Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes

Nature

Volumn 541, Issue 7636, 2017, Pages 217-221

  Qiang, Wei ^a,c   Yau, Wai Ming ^a   Lu, Jun Xia ^a,d   Collinge, John ^b   Tycko, Robert ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b UNIVERSITY COLLEGE LONDON   (United Kingdom)

^c BINGHAMTON UNIVERSITY   (United States)

^d SHANGHAITECH UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN[1-40]; AMYLOID BETA PROTEIN[1-42]; AMYLOID; AMYLOID BETA PROTEIN; AMYLOID BETA-PROTEIN (1-42); PEPTIDE FRAGMENT;

BRAIN; EXPERIMENTAL STUDY; HETEROGENEITY; MENTAL HEALTH; NUCLEAR MAGNETIC RESONANCE; PEPTIDE; PHENOTYPE; POLYMER; POLYMORPHISM;

ADULT; AGED; ALZHEIMER DISEASE; ARTICLE; BRAIN CORTEX; BRAIN CORTEX ATROPHY; BRAIN TISSUE; CARBON NUCLEAR MAGNETIC RESONANCE; CLINICAL ARTICLE; CONTROLLED STUDY; DISEASE COURSE; DISEASE DURATION; FEMALE; HUMAN; HUMAN TISSUE; MALE; MIDDLE AGED; NITROGEN NUCLEAR MAGNETIC RESONANCE; ONSET AGE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN STRUCTURE; VERY ELDERLY; CHEMISTRY; CLASSIFICATION; METABOLISM; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PATHOLOGY; PHENOTYPE; PRINCIPAL COMPONENT ANALYSIS; ULTRASTRUCTURE;

AGED; AGED, 80 AND OVER; ALZHEIMER DISEASE; AMYLOID; AMYLOID BETA-PEPTIDES; CEREBRAL CORTEX; FEMALE; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MALE; MIDDLE AGED; PEPTIDE FRAGMENTS; PHENOTYPE; PRINCIPAL COMPONENT ANALYSIS;

EID: 85016148714     PISSN: 00280836     EISSN: 14764687     Source Type: Journal    
DOI: 10.1038/nature20814     Document Type: Article

References (30)

