具有真实朊病毒感染性的错误折叠朊病毒蛋白的无细胞形成。
Cell-free formation of misfolded prion protein with authentic prion infectivity.
作者信息
Weber Petra, Giese Armin, Piening Niklas, Mitteregger Gerda, Thomzig Achim, Beekes Michael, Kretzschmar Hans A
机构信息
Center for Neuropathology and Prion Research, Ludwig Maximilians University of Munich, Feodor-Lynen-Strasse 23, 81377 Munich, Germany.
出版信息
Proc Natl Acad Sci U S A. 2006 Oct 24;103(43):15818-23. doi: 10.1073/pnas.0605608103. Epub 2006 Oct 9.
Abstract
Prion propagation has been modeled in vitro; however, the low infectious titer of PrP(Sc) thus generated has cast doubt on the "protein-only" hypothesis. Here we show that prion delivery on suitable nitrocellulose carrier particles abrogates the apparent dissociation of PrP(Sc) and infectivity. Misfolded prion protein generated by protein misfolding cyclic amplification is as infectious as authentic brain-derived PrP(Sc) provided that confounding effects related to differences in the size distribution of prion protein aggregates generated in vitro and consecutive differences in regard to biological clearance are abolished.
摘要
朊病毒的传播已在体外建立了模型；然而，由此产生的低感染滴度的PrP(Sc)对“仅蛋白质”假说提出了质疑。在这里，我们表明，在合适的硝酸纤维素载体颗粒上递送朊病毒可消除PrP(Sc)与传染性之间明显的解离。通过蛋白质错误折叠循环扩增产生的错误折叠朊病毒蛋白与源自真实大脑的PrP(Sc)一样具有传染性，前提是消除与体外产生的朊病毒蛋白聚集体大小分布差异以及生物清除方面的连续差异相关的混杂效应。
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