We have demonstrated that a mouse monoclonal IgE antibody, SJ18 epsilon.1, recognizes a 97 kDa surface molecule (Sj97) of Schistosoma japonicum larvae and that the antibody induces partial but significant protection against the skin to lung-stage of S. japonicum infection. The antibody stimulates eosinophil- and macrophage-mediated killing of schistosomula in vitro. In the present study, we isolated the putative full-length cDNA of Sj97 by screening a lambda gt11 cDNA library from S. japonicum adult worms with SJ18 epsilon.1. The predicted amino acid sequence of the cDNA showed highly significant homology to that of S. mansoni paramyosin, a potential vaccine candidate for schistosomiasis. The deletion mutants of S. japonicum paramyosin were expressed in Escherichia coli and the translation product of 443 amino acid residues of paramyosin was found to be recognized by the antibody. Moreover, we observed by immunoelectron microscopy the presence of paramyosin in the post-acetabular gland as well as in the tegument and muscle layers of the larvae. These results suggest that paramyosin is a secretory protein which may be incorporated into the tegument during the development of schistosomula, thus becoming a target for protective immunity during the migratory phase of the parasite.