1. Petkova, A. T., et al. Self-propagating, molecular-level polymorphism in Alzheimer's-amyloid fibrils. Science 307, 262-265 (2005).
2. Paravastu, A. K., Leapman, R. D., Yau, W. M., Tycko, R. Molecular structural basis for polymorphism in Alzheimer's-amyloid fibrils. Proc. Natl Acad. Sci. USA 105, 18349-18354 (2008).
3. Paravastu, A. K., Qahwash, I., Leapman, R. D., Meredith, S. C., Tycko, R. Seeded growth of-amyloid fibrils from Alzheimer's brain-derived fibrils produces a distinct fibril structure. Proc. Natl Acad. Sci. USA 106, 7443-7448 (2009).
4. Lu, J. X., et al. Molecular structure of-amyloid fibrils in Alzheimer's disease brain tissue. Cell 154, 1257-1268 (2013).
5. Bertini, I., Gonnelli, L., Luchinat, C., Mao, J., Nesi, A. A new structural model of A 40 fibrils. J. Am. Chem. Soc. 133, 16013-16022 (2011).
6. Schutz, A. K., et al. Atomic-resolution three-dimensional structure of amyloid fibrils bearing the Osaka mutation. Angew. Chem. Int. Edn Engl. 54, 331-335 (2015).
7. Xiao, Y., et al. A (1-42) fibril structure illuminates self-recognition and replication of amyloid in Alzheimer's disease. Nat. Struct. Mol. Biol. 22, 499-505 (2015).
8. Sgourakis, N. G., Yau, W. M., Qiang, W. Modeling an in-register, parallel "Iowa" a fibril structure using solid-state NMR data from labeled samples with Rosetta. Structure 23, 216-227 (2015).
9. Goldsbury, C., Frey, P., Olivieri, V., Aebi, U., Müller, S. A. Multiple assembly pathways underlie amyloid-fibril polymorphisms. J. Mol. Biol. 352, 282-298 (2005).
10. Meinhardt, J., Sachse, C., Hortschansky, P., Grigorieff, N., Fändrich, M. A (1-40) fibril polymorphism implies diverse interaction patterns in amyloid fibrils. J. Mol. Biol. 386, 869-877 (2009).
11. Zhang, R., et al. Interprotofilament interactions between Alzheimer's A 1-42 peptides in amyloid fibrils revealed by cryoEM. Proc. Natl Acad. Sci. USA 106, 4653-4658 (2009).
12. Kodali, R., Williams, A. D., Chemuru, S., Wetzel, R. A (1-40) forms five distinct amyloid structures whose-sheet contents and fibril stabilities are correlated. J. Mol. Biol. 401, 503-517 (2010).
13. Meyer-Luehmann, M., et al. Exogenous induction of cerebral-amyloidogenesis is governed by agent and host. Science 313, 1781-1784 (2006).
14. Langer, F., et al. Soluble A seeds are potent inducers of cerebral-amyloid deposition. J. Neurosci. 31, 14488-14495 (2011).
15. Stöhr, J., et al. Distinct synthetic A prion strains producing different amyloid deposits in bigenic mice. Proc. Natl Acad. Sci. USA 111, 10329-10334 (2014).
16. Cohen, M. L., et al. Rapidly progressive Alzheimer's disease features distinct structures of amyloid-. Brain 138, 1009-1022 (2015).
17. Bessen, R. A., Marsh, R. F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68, 7859-7868 (1994).
18. Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J., Hill, A. F. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 383, 685-690 (1996).
19. Safar, J., et al. Eight prion strains have PrPSc molecules with different conformations. Nat. Med. 4, 1157-1165 (1998).
20. Gath, J., et al. Unlike twins: an NMR comparison of two-synuclein polymorphs featuring different toxicity. PLoS One 9, e90659 (2014).
21. van der Wel, P. C. A., Lewandowski, J. R., Griffin, R. G. Solid-state NMR study of amyloid nanocrystals and fibrils formed by the peptide GNNQQNY from yeast prion protein Sup35p. J. Am. Chem. Soc. 129, 5117-5130 (2007).
22. Collinge, J., Clarke, A. R. A general model of prion strains and their pathogenicity. Science 318, 930-936 (2007).
23. Tang-Wai, D. F., et al. Clinical, genetic, neuropathologic characteristics of posterior cortical atrophy. Neurology 63, 1168-1174 (2004).
24. Schmidt, C., et al. Rapidly progressive Alzheimer's disease: a multicenter update. J. Alzheimers Dis. 30, 751-756 (2012).
25. Henry, E. R., Hofrichter, J. Singular value decomposition: application to analysis of experimental data. Methods Enzymol. 210, 129-192 (1992).
26. Qiang, W., Yau, W. M., Luo, Y., Mattson, M. P., Tycko, R. Antiparallel-sheet architecture in Iowa-mutant-amyloid fibrils. Proc. Natl Acad. Sci. USA 109, 4443-4448 (2012).
27. Colvin, M. T., et al. Atomic resolution structure of monomorphic A 42 amyloid fibrils. J. Am. Chem. Soc. 138, 9663-9674 (2016).
28. Wälti, M. A., et al. Atomic-resolution structure of a disease-relevant A (1-42) amyloid fibril. Proc. Natl Acad. Sci. USA 113, E4976-E4984 (2016).
29. Guo, J. L., et al. Distinct-synuclein strains differentially promote tau inclusions in neurons. Cell 154, 103-117 (2013).
30. Sanders, D. W., et al. Distinct tau prion strains propagate in cells and mice and define different tauopathies. Neuron 82, 1271-1288 (2014)