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首页> 外文期刊>Infection and immunity >The Plasmodium vivax Merozoite Surface Protein 1 Paralog Is a Novel Erythrocyte-Binding Ligand of P. vivax
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The Plasmodium vivax Merozoite Surface Protein 1 Paralog Is a Novel Erythrocyte-Binding Ligand of P. vivax

机译：间日疟原虫裂殖子表面蛋白1旁系同源物是间日疟原虫的一种新型的红细胞结合配体。

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Merozoite surface protein 1 of Plasmodium vivax (PvMSP1), a glycosylphosphatidylinositol-anchored protein (GPI-AP), is a malaria vaccine candidate for P. vivax. The paralog of PvMSP1, named P. vivax merozoite surface protein 1 paralog (PvMSP1P; PlasmoDB PVX_099975), was recently identified and predicted as a GPI-AP. The similarities in genetic structural characteristics between PvMSP1 and PvMSP1P (e.g., size of open reading frames, two epidermal growth factor-like domains, and GPI anchor motif in the C terminus) led us to study this protein. In the present study, different regions of the PvMSP1P protein, demarcated based on the processed forms of PvMSP1, were expressed successfully as recombinant proteins [i.e., 83 (A, B, and C), 30, 38, 42, 33, and 19 fragments]. We studied the naturally acquired immune response against each fragment of recombinant PvMSP1P and the potential ability of each fragment to bind erythrocytes. The N-terminal fragment (83A) and two C-terminal fragments (33 and 19) reacted strongly with sera from P. vivax-infected patients, with 50 to 68% sensitivity and 95 to 96% specificity, respectively. Due to colocalization of PvMSP1P with PvMSP1, we supposed that PvMSP1P plays a similar role as PvMSP1 during erythrocyte invasion. An in vitro cytoadherence assay showed that PvMSP1P, especially the 19-kDa C-terminal region, could bind to erythrocytes. We also found that human sera from populations naturally exposed to vivax malaria and antisera obtained by immunization using the recombinant molecule PvMSP1P-19 inhibited in vitro binding of human erythrocytes to PvMSP1P-19. These results provide further evidence that the PvMSP1P might be an essential parasite adhesion molecule in the P. vivax merozoite and is a potential vaccine candidate against P. vivax.
机译：间日疟原虫（PvMSP1）的裂殖子表面蛋白1是糖基磷脂酰肌醇固定蛋白（GPI-AP），是间日疟原虫的疟疾疫苗候选者。 PvMSP1的旁系同源物，称为间日疟原虫裂殖子表面蛋白1旁系同源物（PvMSP1P; PlasmoDB PVX_099975），最近被鉴定并预测为GPI-AP。 PvMSP1和PvMSP1P之间的遗传结构特征相似（例如，开放阅读框的大小，两个表皮生长因子样结构域和C末端的GPI锚定基序）使我们研究了该蛋白。在本研究中，PvMSP1P蛋白的不同区域（根据PvMSP1的加工形式划分）成功表达为重组蛋白[即83（A，B和C），30、38、42、33和19碎片]。我们研究了针对重组PvMSP1P的每个片段的自然获得的免疫应答以及每个片段结合红细胞的潜在能力。 N末端片段（83A）和两个C末端片段（33和19）与间日疟原虫感染患者的血清反应强烈，分别具有50至68％的敏感性和95至96％的特异性。由于PvMSP1P与PvMSP1共定位，我们认为PvMSP1P在红细胞入侵过程中起着与PvMSP1类似的作用。体外细胞粘附试验表明，PvMSP1P，尤其是19-kDa C末端区域，可以与红细胞结合。我们还发现，来自自然暴露于间日间疟疾疟疾的人群的人血清和通过使用重组分子PvMSP1P-19免疫接种获得的抗血清抑制了人红细胞与PvMSP1P-19的体外结合。这些结果提供了进一步的证据，表明PvMSP1P可能是间日疟原虫裂殖子中必不可少的寄生虫粘附分子，并且是抗间日疟原虫的潜在疫苗候选者。

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