Summary: The 19 kDa carboxy-terminal domain of merozoite surface protein-1 (MSP1) was expressed in vaccine strains as a carboxy-terminal fusion to fragment C of tetanus toxin (TetC). This study demonstrates that antibodies that recognize disulphide-dependent conformational epitopes in native MSP1 react with the TetC-MSP1 fusion protein expressed in The proper folding of MSP1 polypeptide is dependent on both the host strain and the protein to which the MSP1 polypeptide is fused. Serum from mice immunized with C5 expressing TetC-MSP1 recognized native MSP1 as shown by immunofluorescence with -infected erythrocytes. Antibody levels to MSP1 were highest in out-bred mice immunized with C5 carrying pTECH2-MSP1 and antibody was mostly directed against reduction-sensitive conformational epitopes. However, antibody levels were lower than in BALB/c mice immunized with a glutathione -transferase (GST)-MSP1 fusion protein in Freund's adjuvant, and which were protected against challenge infection. In challenge experiments with the -immunized mice were not protected, probably reflecting the magnitude of the antibody response. The results of this study have important implications in the design of live multivalent bacterial vaccines against eukaryotic pathogens.


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