Isolation and Characterization of Surface Antigens from Schistosoma mansoni. II Antigenicity of Radiolabeled Proteins from Adult Worms

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Abstract
Adult S. mansoni were radiolabeled in vitro with 125I Bolton-Hunter reagent. Surface membrane antigens were solubilized with non-ionic detergent, then reacted with infection or normal serum. The antigen-antibody complexes were then precipitated with staphylococcal protein A immunoadsorbent, eluted with urea and SDS [sodium dodecyl sulfate], and fractionated by SDS-PAGE [polyacrylamide gel electrophoresis]. The presence of 6 to 8 tegument antigens was indicated depending on the type of antisera used. Human antisera to S. japonicum and S. haematobium reacted with some but not all of the antigens identified with human S. mansoni infection serum; this implies the presence of species-specific tegument antigens. The MW of the radiolabeled antigens ranged from 10,000-100,000. A large MW (> 100,000) glycoprotein and an uncharacterized lipid fraction appeared to be precipitated nonspecifically. Immunoprecipitation methods with anti-mouse Ig[immunoglobulin]G and anti-mouse whole serum failed to detect the presence of host-like antigens in the labeled extracts. Several of the labeled proteins from S. mansoni reacted with serum from patients infected with either S. haematobium or S. japonicum.

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