The structure of fibrils from 'misfolded' proteins

Current Opinion in Structural Biology

Volumn 30, Issue , 2015, Pages 43-49

  Meier, Beat H ^a   Böckmann, Anja ^b  

^a ETH ZURICH   (Switzerland)

^b UNIVERSITÉ DE LYON   (France)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA SYNUCLEIN; AMYLOID BETA PROTEIN; MONOMER; PRION PROTEIN; PROTEIN; PROTEIN FIBRIL; UNCLASSIFIED DRUG; AMYLOID; PRION;

NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN POLYMORPHISM; PROTEIN SECONDARY STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE; REVIEW; SOLID STATE; SOLID STATE NUCLEAR MAGNETIC RESONANCE; STRUCTURE ANALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; PRION; PROCEDURES; PROTEIN FOLDING;

ALPHA-SYNUCLEIN; AMYLOID; MODELS, MOLECULAR; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PRIONS; PROTEIN FOLDING;

EID: 84919772780     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2014.12.001     Document Type: Review

References (40)

1. Dong S., Duan Y., Hu Y., Zhao Z. Advances in the pathogenesis of Alzheimer's disease: a re-evaluation of amyloid cascade hypothesis. Transl Neurodegener 2012, 1:18.
2. Fowler D.M., Koulov A.V., Alory-Jost C., Marks M.S., Balch W.E., Kelly J.W. Functional amyloid formation within mammalian tissue. PLoS Biol 2006, 4:e6.
3. Maji S.K., Perrin M.H., Sawaya M.R., Jessberger S., Vadodaria K., Rissman R.A., Singru P.S., Nilsson K.P.R., Simon R., Schubert D., et al. Functional amyloids as natural storage of peptide hormones in pituitary secretory granules. Science 2009, 325:328-332.
4. Prusiner S.B. Cell biology. A unifying role for prions in neurodegenerative diseases. Science 2012, 336:1511-1513.
5. Winner B., Jappelli R., Maji S.K., Desplats P.A., Boyer L., Aigner S., Hetzer C., Loher T., Vilar M., Campioni S., et al. In vivo demonstration that alpha-synuclein oligomers are toxic. Proc Natl Acad Sci 2011, 108:4194-4199.
6. Aguzzi A., Rajendran L. The transcellular spread of cytosolic amyloids, prions, and prionoids. Neuron 2009, 64:783-790.
7. Freundt E.C., Maynard N., Clancy E.K., Roy S., Bousset L., Sourigues Y., Covert M., Melki R., Kirkegaard K., Brahic M. Neuron-to-neuron transmission of α-synuclein fibrils through axonal transport. Ann Neurol 2012, 72:517-524.
8. Pieri L., Madiona K., Bousset L., Melki R. Fibrillar α-synuclein and huntingtin exon 1 assemblies are toxic to the cells. Biophys J 2012, 102:2894-2905.
9. Bousset L., Pieri L., Ruiz-Arlandis G., Gath J., Jensen P.H., Habenstein B., Madiona K., Olieric V., Böckmann A., Meier B.H., et al. Structural and functional characterization of two alpha-synuclein strains. Nat Commun 2013, 4:2575.
10. Goldsbury C., Baxa U., Simon M.N., Steven A.C., Engel A., Wall J.S., Aebi U., Müller S.A. Amyloid structure and assembly: insights from scanning transmission electron microscopy. J Struct Biol 2011, 173:1-13.
11. Wishart D.S., Sykes B.D. The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 1994, 4:171-180.
12. Huber M., Ovchinnikova O.Y., Schütz A.K., Glockshuber R., Meier B.H., Böckmann A. Solid-state NMR sequential assignment of Osaka-mutant amyloid-beta (Aβ1-40 E22δ) fibrils. Biomol NMR Assign 2014, 10.1007/s12104-013-9535-9540.
13. Petkova A.T., Leapman R.D., Guo Z., Yau W.-M., Mattson M.P., Tycko R. Self-propagating, molecular-level polymorphism in Alzheimer's beta-amyloid fibrils. Science 2005, 307:262-265.
14. Paravastu A.K., Petkova A.T., Tycko R. Polymorphic fibril formation by residues 10-40 of the Alzheimer's β-amyloid peptide. Biophys J 2006, 90:4618-4629.
15. Heise H., Hoyer W., Becker S., Andronesi O.C., Riedel D., Baldus M. Molecular-level secondary structure, polymorphism, and dynamics of full-length alpha-synuclein fibrils studied by solid-state NMR. Proc Natl Acad Sci USA 2005, 102:15871-15876.
16. 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 2007, 129:5117-5130.
17. Gath J., Bousset L., Habenstein B., Melki R., Böckmann A., Meier B.H. Unlike twins: an NMR comparison of two α-synuclein polymorphs featuring different toxicity. PLoS ONE 2014, 9:e90659.
18. Habenstein B., Bousset L., Sourigues Y., Kabani M., Loquet A., Meier B.H., Melki R., Böckmann A. A native-like conformation for the C-terminal domain of the prion Ure2p within its fibrillar form. Angew Chem Int Ed 2012, 51:7963-7966.
19. Habenstein B., Wasmer C., Bousset L., Sourigues Y., Schütz A., Loquet A., Meier B.H., Melki R., Böckmann A. Extensive de novo solid-state NMR assignments of the 33kDa C-terminal domain of the Ure2 prion. J Biomol NMR 2011, 51:235-243.
