Selective neuronal targeting in prion disease
Selective neuronal targeting in prion disease
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DOI：
10.1016/s0896-6273(00)80424-9
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发表时间：
1997-12-01
期刊：
影响因子：
16.2
通讯作者：
Prusiner, SB
中科院分区：
文献类型：
--
作者：
DeArmond, SJ;Sánchez, H;Prusiner, SB
对于每种朊病毒株，羊瘙痒症朊病毒蛋白（PrPSc）在脑中积累的模式是不同的。我们测试了PrPSc沉积模式是否受转基因小鼠中PrPC的Asn连接寡糖的影响。删除第一个寡糖改变了PrPC的运输，并防止感染两种朊病毒株。删除第二个没有改变PrPC贩运，允许感染一个朊病毒株，并对PrPSc沉积模式产生深远的影响。我们的数据提出的可能性，糖基化可以修改构象的PrPC。糖基化可以影响PrPC对PrPSc的特定构象的亲和力，从而确定新生PrPSc形成的速率和PrPSc沉积的特定模式。
The pattern of scrapie prion protein (PrPSc) accumulation in the brain is different for each prion strain. We tested whether the PrPSc deposition pattern is influenced by the Asn-linked oligosaccharides of PrPC in transgenic mice. Deletion of the first oligosaccharide altered PrPC trafficking and prevented infection with two prion strains. Deletion of the second did not alter PrPC trafficking, permitted infection with one prion strain, and had a profound effect on the PrPSc deposition pattern. Our data raise the possibility that glycosylation can modify the conformation of PrPC. Glycosylation could affect the affinity of PrPC for a particular conformer of PrPSc, thereby determining the rate of nascent PrPSc formation and the specific patterns of PrPSc deposition.