Peretz D, Williamson R A, Matsunaga Y, Serban H, Pinilla C, Bastidas R B, Rozenshteyn R, James T L, Houghten R A, Cohen F E, Prusiner S B, Burton D R
Department of Neurology, School of Pharmacy, University of California, San Francisco, CA 94143, USA.
J Mol Biol. 1997 Oct 31;273(3):614-22. doi: 10.1006/jmbi.1997.1328.
The scrapie prion protein (PrPSc) is formed from the cellular isoform (PrPC) by a post-translational process that involves a profound conformational change. Linear epitopes for recombinant antibody Fab fragments (Fabs) on PrPC and on the protease-resistant core of PrPSc, designated PrP 27-30, were identified using ELISA and immunoprecipitation. An epitope region at the C terminus was accessible in both PrPC and PrP 27-30; in contrast, epitopes towards the N-terminal region (residues 90 to 120) were accessible in PrPC but largely cryptic in PrP 27-30. Denaturation of PrP 27-30 exposed the epitopes of the N-terminal domain. We argue from our findings that the major conformational change underlying PrPSc formation occurs within the N-terminal segment of PrP 27-30.
瘙痒病朊病毒蛋白（PrPSc）由细胞异构体（PrPC）通过一个涉及深刻构象变化的翻译后过程形成。使用酶联免疫吸附测定（ELISA）和免疫沉淀法确定了PrPC以及PrPSc的蛋白酶抗性核心（称为PrP 27-30）上重组抗体Fab片段（Fabs）的线性表位。PrPC和PrP 27-30的C末端均存在一个表位区域；相比之下，PrPC中靠近N端区域（第90至120位氨基酸残基）的表位在PrP 27-30中基本隐藏。PrP 27-30的变性暴露了N端结构域的表位。基于我们的研究结果，我们认为PrPSc形成过程中发生的主要构象变化发生在PrP 27-30的N端片段内。
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