Normal monomeric tau can be converted into pathogenic aggregates and acquire protease resistance in a prion-like manner. This acquisition of partial protease-resistance in tau aggregates has to date only been partially investigated in various studies exploring the prion-like properties of tau. In this study, we induced the aggregation of tau repeat domain (RD) in cultured cells using detergent insoluble fractions of Alzheimer’s brain tissue as seeds. The seeded aggregation of tau RD in cultured cells formed a ~7 kDa protease-resistant fragment in contrast to the ~12 kDa tau fragment characteristic of the AD seeds, suggesting that the in vitro generated tau aggregates were conformationally distinct from parent seeds.

正常的单体tau可以转化为致病性聚集体，并以a病毒样方式获得蛋白酶抗性。迄今为止，在探索tau的病毒样特性的各种研究中，仅部分研究了tau聚集体中部分蛋白酶抗性的获得。在这项研究中，我们使用阿尔茨海默氏症脑组织的去污剂不溶级分作为种子，诱导了培养细胞中tau重复域（RD）的聚集。与AD种子的〜12 kDa tau片段特征相反，培养细胞中tau RD的种子聚集形成了〜7 kDa蛋白酶抗性片段，这表明体外产生的tau聚集体在构象上与亲本种子不同。