Eight IgM monoclonal antibodies (mAbs) obtained from a Schistosoma mansoni chronically infected mouse immunized twice with adult worms butanolic extract (BE) and soluble egg antigen (SEA) were characterized by immunochemical methods. An intense cross-reactivity between different developmental stages was observed by indirect immunofluorescence assay (IIFA) with five anti-SEA mAbs. These mAbs appeared to recognize glycosidic residues, as suggested by 1) the inhibition of their reactivity by periodate oxidation of SEA, 2) the multiple polypeptide recognition in radioimmunoprecipitation and immunoblot assays and 3) reactivity with KLH. Anti-SEA mAbs were able to mediate in vitro killing of schistosomula but they were not consistently able to mediate passive transfer immunity in vivo. Three of anti-SEA mAbs were suitable for the performance of a sandwich ELISA for antibody detection in S. mansoni infected patients, allowing an increase in the signal to noise ratio as compared to the direct ELISA SEA method. Three anti-BE mAbs showed a more stage restricted pattern of antigen recognition by IIFA. Only one out of three seemed to be directed against glycan residues, but the other mAbs showed a plural pattern of polypeptide recognition on BE immunoblot, suggesting that repeated epitopic motifs are also present in different proteins within the same parasite developmental stage.