Molecular characterization of the surface and cyst fluid components of Taenia crassiceps

Abstract

Information relating to the characterization of cestode surface macromolecules is limited. This is especially the case with Taenia crassiceps, a well-recognized model for the study of larval cestodiasis. Here, the protein and glycoprotein composition of the tegumental surface and cyst fluid of the metacestode have been investigated using radio-isotope labelling, immunoprecipitation, SDS-PAGE and lectin affinity chromatography. A restricted number of surface proteins was labelled with the 125I/Iodogen method although the majority were immunogenic; in contrast an array of cyst fluid antigens were labelled. Host serum proteins, including immunoglobulins, were identified on the surface and in the cyst fluid. Some of the 125I-labelled surface proteins, including a 37 kDa molecule, have been shown to be glycoproteins and probably contain-D-mannose and/or D-glucose; there is limited or no N-acetylglucosamine and no terminal galactose present on these components. A 37 kDa surface molecule, possibly the same glycoprotein, was also precipitated by infection sera and this may endorse the theory that highly immunogenic carbohydrates are continuously shed by T. crassiceps as a mechanism for diverting the immune response of the host. Radio-iodinated and biosynthetically labelled T. crassiceps antigens were highly cross-reactive with antibody raised to other cestodes and not one antigen was identified as a possible candidate for use in specific immunodiagnosis of any of the important taeniid infections.

Characterization of GP39-42 and GP24 antigens from Taenia solium cysticerci and of their antigenic GP10 subunit

“…Finally, it is known that one of the main functions of carbohydrates associated with proteins is protection of the polypeptide chain (Allen and Kisailus 1992;Montreuil 1993;Varki 1993). This would be especially important in host-parasite relationships, as has been suggested for Schistosoma mansoni (Schmidt 1995), T. crassiceps (Lamsam and McManus 1990), and T. taeniaeformis (Hammerberg et al 1980), and in this paper, preliminary data for T. solium are presented.…”

Biochemical Characterization and Differential Expression of a 16.5-Kilodalton Tegument-Associated Antigen from the Liver Fluke Fasciola hepatica

“…On the other hand, numerous tegumental proteins lacking the DM9 motif have been identified and purified from F. gigantica (5)(6)(7)64), S. japonicum (69,70), S. mansoni (31,39,55), C. sinensis (18,74), Echinococcus granulosus (56), and Taenia spp. (40,42,54), and none of these proteins shares homology with FhTP16.5. Proteins of 50 kDa and 25 to 40 kDa have also been identified in the tegumental syncytium of various F. hepatica stages using monoclonal antibodies (2,34), but these proteins have not yet been purified and characterized.…”

Developmental changes of Echinococcus multilocularis metacestodes revealed by tegumental ultrastructure and lectin-binding sites

“…Aspecific reactions may reveal that these glycoconjugates are glycoproteins reacting, as endogenous lectins, with sugar moities of FITC-lectins. Lamsam & McManus (1990) suggested that T. crassiceps metacestode releases glycoproteins from its surface. Highly immunogenic carbohydrates of these glycoproteins may serve to divert the host immune response, for example by fixing complement.…”