In neurodegenerative disorders such as Alzheimer’s disease and corticobasal degeneration, the microtubule-associated protein tau forms toxic fibrils, whose regional spreading in the human brain correlates well with cognitive decline and disease severity. Studies have raised the possibility that tau filaments, like prion aggregates, propagate in a manner whereby misfolded seeds serve as templates for the misfolding of native proteins. However, direct evidence supporting this view has been missing. Writing in Nature, Lövestam, Shimozawa, Tarutani and colleagues addressed this issue by injecting tau filaments extracted from the brains of patients with Alzheimer’s disease or corticobasal degeneration into wild-type mouse brains and comparing the atomic structures of tau assemblies across species. They found that the resulting mouse tau assemblies faithfully replicated the precise, disease-specific folds of the human seeds. These data provide long-sought proof that tau filaments, like prion proteins, propagate through the brain through templated seeding. Future studies could reveal at which step of tau propagation this faithful structural templating occurs.
Original reference: Nature https://doi.org/10.1038/s41586-026-11061-x (2026)
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Source: Nature Neuroscience — Read the full article on the original site ↗