Caughey B
Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, Hamilton, MT 59840, USA.
Curr Issues Mol Biol. 2000 Jul;2(3):95-101.
In transmissible spongiform encephalopathies (TSE) or prion diseases, the endogenous protease-sensitive prion protein (PrP-sen) of the host is converted to an abnormal pathogenic form that has a characteristic partial protease resistance (PrP-res). Studies with cell-free reactions indicate that the PrP-res itself can directly induce this conversion of PrP-sen. This PrP-res induced conversion reaction is highly specific in ways that might account at the molecular level for TSE species barriers, polymorphism barriers, and strains. Not only has this reaction been observed using mostly purified PrP-sen and PrP-res reactants, but also in TSE-infected brain slices. The conversion mechanism appears to involve both the binding of PrP-sen to polymeric PrP-res and a conformational change that results in incorporation into the PrP-res polymer.
在传染性海绵状脑病（TSE）或朊病毒疾病中，宿主的内源性蛋白酶敏感型朊病毒蛋白（PrP-sen）会转化为具有特征性部分蛋白酶抗性的异常致病形式（PrP-res）。无细胞反应研究表明，PrP-res本身可直接诱导PrP-sen的这种转化。这种由PrP-res诱导的转化反应具有高度特异性，可能在分子水平上解释了TSE的种属屏障、多态性屏障和毒株现象。不仅使用纯化的PrP-sen和PrP-res反应物观察到了这种反应，在TSE感染的脑切片中也观察到了。转化机制似乎既涉及PrP-sen与聚合的PrP-res的结合，也涉及导致其掺入PrP-res聚合物的构象变化。
