What it is
Most neurodegenerative diseases are thought to spread through the brain by prion-like mechanisms, in which filamentous protein assemblies self-propagate by templated seeding, and distinct conformations of amyloid filaments may provide the physical basis for the strains that lead to different diseases. A central pillar of the prion hypothesis, that strains retain their structural identity upon transmission, had not been demonstrated. The authors injected tau filaments from the brains of people with Alzheimer's disease or corticobasal degeneration into the brains of wild-type mice, and found that this led to the seeded assembly of amyloid filaments made of mouse tau with the same structures as those of the seeds.
Why it matters
The result shows that, similar to prion strains, tau filaments propagate through templated seeding, with the mouse's own tau taking on the structures of the human filaments it was seeded with. It also establishes the mouse as a suitable model for studying the molecular mechanisms by which distinct tau folds drive disease-specific pathology in the brain.
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Filed underPrion Diseases and Protein Misfolding, Alzheimer's disease research and treatments, Amyotrophic Lateral Sclerosis Research
