Assistance of Maltose Binding Protein to the in Vivo Folding of the Disulfide-Rich C-Terminal Fragment from Plasmodium falciparum Merozoite Surface Protein 1 Expressed in Escherichia coli†

摘要: The C-terminal fragment of Plasmodium falciparum merozoite surface protein 1 (F19) is a leading candidate for the development malaria vaccine. Successful vaccination trials on primates, immunochemistry, and structural studies have shown importance its native conformation protective role against infection. F19 disulfide-rich protein, correct pairing 12 half-cystines required state protein. has been produced in Escherichia coli periplasm, which an oxidative environment favorable formation disulfide bonds. was either expressed as fusion with maltose binding (MBP) or directly addressed to periplasm by fusing it MBP signal peptide. Direct expression led misfolded heterogeneous distribution bridges. On contrary, when E. MBP, moiety natively folded. Indeed, after proteolysis resulting possesses characteristics immunochemical reactivity analogous baculovirus-infected insect cells yeast. These results demonstrate that positive effect assisting folding passenger proteins extends bridges vivo. Although fragments fused frequently success, our comparative study evidences first time helping property