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Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change
Open accessAbstract
Tauopathies are sporadic and genetic neurodegenerative diseases characterized by aggregation of the microtubule-associated protein Tau. Tau pathology occurs in over 20 phenotypically distinct neurodegenerative diseases, including Alzheimer disease and frontotemporal dementia. The molecular basis of this diversity among sporadic tauopathies is unknown, but distinct fibrillar wild-type (WT) Tau conformations could play a role. Using Fourier transform infrared spectroscopy, circular dichroism, and electron microscopy, we show that WT Tau fibrils and P301L/V337M Tau fibrils have distinct secondary structures, fragilities, and morphologies. Furthermore, P301L/V337M fibrillar seeds induce WT Tau monomer to form a novel fibrillar conformation, termed WT*, that is maintained over multiple seeding reactions. WT* has secondary structure, fragility, and morphology that are similar to P301L/V337M fibrils and distinct from WT fibrils. WT Tau is thus capable of conformational diversity that arises via templated conformation change, as has been described for amyloid beta, beta2-microglobulin, and prion proteins.
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“Exogenously supplied fibrils will seed aggregation of transgenic human and endogenous mouse tau fibrils in mouse tauopathy models by enhancing nucleation of new fibrils. These aggregates then spread transsynaptically to remote anatomically connected brain regions inducing further seeding and aggregation”
From Alzheimer Disease: An Update on Pathobiology and Treatment Strategies (2019) · cites this paper as Frost et al., 2009
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Metadata
- Authors
- Frost, B., Ollesch, J., Wille, H., & Diamond, M. I.
- Affiliations
- University of California, San Francisco (US)
- Corresponding author
- Diamond, Marc I.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-02
- Volume
- 284
- Issue
- 6
- Pages
- 3546-3551
- ISSN
- 0021-9258 (ISSN-L)
- PMC
- PMC2635036
- OpenAlex
- W1987549963
- Cited by
- 224
- References
- 25
- Citations by year
- 2026: 3 · 2025: 6 · 2024: 5 · 2023: 14 · 2022: 14 · 2021: 10 · 2020: 11 · 2019: 17 · 2018: 16 · 2017: 13 · 2016: 15 · 2015: 10 · 2014: 12 · 2013: 18 · 2012: 20
- FWCI
- 9.03
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institute of Neurological Disorders and Stroke (R01NS050284, R01 NS50284-03)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Keywords
- tau protein, tau fibrils, conformational heterogeneity, tauopathy, Alzheimer's disease, frontotemporal dementia, fibril morphology, protein aggregation
- MeSH terms
- Alzheimer Disease, Circular Dichroism, Humans, tau Proteins, Protein Structure, Secondary, Spectroscopy, Fourier Transform Infrared, Amino Acid Substitution, Mutation, Missense, Protein Structure, Quaternary
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