The 27-kDa excretory-secretory antigen partially purified from adult Fasciola gigantica adult worms (FG27) has been used as the sensitive and specific antigen for immunodiagnosis of human fascioliasis. Lectin-blot analyses have shown that the FG27 possesses both N - and O -glycans. In two-dimensional electrophoresis, silver staining, lectin blotting and immunoblotting, FG27 displayed at least four antigenic-glycosylated protein spots at the pI values of 4.8, 4.9, 5.2 and 5.4, respectively. After removing glycan moieties from the antigen by alkaline treatment, the molecular mass of the FG27 was reduced to 26.5 kDa as a prominent deglycosylated band. Immunoblotting analysis has revealed that the 26.5-kDa band reacts with the pooled human fascioliasis sera without any loss of antigenicity. These results suggest that the major antigenicity of the FG27 is due to its protein epitopes.