El papel de los carbohidratos en la antigenicidad de las glicoproteínas del cisticerco de la Taenia solium.

The glycoproteins af 12-28 kD from Taenia solium rnetaoestcdes provide a high specificity and sensitivei for the serological diagnosis of the central nervous systern infection, neurocysticercosis. their widespread use as antigens for routine serlogical assays will require their production in large and reproducible amounts. Prior to deterrnining the ideal strategy to produce these antigens at a large scale, it is important to determine the contribution of the carbohydrates to the antigenicity of these molecules, given the uncertainty of reproducing saccharidic epitopes in recombinant expression systems. In thia study we examined this issue. The chemical oxidation of the carbohydrates of the 12-28 kD glycsproteins with sodium metaperiodate, reduced the antigenicity of the rnolecules to variable  extents, with the more notable changes being detected for the 18 and 28 kD antigens. This approach was complemented by purification of the 12, 16 and 18 k5 antigens, followed by the enzymatic deglycosylation af their abundant N-linked oligosaccharides. Silver-stained SDS-PAGE anatysis indicated that the three deglycosylated antigens now migrated as 7 kD products, suggesting a protein backbone with a similar size, but different sxtents of glycosylation. By Western blot, the antigenicity of these antigens was diminished. This was more notable for the 18 kD antigen,which is more heavily glycosylated than the 12 or 16 kD glycoproteins. These data suggest that the antigenicity of the glycoproteins of T: solium is due to a combination of carbohydrate and protein epitopes.