Abstract: Truncated 45W-4B with the deletion of signal peptide sequence and C?terminal nucleotides encoding 17 hydrophobic amino acids, cloned into BamH I and EcoR I pre-digested pGEX-4T-1 and transformed into competent BL21 and the positive transformants were determined by enzyme restriction and PCR and sequencing, followed by ligating with the signal sequence-removed 18ku fragment, the positive designed as pGEX-4BX/18. Results of SDS-PAGE and Western blot showed that the 50ku fusion protein was expressed at a high level in E. coli and recognized by sera from either patients or pigs early infected by Cysticercus cellulosae. In order to evaluate the efficacy of 4BX/18 and 4BX antigens, vaccination trail was performed with 300礸 dose per pig. Statistic data indicated that the efficacy of the group immunized with 4BX/18 was 99%, a little higher than that of the GST-4BX group (95%), supporting the bases of development of highly efficient recombinant vaccines against cysticercosis jointly using different protective antigens from different developmental stages of parasites.