Neural Repair and Biomaterials Laboratory, National Paraplegia Hospital, Finca la Peraleda s/n, Toledo, Spain.
Prion. 2012 Nov-Dec;6(5):430-2. doi: 10.4161/pri.22309. Epub 2012 Oct 8.
It has been described that the breakdown of β-sheets in PrP (Sc) by denaturation results in loss of infectivity and PK-sensitivity, suggesting a relationship between the structure and PK-resistance. It is also known that an important fraction of total PrP (Sc) is PK-sensitive and can be isolated by the method we already described. Consequently, we decided to employ the PK-sensitive fraction of PrP (Sc) as a potential and useful tool for structural studies. Thus, two essential questions were addressed in our recent article. First, the difference in the infectivity between the sensitive and resistant fractions and second, whether sensitive and resistant PrP (Sc) shared the same conformation or were only different size multimers with the same basic conformation. Here we discuss our latest data in light of recent infectivity studies and their possible implications on the conformation of the prion.
已经有人描述过,通过变性使 PrP(Sc)中的β-折叠结构解体,会导致感染性和 PK 敏感性丧失,这表明结构与 PK 抗性之间存在关联。人们也知道,总 PrP(Sc)中有很大一部分是 PK 敏感的,可以用我们已经描述过的方法分离出来。因此,我们决定将 PrP(Sc)的 PK 敏感部分用作结构研究的潜在有用工具。因此,在我们最近的文章中,我们解决了两个重要问题。首先,敏感和抗性部分之间的感染力差异,其次,敏感和抗性 PrP(Sc)是否具有相同的构象,或者只是具有相同基本构象的不同大小多聚体。在这里,我们根据最近的感染性研究讨论我们的最新数据及其对朊病毒构象的可能影响。