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首页> 美国政府科技报告 >Production of a Recombinant E. coli Expressed Malarial Vaccine from the C-Terminal Fragment of Plasmodium Falciparum 3D7 Merozoite Surface Protein-1
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Production of a Recombinant E. coli Expressed Malarial Vaccine from the C-Terminal Fragment of Plasmodium Falciparum 3D7 Merozoite Surface Protein-1

机译：从恶性疟原虫3D7裂殖子表面蛋白-1的C末端片段生产重组大肠杆菌表达的疟疾疫苗

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P. falciparum Merozoite Surface Protein-1 (MSP-1) is a leading erythrocytic stage vaccine candidate. Following secondary proteolytic processing, it may play a role in binding and/or invasion of erythrocytes. The secondary processing gives a 33kD and 19kD fragment. The MSP1-19 is a target for parasite inhibitory antibodies and protective immunity. However, it appears to lack T-helper epitopes. Since antibody is likely the effector mechanism induced by MSP1-19, it is important to insure that recombinant vaccines based on this antigen be folded correctly and contain T-helper epitopes that will enhance induction of humoral responses. We have developed recombinant MSP1-42 molecules that are structurally correct based on positive reactivities with conformation- dependent mAbs. These proteins have been produced to greater than 95% purity and exceed FDA endotoxin standards. Immunogenicity studies in mice and Rhesus monkeys reveal that good antibody responses are induced to MSP1-42 when these animals are immunized with the MSP1-42 plus SBAS2 adjuvant.

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