Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
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DOI：
10.1083/jcb200307147
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发表时间：
2004-01-05
影响因子：
7.8
通讯作者：
Goldberg, DE
中科院分区：
文献类型：
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作者：
Klemba, M;Beatty, W;Goldberg, DE
血浆蛋白水解酶(Pms)是一类天冬氨酸氨基转移酶家族，在恶性疟原虫食物液泡中的血红蛋白降解过程中起关键作用。为了研究proPM 11的转运，我们对恶性疟原虫染色体上的PM 11基因进行了修饰，编码了proPM II-GFP嵌合体。利用活体寄生虫的绿色荧光蛋白荧光，免疫电子显微镜的超微结构分辨率，以及运输和PM成熟的抑制剂，我们研究了导致食物液泡中成熟PM 11的生物合成途径。我们的数据支持这样一个模型，即ProPM11通过分泌系统运输到细胞气孔空泡，然后与其底物血红蛋白一起被运送到食物液泡，在那里它被蛋白质降解处理成成熟的PM II。
A family of aspartic proteases, the plasmepsins (PMs), plays a key role in the degradation of hemoglobin in the Plasmodium falciparum food vacuole. To study the trafficking of proPM 11, we have modified the chromosomal PM 11 gene in P falciparum to encode a proPM II-GFP chimera. By taking advantage of green fluorescent protein fluorescence in live parasites, the ultrastructural resolution of immunoelectron microscopy, and inhibitors of trafficking and PM maturation, we have investigated the biosynthetic path leading to mature PM 11 in the food vacuole. Our data support a model whereby proPM 11 is transported through the secretory system to cytostomal vacuoles and then is carried along with its substrate hemoglobin to the food vacuole where it is proteolytically processed to mature PM II.