Expression of disulphide-bridge-dependent conformational epitopes and immunogenicity of the carboxy-terminal 19 kDa domain of plasmodium yoelii merozoite surface protein-1 in live attenuated Salmonella vaccine strains

A study was conducted to analyze the expression of the 19 kDa carboxy-terminal domain of Plasmodium yoelii merozoite surface protein in Salmonella vaccine strains as a carboxy-terminal fusion to fragment C of tetanus toxin. The design of live multivalent bacterial vaccines against eukaryotic pathogens was also examined. Experimental results indicated that the lack of protection correlated with the antibody response.