphyin I or III, and 2 decarboxylated porphyrins intermediate between uroporphyrin and coproporphyrin. Cyst porphyrins associated to form conglomerates of high molecular weight that dissociated in acid solutions and were not antigenic themselves nor associated with antigenic molecules. An appreciable fraction of the porphyrins was capable of undergoing oxidation and reduction, indicating that some of the porphyrins were complexed with metal ions. The metabolic basis for the accumulation of porphyrins is unknown. Preliminary results suggest that conditions deleterious to the cysticercus cause release of porphyrins so that the appearance of porphyrins in the cerebrospinal fluid of neurocysticercotic patients may prove useful in monitoring therapeutic attacks on the parasite.

The isolation, purification, and characterization of the collagen of Cysticercus cellulosae.

Insoluble collagen fibrils were obtained from Cysticercus cellulosae after homogenization and treatment with NaCl/mercaptoethanol solutions and were solubilized after limited pepsin digestion. Solubilized Cysticercus collagen shows two different alpha subunits in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent molecular weight of 100,000 and is readily degraded by bacterial collagenase. The amino acid composition is characteristic of collagen except that it contains no hydroxyproline. Segment long spacing crystallites measuring 280 nm in length were prepared. These segments showed a band pattern different from that of vertebrate and other invertebrate collagens. The denaturation temperature at neutral pH was 35 degrees C and correlated with the total pyrrolidine content as observed for other collagens. An intrinsic viscosity value of 15.3 dl/g was obtained for this collagen. Its possible evolutionary relationship with other collagens is discussed.