PLASMODIUM-VIVAX MEROZOITE SURFACE PROTEIN-1 C-TERMINAL RECOMBINANT PROTEINS IN BACULOVIRUS

Recombinant proteins derived from the Plasmodium vivax merozoite surfa ce protein 1 have been produced in the baculovirus expression system. These proteins correspond approximately to the Plasmodium vivax analog s of the 42-kDa or 19-kDa C-terminal processing products previously de scribed for Plasmodium falciparum. Each was produced in two versions, either as a membrane-bound entity located on the cell surface and prob ably carrying a glycosylphosphatidylinositol addition, or as a secrete d entity lacking a membrane anchor. Many native conformational epitope s appear to be accurately reproduced in these molecules. Both the 42-k Da and 19-kDa analogs an be N-glycosylated in the baculovirus system a nd the N-glycosylation appears to be necessary for efficient secretion of both the 42-kDa and 19-kDa recombinant proteins.