恶性疟原虫裂殖子表面主要蛋白－１（ＭＳＡ１），又称Ｐ１９５，与人红细胞具有结合作用，这种结合是裂殖子识别红细胞的基础。为了确定Ｐ１９５蛋白与识别有关的位点，本研究在大肠杆菌中分８段表达了ＭＡＤ２０株恶性疟原虫的Ｐ１９５蛋白。各段蛋白用镍亲和层析柱分离，然后复性。在体外培养疟原虫至成熟裂殖体期，将各段蛋白分别加入到培养基上清中，继续培养２４小时，检查红细胞感染率，通过感染率了解各段蛋白对裂殖子入侵红细胞的影响。结果发现Ｐ１９５蛋白中氨基酸序列为３８４－５９５的一段蛋白（Ｍ６），呈剂量依赖性抑制恶性疟原虫裂殖子入侵人红细胞，且Ｍ６对疟原虫生长无细胞毒性作用。这表明Ｍ６可能含红细胞结合位点，该位点与裂殖子竞争性结合红细胞，而使感染率下降 Plasmodium falciparum merozoite major protein-1 (MSA1), also known as P195, binds to human erythrocytes and is the basis of merozoite recognition of erythrocytes. In order to determine the P195 protein and recognition-related sites, the study in E. coli expression in eight segments of MAD20 P. falciparum P195 protein. Each protein was separated by nickel affinity chromatography and then refolded. In vitro culture of malaria parasite to mature schizont stage, each segment of protein were added to the medium supernatant, cultured for 24 hours, check the rate of infection of red blood cells, infection rate understanding of the impact of each segment of the protein on merozoite invasion of red blood cells . The results showed that a fragment of protein (M6) with the amino acid sequence of 384-595 in P195 protein inhibited human erythrocytes invasion by P. falciparum merozoites in a dose-dependent manner, and M6 had no cytotoxic effect on Plasmodium. This suggests that M6 may contain erythrocyte binding sites that competitively bind erythrocytes with merozoites and cause a reduction in infection rate