Rhoptry neck protein RON2 forms a complex with microneme protein AMA1 in Plasmodium falciparum merozoites
Rhoptry neck protein RON2 forms a complex with microneme protein AMA1 in Plasmodium falciparum merozoites
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恶性疟原虫裂殖子中棒状体颈蛋白 RON2 与微线体蛋白 AMA1 形成复合物
DOI：
10.1016/j.parint.2008.09.005
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发表时间：
2009-03-01
影响因子：
1.9
通讯作者：
Torii, Motomi
中科院分区：
文献类型：
--
作者：
Cao, Jun;Kaneko, Osamu;Torii, Motomi
红细胞入侵是疟原虫感染宿主的重要步骤，也是试图控制该疾病的干预策略的主要目标。最近对密切相关的顶复门寄生虫弓形虫的蛋白质组分析揭示了一组位于菱形颈部的新型蛋白质（RON）。其中三种蛋白 RON2、RON4 和 RON5 已被证明可与微线体蛋白顶端膜蛋白 1 (AMA1) 形成复合物。这种复合物被称为移动连接复合物，在入侵过程中位于寄生虫和宿主细胞的界面处。在这里，我们表征了恶性疟原虫中的 RON2 直向同源物。 PfRON2 转录在成熟裂殖体阶段达到顶峰，并在裂殖子的棒状体颈部表达。 PfRON2、PfRON4 和 PfAMA1 的免疫共沉淀表明弓形虫和恶性疟原虫之间的复合物形成是保守的，这表明棒状体和微线体蛋白的协同功能是顶复门寄生虫在宿主细胞入侵过程中的常见机制。 PfRON2 拥有与菱形体蛋白 PjRhopH1/Clag（RhopH 复合物的一个组成部分）显示同源性的区域。然而，我们在此提出的免疫共沉淀研究表明PfRON2不是RhopH复合物的组成部分并且具有独立的作用，核苷酸多态性分析表明PfRON2处于多样化的选择压力下。这一证据表明，RON2 似乎在顶复门寄生虫入侵宿主细胞中发挥着重要作用，并且是疟疾干预策略的潜在目标。 (C) 2008 Elsevier Ireland Ltd. 保留所有权利。
Erythrocyte invasion is an essential step in the establishment of host infection by malaria parasites, and is a major target of intervention strategies that attempt to control the disease. Recent proteome analysis of the closely-related apicomplexan parasite, Toxoplasma gondii, revealed a panel of novel proteins (RONs) located at the neck portion of the rhoptries. Three of these proteins, RON2, RON4, and RON5 have been shown to form a complex with the microneme protein Apical Membrane Protein 1 (AMA1). This complex, termed the Moving junction complex, localizes at the interface of the parasite and the host cell during the invasion process. Here we characterized a RON2 ortholog in Plasmodium falciparum. PfRON2 transcription peaked at the Mature schizont stage and was expressed at the neck portion of the rhoptry in the merozoite. Co-immunoprecipitation of PfRON2, PfRON4 and PfAMA1 indicated that the complex formation is conserved between T gondii and P. falciparum, suggesting that co-operative function of the rhoptry and microneme proteins is a common mechanism in apicomplexan parasites during host cell invasion. PfRON2 possesses a region displaying homology with the rhoptry body protein PjRhopH1/Clag, a component of the RhopH complex. However, here we present co-immunoprecipitation studies which suggest that PfRON2 is not a component of the RhopH complex and has an independent role, Nucleotide polymorphism analysis suggested that PfRON2 was under diversifying selective pressure. This evidence suggests that RON2 appears to have a fundamental role in host cell invasion by apicomplexan parasites, and is a potential target for malaria intervention strategies. (C) 2008 Elsevier Ireland Ltd. All rights reserved.