Hope J, Manson J
Institute for Animal Health, AFRC and MRC Neuropathogenesis Unit, Edinburgh, UK.
Curr Top Microbiol Immunol. 1991;172:57-74. doi: 10.1007/978-3-642-76540-7_4.
Proteins need help to fold and attain their functional conformation (Ellis and Hemmingsen 1989), and mechanisms have evolved to prevent the accumulation of misfolded protein aggregates within cells (Pelham 1988). These mechanisms fail to prevent the formation of protease-resistant, misfolded forms of PrP (ScPrP) during the development of scrapie and other transmissible spongiform encephalopathies, and ScPrP is a biochemical marker of these diseases. Much is now known about the structure and expression of the PrP gene, but the physiological function of the PrP protein and the mechanism by which the TDE pathogen replicates and specifically interferes with PrP metabolism remain a mystery--a mystery which will entertain prion-ophiliacs for some time yet.
蛋白质需要帮助才能折叠并获得其功能构象（埃利斯和亨明森，1989年），并且已经进化出一些机制来防止细胞内错误折叠的蛋白质聚集体的积累（佩勒姆，1988年）。在羊瘙痒症和其他传染性海绵状脑病的发展过程中，这些机制无法阻止抗蛋白酶的、错误折叠形式的朊蛋白（ScPrP）的形成，并且ScPrP是这些疾病的生化标志物。目前对朊蛋白基因的结构和表达已经了解很多，但朊蛋白的生理功能以及TDE病原体复制并特异性干扰朊蛋白代谢的机制仍然是个谜——这个谜在一段时间内仍将吸引朊病毒爱好者。
