The deposition of amyloid-β (Aβ) plaques and tau-based neurofibrillary tangles is a neuropathological feature of Alzheimer's disease (AD). While studies have shown that the Aβ and tau interaction results in elevated AD pathology, the molecular linkage and mechanism of interaction of Aβ and tau are unclear. A recent study demonstrated the direct interaction between the Aβ core and specific regions of tau that facilitates pathological cross-seeding via a shared epitope. The data suggest that targeting the common epitope could be a more effective treatment strategy rather than targeting only Aβ or only tau. The findings have an important clinical significance for AD and related tauopathies.

中文翻译：

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β-淀粉样蛋白核心和Tau之间的直接相互作用促进了交叉播种：治疗干预的新靶点。

淀粉样蛋白-β（Aβ）斑块和基于tau的神经原纤维缠结的沉积是阿尔茨海默氏病（AD）的神经病理学特征。虽然研究表明，Aβ和tau相互作用导致AD病理升高，但Aβ和tau的分子连锁和相互作用机理尚不清楚。最近的一项研究表明，Aβ核心与tau的特定区域之间存在直接相互作用，这有助于通过共享表位进行病理性交叉播种。数据表明，靶向共同表位可能是一种更有效的治疗策略，而不是仅靶向Aβ或仅靶向tau。这些发现对AD和相关的疾病具有重要的临床意义。