The purification, characterization, serological activity and hepatotoxic properties of two cationic glycoproteins (α1and ω1) fromSchistosoma mansonieggs

Abstract

T cell-deprived mice acutely infected withS. mansonisuffer microvesicular hepatocyte damage which is not seen in infected, immunological intact animals. A cationic fraction (CEF6) of the PBS-soluble portion ofS. mansonieggs (SEA) induces antibodies which, on passive transfer, prevent hepatocyte damage. CEF6 contains 2 antigens, ω₁and α₁, and has also been shown to be a useful serodiagnostic reagent. This paper describes the purification and characterization of the 2 antigens present in CEF6. ω₁is a monomeric glycoprotein with a pI > 9·0 and a molecular weight of 31 kDa. α₁consists of two immunologically cross-reactive dimers, 41 and 36 kDa in non-reducing conditions, each of which consists of one unique and one common glycoprotein subcomponent. In ELISA with mouse and human infection sera ω₁is shown to beS. mansonispecific and is better able to distinguishS. mansoniinfections from other schistosome infections than are unfractionated SEA, CEF6 or α₁. Passive transfer of monospecific anti-ω₁sera intoS. mansoniinfected, T cell-deprived mice completely prevented the occurrence of microvesicular hepatocyte damage in these animals. Monospecific anti-α₁serum had no hepatoprotective capacity.