20. Gath J., Bousset L., Habenstein B., Melki R., Meier B.H., Böckmann A. Yet another polymorph of α-synuclein: solid-state sequential assignments. Biomol NMR Assign 2014, 8:395-404.
21. Gath J., Habenstein B., Bousset L., Melki R., Meier B.H., Böckmann A. Solid-state NMR sequential assignments of α-synuclein. Biomol NMR Assign 2012, 6:51-55.
22. Comellas G., Lemkau L.R., Nieuwkoop A.J., Kloepper K.D., Ladror D.T., Ebisu R., Woods W.S., Lipton A.S., George J.M., Rienstra C.M. Structured regions of α-synuclein fibrils include the early-onset Parkinson's disease mutation sites. J Mol Biol 2011, 411:881-895.
23. Lv G., Kumar A., Giller K., Orcellet M.L., Riedel D., Fernandez C.O., Becker S., Lange A. Structural comparison of mouse and human α-synuclein amyloid fibrils by solid-state NMR. J Mol Biol 2012, 420:99-111.
24. Schütz A.K., Habenstein B., Luckgei N., Bousset L., Sourigues Y., Nielsen A.B., Melki R., Böckmann A., Meier B.H. Solid-state NMR sequential assignments of the amyloid core of full-length Sup35p. Biomol NMR Assign 2014, 8:349-356.
25. Luckgei N., Schütz A.K., Habenstein B., Bousset L., Sourigues Y., Melki R., Meier B.H., Böckmann A. Solid-state NMR sequential assignments of the amyloid core of Sup35pNM. Biomol NMR Assign 2014, 8:365-370.
26. Luckgei N., Schütz A.K., Bousset L., Habenstein B., Sourigues Y., Gardiennet C., Meier B.H., Melki R., Böckmann A. The conformation of the prion domain of Sup35p in isolation and in the full-length protein. Angew Chem Int Ed Engl 2013, 52:12741-12744.
27. Van Melckebeke H., Wasmer C., Lange A., Ab E., Loquet A., Böckmann A., Meier B.H. Atomic-resolution three-dimensional structure of HET-s(218-289) amyloid fibrils by solid-state NMR spectroscopy. J Am Chem Soc 2010, 132:13765-13775.
28. Wasmer C., Schütz A., Loquet A., Buhtz C., Greenwald J., Riek R., Böckmann A., Meier B.H. The molecular organization of the fungal prion HET-s in its amyloid form. J Mol Biol 2009, 394:119-127.
29. Loquet A., Bousset L., Gardiennet C., Sourigues Y., Wasmer C., Habenstein B., Schütz A., Meier B.H., Melki R., Böckmann A. Prion fibrils of Ure2p assembled under physiological conditions contain highly ordered, natively folded modules. J Mol Biol 2009, 394:108-118.
30. Böckmann A., Meier B.H. Prions: en route from structural models to structures. Prion 2010, 4:72-79.
31. Wasmer C., Lange A., Van Melckebeke H., Siemer A.B., Riek R., Meier B.H. Amyloid fibrils of the HET-s(218-289) prion form a solenoid with a triangular hydrophobic core. Science 2008, 319:1523-1526.
32. Seuring C., Greenwald J., Wasmer C., Wepf R., Saupe S.J., Meier B.H., Riek R. The mechanism of toxicity in HET-S/HET-s prion incompatibility. PLoS Biol 2012, 10:e1001451.
33. Spencer R.G., Halverson K.J., Auger M., McDermott A.E., Griffin R.G., Lansbury P.T. An unusual peptide conformation may precipitate amyloid formation in Alzheimer's disease: application of solid-state NMR to the determination of protein secondary structure. Biochemistry 1991, 30:10382-10387.
34. Lansbury P.T., Costa P.R., Griffiths J.M., Simon E.J., Auger M., Halverson K.J., Kocisko D.A., Hendsch Z.S., Ashburn T.T., Spencer R.G. Structural model for the beta-amyloid fibril based on interstrand alignment of an antiparallel-sheet comprising a C-terminal peptide. Nat Struct Biol 1995, 2:990-998.
35. Ovchinnikova O.Y., Finder V.H., Vodopivec I., Nitsch R.M., Glockshuber R. The Osaka FAD mutation E22δ leads to the formation of a previously unknown type of amyloid β fibrils and modulates Aβ neurotoxicity. J Mol Biol 2011, 408:780-791.
36. Niu Z., Zhao W., Zhang Z., Xiao F., Tang X., Yang J. The molecular structure of Alzheimer β-amyloid fibrils formed in the presence of phospholipid vesicles. Angew Chem Int Ed Engl 2014, 10.1002/anie.201311106.
37. Bertini I., Gonnelli L., Luchinat C., Mao J., Nesi A. A new structural model of Aβ40 fibrils. J Am Chem Soc 2011, 133:16013-16022.
38. Lu J.-X., Qiang W., Yau W.-M., Schwieters C.D., Meredith S.C., Tycko R. Molecular structure of b-amyloid fibrils in Alzheimer's disease brain tissue. Cell 2013, 154:1257-1268.
39. Schütz A.K., Vagt T., Huber M., Ovchinnikova O.Y., Cadalbert R., Wall J.S., Guntert P., Böckmann A., Glockshuber R., Meier B.H. Atomic-resolution 3D structure of amyloid β fibrils bearing the Osaka mutation. Angew Chem Int Ed 2014, (Epub ahead of print). 10.1002/anie.201408598.
40. Benilova I., Karran E., De Strooper B. The toxic Aβ oligomer and Alzheimer's disease: an emperor in need of clothes. Nat Neurosci 2012, 15:349-357.