The Dual Origin of Toxoplasma gondii N-Glycans
The Dual Origin of Toxoplasma gondii N-Glycans
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DOI：
10.1021/bi801090a
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发表时间：
2008-11-25
期刊：
影响因子：
2.9
通讯作者：
Schwarz, Ralph T.
中科院分区：
文献类型：
--
作者：
Garenaux, Estelle;Shams-Eldin, Hosam;Schwarz, Ralph T.
n -链糖基化是真核细胞中最常见的分泌蛋白修饰，在蛋白质折叠和转运中起着至关重要的作用。在大多数真核生物中，成熟的n -聚糖通过一个高度保守的途径在内质网和高尔基体中依次加工。在这里，我们证明了专性细胞内原生动物寄生虫刚地弓形虫独立地将内源性截断的和宿主衍生的n -聚糖转移到其自身的蛋白质上。因此，我们提出顶复体寄生虫清除宿主细胞的n -糖基化中间体，以补偿其生物合成途径的快速进化，该途径主要致力于用糖基磷脂酰肌醇而不是n -聚糖修饰蛋白质。
N-Linked glycosylation is the most frequent modification of secreted proteins in eukaryotic cells that plays a crucial role in protein folding and trafficking. Mature N-glycans are sequentially processed in the endoplasmic reticulum and Golgi apparatus through a pathway highly conserved in most eukaryotic organisms. Here, we demonstrate that the obligate intracellular protozoan parasite Toxoplasma gondii independently transfers endogenous truncated as well as host-derived N-glycans onto its own proteins. Therefore, we propose that the apicomplexan parasite scavenges N-glycosylation intermediates from the host cells to compensate for the rapid evolution of its biosynthetic pathway, which is primarily devoted to modification of proteins with glycosylphosphatidylinositols rather than N-glycans.