Amyloid-β nanotubes are associated with prion protein-dependent synaptotoxicity
Open accessAbstract
Growing evidence suggests water-soluble, non-fibrillar forms of amyloid-β protein (Aβ) have important roles in Alzheimer’s disease with toxicities mimicked by synthetic Aβ1–42. However, no defined toxic structures acting via specific receptors have been identified and roles of proposed receptors, such as prion protein (PrP), remain controversial. Here we quantify binding to PrP of Aβ1–42 after different durations of aggregation. We show PrP-binding and PrP-dependent inhibition of long-term potentiation (LTP) correlate with the presence of protofibrils. Globular oligomers bind less avidly to PrP and do not inhibit LTP, whereas fibrils inhibit LTP in a PrP-independent manner. That only certain transient Aβ assemblies cause PrP-dependent toxicity explains conflicting reports regarding the involvement of PrP in Aβ-induced impairments. We show that these protofibrils contain a defined nanotubular structure with a previously unidentified triple helical conformation. Blocking the formation of Aβ nanotubes or their interaction with PrP might have a role in treatment of Alzheimer’s disease. Prion protein has been suggested to bind toxic amyloid-ß oligomers. Nicollet al.demonstrate that binding to prion protein and prion protein-dependent synaptotoxicity correlate with the presence of a tubular form of amyloid-ß with a defined triple helical structure.
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Antibodies targeting various regions in PrPC abolish LTP impairment triggered by exposure to human AD brain extracts.
“Antibodies targeting various regions in PrPC abolish LTP impairment triggered by exposure to human AD brain extracts [90], and peripheral injection of these antibodies displays protective effects in AD mouse models [91].”
From Molecular and cellular mechanisms underlying the pathogenesis of Alzheimer’s disease (2020) · cites this paper as [90]
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Sleep is bi-directionally modified by amyloid beta oligomersPreprint
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- Authors
- Nicoll, A. J., Panico, S., Freir, D. B., Wright, D., Terry, C., Risse, E., Herron, C. E., O’Malley, T., Wadsworth, J. D. F., Farrow, M. A., Walsh, D. M., Saibil, H. R., & Collinge, J.
- Affiliations
- MRC Prion Unit (GB)
- Institute of Structural and Molecular Biology (GB)
- University College Dublin (IE)
- Brigham and Women's Hospital (US)
- Corresponding author
- Saibil, Helen R.
- Collinge, John
- ORCID
- Venue
- Nature Communications
- Published
- 2013-09-11
- Volume
- 4
- Issue
- 1
- Pages
- 2416-2416
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC3908552
- OpenAlex
- W2171300315
- Cited by
- 119
- References
- 52
- Citations by year
- 2026: 2 · 2025: 2 · 2024: 5 · 2023: 4 · 2022: 9 · 2021: 8 · 2020: 10 · 2019: 7 · 2018: 12 · 2017: 14 · 2016: 13 · 2015: 17 · 2014: 14 · 2013: 2
- FWCI
- 10.65
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Nature Communications (publishedVersion, cc-by-nc-nd)
- Europe PMC (PubMed Central) (publishedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Digital Access to Scholarship at Harvard (DASH) (Harvard University) (submittedVersion, cc-by)
- Arrow@dit (Dublin Institute of Technology) (submittedVersion, cc-by-nc-nd)
- RePEc: Research Papers in Economics (submittedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Research Repository UCD (University College Dublin) (submittedVersion, cc-by-nc-nd)
- Funders
- Foundation for Neurologic Diseases
- Wellcome Trust
- Medical Research Council
- 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
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- amyloid-beta, prion protein, synaptotoxicity, protofibrils, triple-helical conformation, long-term potentiation, Alzheimer's disease, amyloid-beta aggregation, oligomers, fibrils, receptor binding
- MeSH terms
- Animals, Humans, Male, Mice, Inbred C57BL, Prions, Protein Binding, Synapses, Time Factors, Tomography, Amyloid beta-Peptides, Protein Structure, Secondary, Long-Term Potentiation, Protein Structure, Quaternary, Nanotubes, Mice
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