Analysis and preliminary purification of glycoproteins isolated from eggs in the urine of patients with Schistosoma haematobium infection

Preliminary analysis and purification of glycoproteins from Schistosoma haematobium eggs were carried out with a small quantity of antigenic material obtained from the urine of infected human patients. A soluble egg extract was ¹²⁵I-labeled and was fractionated by lectin affinity chromatography for separating egg glycoproteins. The crude glycoprotein fraction was run on SDS-PAGE to yield three polydisperse peaks with R(f) values of 0.31, 0.57, and 0.84. ¹²⁵I-labeled egg glycoproteins were further fractionated by ion exchange chromatography to yield four peaks or shoulders. One of these peaks constituted the major labeled egg glycoprotein of S. haematobium (MEG(L)-H) in a relatively pure form as determined by SDS-PAGE, and its estimated m.w. was 70,000. This glycoprotein was consistently and highly reactive serologically with a serum pool from schistosomiasis haematobia patients by a Farr-type radioimmunoassay (RIA). A limited cross-specificity study by inhibition RIA indicated that S. mansoni eggs contain components that cross-react only partially with MEG(L)-H. These results focus attention on MEG(L)-H as a potential serodiagnostic probe.