Prion-like transmission of human tau strains in the mouse brain

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.

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Publication Details

Journal
Nature
Published
2026-09-30
DOI
https://doi.org/10.1038/s41586-026-11061-x
Citations
1
Primary Topic
Prion Diseases and Protein Misfolding
Type
article
Field-Weighted Citation Impact
2.41
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Prion-like transmission of human tau strains in the mouse brain

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Prion-like transmission of human tau strains in the mouse brain

Hisaomi Suzuki, Mitsumoto Onaya, Mari Yoshida, Masami Masuda‐Suzukake, Shigeo Murayama, Michel Goedert, Andrew Robinson, Aki Shimozawa, Sjors H. W. Scheres, Airi Tarutani, Reiko Ohtani, Masato Hasegawa, Yuko Saito, Kazuko Hasegawa, Sofia Lövestam
article en
1 citations

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.

Nature
Aichi Medical University (JP), MRC Laboratory of Molecular Biology (GB), University of Manchester (GB), Tokyo Metropolitan Institute of Medical Science (JP), National Sagamihara Hospital (JP), National Hospital Organization (JP), Tokyo Metropolitan Institute of Gerontology (JP), Osaka Metropolitan University (JP)
Openalex Percentile: Top 8%
Prion Diseases and Protein Misfolding
2.41
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