DeArmond S J, McKinley M P, Barry R A, Braunfeld M B, McColloch J R, Prusiner S B
Cell. 1985 May;41(1):221-35. doi: 10.1016/0092-8674(85)90076-5.
Extracellular collections of abnormal filaments composed of prion proteins have been identified in the brains of scrapie-infected hamsters using immunoelectron microscopy. Some of the filaments were 1500 nm in length; generally, they exhibited a uniform diameter of 16 nm. Rarely, the filaments had a twisted appearance, raising the possibility that they are flattened cylinders or are composed of helically wound protofilaments. The prion filaments possess the same diameter and limited twisting as the shorter rod-shaped particles observed in purified preparations of prions. Both the filaments and rods are composed of PrP 27-30 molecules, as determined by immunoelectron microscopy using affinity-purified antibodies. The ultrastructural features of the prion filaments are similar to those reported for amyloid in many tissues including brain. These results provide the first evidence that prion proteins assemble into filaments within the brain and that these filaments accumulate in extracellular spaces to form amyloid plaques.
利用免疫电子显微镜技术，在感染羊瘙痒病的仓鼠大脑中发现了由朊病毒蛋白组成的异常细丝的细胞外聚集体。其中一些细丝长度为1500纳米；一般来说，它们的直径均匀为16纳米。细丝很少呈现扭曲的外观，这增加了它们是扁平圆柱体或由螺旋缠绕的原纤维组成的可能性。朊病毒细丝的直径与在纯化的朊病毒制剂中观察到的较短杆状颗粒相同，且扭曲程度有限。通过使用亲和纯化抗体的免疫电子显微镜确定，细丝和杆状物均由PrP 27 - 30分子组成。朊病毒细丝的超微结构特征与许多组织（包括大脑）中报道的淀粉样蛋白相似。这些结果首次证明，朊病毒蛋白在大脑中组装成细丝，并且这些细丝在细胞外空间积累形成淀粉样斑块。
