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首页> 外文期刊>Protein Science: A Publication of the Protein Society >Identifying Plasmodium falciparum merozoite surface antigen 3 (MSP3) protein peptides that bind specifically to erythrocytes and inhibit merozoite invasion.
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Identifying Plasmodium falciparum merozoite surface antigen 3 (MSP3) protein peptides that bind specifically to erythrocytes and inhibit merozoite invasion.

机译：鉴定恶性疟原虫裂殖子表面抗原3（MSP3）蛋白肽，该蛋白肽特异性结合红细胞并抑制裂殖子入侵。

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摘要

Receptor-ligand interactions between synthetic peptides and normal human erythrocytes were studied to determine Plasmodium falciparum merozoite surface protein-3 (MSP-3) FC27 strain regions that specifically bind to membrane surface receptors on human erythrocytes. Three MSP-3 protein high activity binding peptides (HABPs) were identified; their binding to erythrocytes became saturable, had nanomolar affinity constants, and became sensitive on being treated with neuraminidase and trypsin but were resistant to chymotrypsin treatment. All of them specifically recognized 45-, 55-, and 72-kDa erythrocyte membrane proteins. They all presented alpha-helix structural elements. All HABPs inhibited in vitro P. falciparum merozoite invasion of erythrocytes by ~55%-85%, suggesting that MSP-3 protein's role in the invasion process probably functions by using mechanisms similar to those described for other MSP family antigens.
机译：研究了合成肽与正常人红细胞之间的受体-配体相互作用，以确定与人红细胞膜表面受体特异性结合的恶性疟原虫裂殖子表面蛋白3（MSP-3）FC27菌株区域。鉴定了三种MSP-3蛋白高活性结合肽（HABP）;它们与红细胞的结合变得饱和，具有纳摩尔摩尔亲和常数，并且在接受神经氨酸酶和胰蛋白酶治疗时变得敏感，但对胰凝乳蛋白酶治疗具有抗性。它们全部特异性识别45、55和72kDa的红细胞膜蛋白。他们都提出了α-螺旋结构元素。所有HABP均抑制体外恶性疟原虫裂殖子侵染红细胞约55％-85％，这表明MSP-3蛋白在侵袭过程中的作用可能是通过使用与其他MSP家族抗原相似的机制起作用的。

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