LOCALIZATION OF PLASMODIUM PROTEINS DURING THEIR EXPORT TO HOST ERYTHROCYTE

疟疾寄生虫改变并影响宿主红细胞。 在感染者体内观察到了几个新的寄生虫诱导的隔间 红细胞和寄生虫蛋白定位于这些不同的 车厢。目前尚不清楚这种寄生虫是如何运输和 靶向蛋白质到其自身质膜以外的位置。 进行了超微结构研究和免疫金定位。 要了解更多关于寄生虫如何运输和靶向蛋白质的信息 到宿主红细胞。特别是93 kDa的出口 查鲍迪疟原虫蛋白，与宿主相关 对红细胞膜进行检测。使用Brefeldin A、An的研究 分泌途径的抑制物，表明有一些输出 疟原虫蛋白质利用另一种分泌途径。这些 输出的蛋白质确实会通过内质网和 Golgi，但目标是Brefeldin A诱导的一个新的隔室。 从这个新的隔间，蛋白质很可能被分泌到 寄生性液泡，在那里它们变得与 来源于寄生虫液泡的管泡结构 薄膜。出口寄生虫蛋白的靶向和分选可能 发生在寄生性液泡膜水平上。

The malarial parasite alters and affects the host erythrocyte. Several new parasite-induced compartments are observed in the infected erythrocyte and parasite proteins are localized to these various compartments. It is not known how the parasite can transport and target proteins to locations beyond its own plasma membrane. Ultrastructural studies and immunogold localization were carried out to learn more about how the parasite transports and targets proteins to the host erythrocyte. In particular the export of the 93 kDa Plasmodium chabaudi protein, which is associated with the host erythrocyte membrane, was examined. Studies using Brefeldin A, an inhibitor of the secretory pathway, indicated that some exported Plasmodium proteins utilize an alternative secretory pathway. These exported proteins do transit through the endoplasmic reticulum and Golgi, but are targeted to a new Brefeldin A-induced compartment. From this new compartment the proteins are probably secreted into the parasitophorous vacuole, where they become associated with tubovesicular structures derived from the parasitophorous vacuolar membrane. The targeting and sorting of exported parasite proteins may occur at the level of parasitophorous vacuolar membrane.