Distinct Tau Prion Strains Propagate in Cells and Mice and Define Different Tauopathies
Open accessAbstract
Prion-like propagation of tau aggregation might underlie the stereotyped progression of neurodegenerative tauopathies. True prions stably maintain unique conformations ("strains") in vivo that link structure to patterns of pathology. We now find that tau meets this criterion. Stably expressed tau repeat domain indefinitely propagates distinct amyloid conformations in a clonal fashion in culture. Reintroduction of tau from these lines into naive cells reestablishes identical clones. We produced two strains in vitro that induce distinct pathologies in vivo as determined by successive inoculations into three generations of transgenic mice. Immunopurified tau from these mice recreates the original strains in culture. We used the cell system to isolate tau strains from 29 patients with 5 different tauopathies, finding that different diseases are associated with different sets of strains. Tau thus demonstrates essential characteristics of a prion. This might explain the phenotypic diversity of tauopathies and could enable more effective diagnosis and therapy.
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In mouse models, network studies have been based on inoculation of seeds, which does not reflect a normal disease process, and is prone to experimental artifact.
“In mouse models, network studies have been based on inoculation of seeds (Sanders et al., 2014; Detrez et al., 2019), which does not reflect a normal disease process, and is prone to experimental artifact.”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Sanders et al., 2014
The Results sections on tau pathology and spread in mice describe hippocampal inoculation followed by pathology in connected regions. The paper also says it cannot exclude spread of the inoculum itself as an explanation for the observed spread. It does not state that inoculation fails to reflect a normal disease process or that such studies are generally prone to experimental artifact. Page numbers were not available in our copy. (LLM, conf=0.85)
Experimental — accuracy not yet measuredTau toxicity is likely qualitatively and quantitatively heterogeneous, possibly due to diversity of tau species associated with distinct modifications, binding partners, and/or cellular locations.
“Tau toxicity is likely to be qualitatively and quantitatively heterogeneous, possibly due to the diversity of tau species associated with distinct modifications, binding partners, and/or cellular locations [113].”
From Stabilization of Microtubule-Unbound Tau via Tau Phosphorylation at Ser262/356 by Par-1/MARK Contributes to Augmentation of AD-Related Phosphorylation and Aβ42-Induced Tau Toxicity (2016) · cites this paper as [113]
The Results section (“Tau RD propagates conformationally distinct strains”; page not provided) reports that two tau strains differed in their effects on cell growth and survival, supporting heterogeneous toxicity. The paper also reports diverse patient-derived tau strains, but the passages do not attribute differences in toxicity to distinct modifications, binding partners, or cellular locations. (LLM, conf=0.88)
Experimental — accuracy not yet measuredTau forms strains, defined assembly conformations that propagate faithfully in vivo, creating unique transmissible pathologies.
“Tau also forms strains, which are defined assembly conformations that propagate faithfully in vivo, creating unique transmissible pathologies (Sanders et al., 2014; Kaufman et al., 2016).”
From Spontaneous pathology in PS19 tauopathy mice progresses via brain networks (2025) · cites this paper as Sanders et al., 2014
Seeded synthetic tau fibrils, or brain extracts from tau transgenic mice or human patients with tauopathy injected into the brain of tau transgenic or WT mice induce pathological tau spreading at sites distal to the injection site.
“seeded synthetic tau fibrils, or brain extracts from tau transgenic mice or human patients with tauopathy injected into the brain of tau transgenic or WT mice was found to induce pathological tau spreading at sites distal to the injection site [232–235].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [234]
Tau propagation-induced tau pathology is based on the spread of tau between neurons and the dissemination between neurons and glial cells.
“Furthermore, tau propagation-induced tau pathology is based on the spread of tau between neurons and the dissemination between neurons and glial cells [81, 82].”
From Tau and neuroinflammation in Alzheimer’s disease: interplay mechanisms and clinical translation (2023) · cites this paper as [81]
Previous reports show that on SDD-AGE, low-molecular-weight tau accumulates at the bottom of the gel and high-molecular-weight tau oligomers appear as smears at the top.
“Previous reports of HMW and LMW tau run on SDD-AGE show an accumulation of LMW tau at the bottom of the gel with smears of HMW tau oligomers at the top (7, 63–65).”
From Tau reduction prevents neuronal loss and reverses pathological tau deposition and seeding in mice with tauopathy (2017) · cites this paper as [63]
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Self-citation
- Authors
- Sanders, D. W., Kaufman, S. K., DeVos, S. L., Sharma, A. M., Mirbaha, H., Li, A., Barker, S. J., Foley, A. C., Thorpe, J. R., Serpell, L. C., Miller, T. M., Grinberg, L. T., Seeley, W. W., & Diamond, M. I.
- Affiliations
- Washington University in St. Louis (US)
- University of Sussex (GB)
- University of California, San Francisco (US)
- Corresponding author
- Diamond, Marc I.
- ORCID
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2014-06
- Volume
- 82
- Issue
- 6
- Pages
- 1271-1288
- ISSN
- 0896-6273 (ISSN-L)
- PMC
- PMC4171396
- OpenAlex
- W2081966615
- Cited by
- 986
- References
- 69
- Citations by year
- 2026: 44 · 2025: 70 · 2024: 47 · 2023: 73 · 2022: 68 · 2021: 107 · 2020: 107 · 2019: 94 · 2018: 101 · 2017: 96 · 2016: 94 · 2015: 56 · 2014: 26
- FWCI
- 60.28
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- eScholarship (California Digital Library) (submittedVersion)
- Sussex Research Online (University of Sussex) (submittedVersion)
- Figshare (submittedVersion, cc-by)
- Funders
- American Health Assistance Foundation
- Muscular Dystrophy Association
- Hope Center for Neurological Disorders
- National Institutes of Health
- Medical Research Council (MR/K022105/1)
- National Institute on Aging (F30AG048653, P01AG019724, P50AG023501)
- National Institute of General Medical Sciences (T32GM008151)
- National Institute of Neurological Disorders and Stroke (P30NS057105, F31NS086251, R01NS078398, R01NS071835)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- tauopathy, prion-like propagation, tau aggregation, amyloid conformation, tau repeat domain, transgenic mouse model, strain isolation, neurodegeneration
- MeSH terms
- Animals, Hippocampus, Humans, Mice, Transgenic, Prions, tau Proteins, Disease Progression, Neurodegenerative Diseases, Tauopathies, Mice, HEK293 Cells, Plaque, Amyloid
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
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