Seeding selectivity and ultrasensitive detection of tau aggregate conformers of Alzheimer disease
Open accessAbstract
Alzheimer disease (AD) and chronic traumatic encephalopathy (CTE) involve the abnormal accumulation in the brain of filaments composed of both three-repeat (3R) and four-repeat (4R) (3R/4R) tau isoforms. To probe the molecular basis for AD’s tau filament propagation and to improve detection of tau aggregates as potential biomarkers, we have exploited the seeded polymerization growth mechanism of tau filaments to develop a highly selective and ultrasensitive cell-free tau seed amplification assay optimized for AD (AD real-time quaking-induced conversion or AD RT-QuIC). The reaction is based on the ability of AD tau aggregates to seed the formation of amyloid fibrils made of certain recombinant tau fragments. AD RT-QuIC detected seeding activity in AD ( n = 16) brains at dilutions as extreme as 10 7 –10 10 -fold, but was 10 2 –10 6 -fold less responsive when seeded with brain from most cases of other types of tauopathy with comparable loads of predominant 3R or 4R tau aggregates. For example, AD brains had average seeding activities that were orders of magnitude higher than Pick disease brains with predominant 3R tau deposits, but the opposite was true using our previously described Pick-optimized tau RT-QuIC assay. CTE brains ( n = 2) had seed concentrations comparable to the weakest of the AD specimens, and higher than 3 of 4 specimens with 3R/4R primary age-related tauopathy. AD seeds shared properties with the tau filaments found in AD brains, as AD seeds were sarkosyl-insoluble, protease resistant, and reactive with tau antibodies. Moreover, AD RT-QuIC detected as little as 16 fg of pure synthetic tau fibrils. The distinctive seeding activity exhibited by AD and CTE tau filaments compared to other types of tauopathies in these seeded polymerization reactions provides a mechanistic basis for their consistent propagation as specific conformers in patients with 3R/4R tau diseases. Importantly, AD RT-QuIC also provides rapid ultrasensitive quantitation of 3R/4R tau-seeding activity as a biomarker.
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Seeding activity has been shown to identify the action of high molecular weight tau and to differentiate between specific conformers in 3R/4R tau diseases.
“As a pathological readout, seeding activity has been shown to identify the action of high molecular weight tau (Martinez et al., 2022) and even differentiate between specific conformers in 3R/4R tau diseases (Kraus et al., 2019).”
From Network analysis identifies strain-dependent response to tau and tau seeding-associated genes (2023) · cites this paper as Kraus et al., 2019
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Severe oligomeric tau toxicity can be reversed without long-term sequelae
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Defining the Protein Seeds of Neurodegeneration using Real-Time Quaking-Induced Conversion Assays
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- Authors
- Kraus, A., Saijo, E., Metrick, M. A., Newell, K., Sigurdson, C. J., Zanusso, G., Ghetti, B., & Caughey, B.
- Affiliations
- Rocky Mountain Laboratories (US)
- University of Kansas (US)
- University of California San Diego (US)
- University of Verona (IT)
- Indiana University School of Medicine (US)
- Corresponding author
- Caughey, Byron
- ORCID
- Venue
- Acta Neuropathologica
- Published
- 2018-12-20
- Volume
- 137
- Issue
- 4
- Pages
- 585-598
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- PMC
- PMC6426988
- OpenAlex
- W2906247002
- Cited by
- 143
- References
- 48
- Citations by year
- 2026: 15 · 2025: 25 · 2024: 17 · 2023: 18 · 2022: 20 · 2021: 17 · 2020: 17 · 2019: 14
- FWCI
- 8.25
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Acta Neuropathologica (publishedVersion, cc-by)
- Europe PMC (PubMed Central) (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- National Institute of Allergy and Infectious Diseases (ZIA AI001086-08)
- The CJD Foundation (none)
- National Institute on Aging (PHS P30-AG010133, P30- AG035982, P50 AG005131, P30 AG19610)
- Japan Society for the Promotion of Science (Fellowship for Japanese Biochemical, Behavioral Researchers at NIH)
- National Institute of Neurological Disorders and Stroke (none)
- National Institute of Mental Health (none)
- National Multiple Sclerosis Society (none)
- U.S. Department of Veterans Affairs (none)
- Arizona Biomedical Research Commission (4001, 0011, 05-901, 1001)
- Michael J. Fox Foundation for Parkinson's Research (none)
- Massachusetts Alzheimer's Disease Research Center (P50 AG005134)
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Psychiatry and Mental health › Dementia and Cognitive Impairment Research
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Prion Diseases and Protein Misfolding
- Keywords
- Alzheimer's disease, tau aggregates, RT-QuIC, tauopathy, chronic traumatic encephalopathy, Pick's disease, primary age-related tauopathy, ultrasensitive detection, biomarkers, sarkosyl-insoluble tau, protease resistance
- MeSH terms
- Alzheimer Disease, Animals, Brain, Humans, tau Proteins, Mice, Knockout, Tauopathies, Mice, Protein Aggregates
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