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.