The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking
The cytoplasmic domain of the Plasmodium falciparum ligand EBA-175 is essential for invasion but not protein trafficking
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DOI：
10.1083/jcb.200301046
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发表时间：
2003-07-21
影响因子：
7.8
通讯作者：
Cowman, AF
中科院分区：
文献类型：
--
作者：
Gilberger, TW;Thompson, JK;Cowman, AF
恶性疟原虫（Plasmodium, falciparum）入侵宿主细胞需要寄生虫和宿主受体之间特定的蛋白质-蛋白质相互作用，以及细胞内易位机制为这一过程提供动力。跨膜红细胞结合蛋白175 （EBA-175）和血栓反应蛋白相关匿名蛋白（TRAP）在这一过程中起核心作用。EBA-175在入侵过程中与人红细胞上的糖蛋白A结合，将寄生虫与宿主细胞表面连接起来。在本报告中，我们发现EBA-175的细胞质结构域编码了其在裂殖子入侵中所起作用的关键信息，并且该蛋白的运输独立于该结构域。此外，我们发现TRAP的细胞质结构域可以替代EBA-175的细胞质结构域。TRAP是一种不在裂殖子中表达的蛋白质，但在孢子子阶段侵入肝细胞时是必不可少的。这些结果表明，无论宿主细胞类型和入侵形式如何，寄生虫都使用其细胞机制的相同组成部分进行入侵。
The invasion of host cells by the malaria parasite Plasmodium, falciparum requires specific protein-protein interactions between parasite and host receptors and an intracellular translocation machinery to power the process. The transmembrane erythrocyte binding protein-175 (EBA-175) and thrombospondin-related anonymous protein (TRAP) play central roles in this process. EBA-175 binds to glycophorin A on human erythrocytes during the invasion process, linking the parasite to the surface of the host cell. In this report, we show that the cytoplasmic domain of EBA-175 encodes crucial information for its role in merozoite invasion, and that trafficking of this protein is independent of this domain. Further, we show that the cytoplasmic domain of TRAP, a protein that is not expressed in merozoites but is essential for invasion of liver cells by the sporozoite stage, can substitute for the cytoplasmic domain of EBA-175. These results show that the parasite uses the same components of its cellular machinery for invasion regardless of the host cell type and invasive form.