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首页> 外文期刊>Infection and immunity >Plasmodium falciparum Merozoite Surface Protein 8 Is a Ring-Stage Membrane Protein That Localizes to the Parasitophorous Vacuole of Infected Erythrocytes
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Plasmodium falciparum Merozoite Surface Protein 8 Is a Ring-Stage Membrane Protein That Localizes to the Parasitophorous Vacuole of Infected Erythrocytes

机译：疟原虫疟原虫Merozoite表面蛋白8是环级膜蛋白，其定位于受感染的红细胞的吸血管液中

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To date, the following seven glycosylphosphatidylinositol (GPI)-anchored merozoite antigens have been described in Plasmodium falciparum: merozoite-associated surface protein 1 (MSP-1), MSP-2, MSP-4, MSP-5, MSP-8, MSP-10, and the rhoptry-associated membrane antigen. Of these, MSP-1, MSP-8, and MSP-10 possess a double epidermal growth factor (EGF)-like domain at the C terminus, and these modules are considered potential targets of protective immunity. In this study, we found that surprisingly, P. falciparum MSP-8 is transcribed and translated in the ring stage and is absent from the surface of merozoites. MSP-8 is the only GPI-anchored protein known to be expressed at this time. It is synthesized as a mature 80-kDa protein which is rapidly processed to a C-terminal 17-kDa species that contains the double EGF module. As determined by a combination of immunofluorescence and membrane purification approaches, it appears likely that MSP-8 initially localizes to the parasite plasma membrane in the ring stage. Although the C-terminal 17-kDa fragment is present in more mature stages, at these times it is found in the food vacuole. We successfully disrupted the MSP-8 gene in P. falciparum, a process that validated the specificity of the antibodies used in this study and also demonstrated that MSP-8 does not play a role essential to maintenance of the erythrocyte cycle. This finding, together with the observation that MSP-8 is exclusively intracellular, casts doubt over the viability of this antigen as a vaccine. However, it is still possible that MSP-8 is involved in an early parasitophorous vacuole function that is significant for pathogenesis in the human host.
机译：迄今为止，已在疟原虫（Malozoite相关的表面蛋白1（MSP-1），MSP-2，MSP-4，MSP - 5，MSP-8，MSP-10和鼻窦相关膜抗原。其中MSP-1，MSP-8和MSP-10具有在C末端的双表皮生长因子（EGF）域，并且这些模块被认为是保护性免疫的潜在目标。在这项研究中，我们发现令人惊讶的是， p。在环阶段转录并翻译恶妖程度，并从Merozoites的表面缺席。 MSP-8是此时已知唯一已知的GPI锚定蛋白质。它被合成为成熟的80-KDA蛋白，其迅速加工成含有双EGF模块的C末端17-KDA物种。通过免疫荧光和膜净化方法的组合来确定，MSP-8似乎最初定位在环阶段中的寄生虫膜膜。虽然C末端17-KDA片段在更成熟的阶段存在，但是在这些时间存在于食物液泡中。我们成功地中断了 P中的 MSP-8 基因。 Falciparum ，验证了本研究中使用的抗体的特异性的过程，并证明MSP-8不会发挥对性红细胞循环的影响至关重要的作用。这种发现与MSP-8专为细胞内的观察结果一起施放对该抗原作为疫苗的可行性的疑虑。然而，MSP-8仍然可以参与早期吸引力的液泡功能，这对于人宿主中的发病性具有重要意义。

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