Taenia crassiceps surface immunoglobulins: parasite- or host-derived?

In common with other taeniid cestodes, host or host-like proteins, especially immunoglobulins, occur on the surface and in the cyst fluid of Taenia crassiceps metacestodes. Here, several approaches have been used to determine the origin of the immunoglobulins present on the tegument. Indirect IFAT showed that IgG was almost totally lost from the surface of bladders after 6 days culture in vitro. There was a rapid reacquisition of immunoglobulins following incubation of the cultured metacestodes with either normal mouse serum or mouse anti-T. crassiceps antiserum. Immunoprecipitation of in vitro translation products and biosynthetically labelled T. crassiceps proteins with a panel of anti-IgG antisera failed to positively identify any molecule with homology to mammalian immunoglobulins. These results suggest strongly that the immunoglobulins located on the surface of T. crassiceps are of host rather than parasite origin. The occurrence of a relatively low abundance receptor in the surface of the bladders, which binds non-specific host immunoglobulin, together with surface-bound specific anti-T. crassiceps antibodies can account for the presence of these host proteins. Freshly obtained bladders and metacestodes cultured in vitro for 6 days were transplanted into naive mice and the survival and development of the resulting parasites compared. In some individual mice there was a decrease in the number and volume of metacestodes and an increase in encapsulated parasites arising from cultured bladders. This was probably not related to the loss of host immunoglobulins from the parasite surface during culture as the reacquisition of these proteins after transplantation is likely to be far more rapid than any immune response could evoke in a naive host.

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

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.