Cited by 224Alzheimer's disease research and treatmentsPrion Diseases and Protein MisfoldingProtein Structure and Dynamics

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Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change

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Frost, Bess, Ollesch, Julian, Wille, Holger, Diamond, Marc I.·2009·Journal of Biological Chemistry

DOI 10.1074/jbc.m805627200PMC PMC2635036

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Abstract

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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Authors: Frost, B., Ollesch, J., Wille, H., & Diamond, M. I.
Affiliations: University of California, San Francisco (US)
Corresponding author: Diamond, Marc I.
ORCID: Frost, Bess
Wille, Holger
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)
DOI: 10.1074/jbc.m805627200
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: cc-by
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
creativecommons.org/licenses/by/4.0/ (vor, 4263 d)
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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Conformational Diversity of Wild-type Tau Fibrils Specified by Templated Conformation Change

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