首页> 美国卫生研究院文献>The Journal of Biological Chemistry >Multiple Plasmodium falciparum Merozoite Surface Protein 1 Complexes Mediate Merozoite Binding to Human Erythrocytes
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Multiple Plasmodium falciparum Merozoite Surface Protein 1 Complexes Mediate Merozoite Binding to Human Erythrocytes

机译:多个恶性疟原虫裂殖子表面蛋白1复合体介导裂殖子与人类红细胞的结合。

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摘要

Successful invasion of human erythrocytes by Plasmodium falciparum merozoites is required for infection of the host and parasite survival. The early stages of invasion are mediated via merozoite surface proteins that interact with human erythrocytes. The nature of these interactions are currently not well understood, but it is known that merozoite surface protein 1 (MSP1) is critical for successful erythrocyte invasion. Here we show that the peripheral merozoite surface proteins MSP3, MSP6, MSPDBL1, MSPDBL2, and MSP7 bind directly to MSP1, but independently of each other, to form multiple forms of the MSP1 complex on the parasite surface. These complexes have overlapping functions that interact directly with human erythrocytes. We also show that targeting the p83 fragment of MSP1 using inhibitory antibodies inhibits all forms of MSP1 complexes and disrupts parasite growth in vitro.
机译:恶性疟原虫裂殖子成功入侵人的红细胞是宿主感染和寄生虫存活的必要条件。侵袭的早期是通过与人红细胞相互作用的裂殖子表面蛋白介导的。这些相互作用的性质目前尚不十分清楚,但众所周知,裂殖子表面蛋白1(MSP1)对于成功入侵红细胞至关重要。在这里,我们显示外围裂殖子表面蛋白MSP3,MSP6,MSPDBL1,MSPDBL2和MSP7直接与MSP1结合,但彼此独立,从而在寄生虫表面形成多种形式的MSP1复合物。这些复合物具有与人红细胞直接相互作用的重叠功能。我们还显示,使用抑制性抗体靶向MSP1的p83片段可抑制所有形式的MSP1复合物,并在体外破坏寄生虫的生长。

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