Nature· 2026Q1
Prion-like transmission of human tau strains in the mouse brain
- 1citations
- Q1SCImago
- 2026year
Short summary
Human tau filaments from Alzheimer's disease and corticobasal degeneration brains retain their structural identity when transmitted to wild-type mouse brains, seeding mouse tau assemblies with identical structures.
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Key points
- Human tau filaments from Alzheimer's disease and corticobasal degeneration were injected into wild-type mouse brains.
- Injected tau filaments seeded the assembly of endogenous mouse tau into amyloid filaments.
- The structural conformation of the newly formed mouse tau filaments was identical to the human tau seeds.
- This confirms that tau strains retain structural identity upon transmission via templated seeding.
AI-generated from the title and abstract; the full text is not read.
Abstract
Abstract Most neurodegenerative diseases are thought to spread through the brain by prion-like mechanisms, in which filamentous protein assemblies self-propagate by templated seeding 1 . Distinct conformations of amyloid filaments may provide the physical basis for the strains that lead to different diseases 2 . However, a central pillar of the prion hypothesis, that strains retain their structural identity upon transmission, has not been demonstrated. Here we show that the injection of tau filaments from the brains of individuals with Alzheimer’s disease or corticobasal degeneration into the brains of wild-type mice leads to the seeded assembly of amyloid filaments made of mouse tau with the same structures as those of the seeds. Thus, we show that, similar to prion strains, tau filaments propagate through templated seeding, and that the mouse is a suitable model to study the molecular mechanisms by which distinct tau folds drive disease-specific pathology in the brain.
The authors' abstract, as published at the source. Nature, 2026 · DOI ↗
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Field: Molecular Biology
Molecular BiologyBiochemistry, Genetics and Molecular Biology