Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

Tuttle, Marcus D.; Comellas, Gemma; Nieuwkoop, Andrew J.; Covell, Dustin J.; Berthold, Deborah A.; Kloepper, Kathryn D.; Courtney, Joseph M.; Kim, Jae K.; Barclay, Alexander M.; Kendall, Amy; Wan, William; Stubbs, Gerald; Schwieters, Charles D.; Lee, Virginia M. Y.; George, Julia M.; Rienstra, Chad M.

doi:10.1038/nsmb.3194

Title: Solid-state NMR structure of a pathogenic fibril of full-length human α-synuclein

Journal Article · Mon Mar 28 00:00:00 EDT 2016 · Nature Structural & Molecular Biology

DOI:https://doi.org/10.1038/nsmb.3194· OSTI ID:1467083

Tuttle, Marcus D. ^[1]; Comellas, Gemma ^[2]; Nieuwkoop, Andrew J. ^[1]; Covell, Dustin J. ^[3]; Berthold, Deborah A. ^[1]; Kloepper, Kathryn D. ^[1]; Courtney, Joseph M. ^[1]; Kim, Jae K. ^[1]; Barclay, Alexander M. ^[2]; Kendall, Amy ^[4]; Wan, William ^[4]; Stubbs, Gerald ^[4]; Schwieters, Charles D. ^[5]; Lee, Virginia M. Y. ^[3]; George, Julia M. ^[6]; Rienstra, Chad M. ^[7]

Univ. of Illinois, Urbana, IL (United States). Dept. of Chemistry
Univ. of Illinois, Urbana, IL (United States). Center for Biophysics and Quantitative Biology
Univ. of Pennsylvania, Philadelphia, PA (United States). School of Medicine. Dept. of Pathology and Lab. Medicine. Inst. on Aging. Center for Neurodegenerative Disease Research
Vanderbilt Univ., Nashville, TN (United States). Dept. of Biological Sciences. Center for Structural Biology
National Inst. of Health (NIH), Bethesda, MD (United States). Division of Computational Bioscience. Center for Information Technology
Queen Mary Univ. of London (United Kingdom). Dept. of Biological and Experimental Psychology. School of Biological and Chemical Sciences
Univ. of Illinois, Urbana, IL (United States). Dept. of Chemistry. Center for Biophysics and Quantitative Biology. Dept. of Biochemistry

Misfolded α-synuclein amyloid fibrils are the principal components of Lewy bodies and neurites, hallmarks of Parkinson's disease (PD). In this paper, we present a high-resolution structure of an α-synuclein fibril, in a form that induces robust pathology in primary neuronal culture, determined by solid-state NMR spectroscopy and validated by EM and X-ray fiber diffraction. Over 200 unique long-range distance restraints define a consensus structure with common amyloid features including parallel, in-register β-sheets and hydrophobic-core residues, and with substantial complexity arising from diverse structural features including an intermolecular salt bridge, a glutamine ladder, close backbone interactions involving small residues, and several steric zippers stabilizing a new orthogonal Greek-key topology. These characteristics contribute to the robust propagation of this fibril form, as supported by the structural similarity of early-onset-PD mutants. Finally, the structure provides a framework for understanding the interactions of α-synuclein with other proteins and small molecules, to aid in PD diagnosis and treatment.

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Research Organization:: Univ. of Illinois at Urbana-Champaign, IL (United States); Univ. of Pennsylvania, Philadelphia, PA (United States); Vanderbilt Univ., Nashville, TN (United States); National Institutes of Health (NIH), Bethesda, MD (United States)

Sponsoring Organization:: USDOE Office of Science (SC), Biological and Environmental Research (BER); USDOE Office of Science (SC), Basic Energy Sciences (BES); National Inst. of Health (NIH) (United States); National Science Foundation (NSF)

Grant/Contract Number:: FG02-07ER46453; FG02-07ER46471; R01-GM073770; P50-NS053488; P01-AG002132; S10-RR025037; T32-GM008276; T32-AG000255; P41-EB2181; S10-RR011966

OSTI ID:: 1467083

Journal Information:: Nature Structural & Molecular Biology, Vol. 23, Issue 5; ISSN 1545-9993

Publisher:: Nature Publishing GroupCopyright Statement

Country of Publication:: United States

Language:: English

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Cited by: 658 works

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Identification of N-linked glycans as specific mediators of neuronal uptake of acetylated α-Synuclein Birol, Melissa; Wojcik, Slawomir P.; Miranker, Andrew D. PLOS Biology, Vol. 17, Issue 6 https://doi.org/10.1371/journal.pbio.3000318	journal	June 2019
Living in Promiscuity: The Multiple Partners of Alpha-Synuclein at the Synapse in Physiology and Pathology. Longhena, Francesca; Faustini, Gaia; Spillantini, Maria Apollo - University of Cambridge Repository https://doi.org/10.17863/cam.37879	text	January 2019
Mechanical and thermodynamic properties of Aβ ₄₂ , Aβ ₄₀ , and α-synuclein fibrils: a coarse-grained method to complement experimental studies Poma, Adolfo B.; Guzman, Horacio V.; Li, Mai Suan Beilstein Journal of Nanotechnology, Vol. 10 https://doi.org/10.3762/bjnano.10.51	journal	January 2019
Graphene quantum dots prevent alpha-synucleinopathy in Parkinson's disease Kim, Donghoon; Yoo, Je Min; Hwang, Heehong arXiv https://doi.org/10.48550/arxiv.1710.07213	text	January 2017
Mapping of Surface-Exposed Epitopes of In Vitro and In Vivo Aggregated Species of Alpha-Synuclein Almandoz-Gil, Leire; Lindström, Veronica; Sigvardson, Jessica Cellular and Molecular Neurobiology, Vol. 37, Issue 7 https://doi.org/10.1007/s10571-016-0454-0	journal	December 2016
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Cryo-EM structure of an amyloid fibril from systemic amyloidosis Liberta, Falk; Loerch, Sarah; Rennegarbe, Matthies Nature Communications https://doi.org/10.1101/357129	journal	June 2018
Exploiting Heterogeneous Time Scale of Dynamics to Enhance 2D HETCOR Solid-State NMR Sensitivity Zhang, Rongchun; Nishiyama, Yusuke; Ramamoorthy, Ayyalusamy Journal of Magnetic Resonance https://doi.org/10.1101/691220	journal	July 2019
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A scalable approach to the computation of invariant measures for high-dimensional Markovian systems Gerber, Susanne; Olsson, Simon; Noé, Frank Macmillan Publishers Limited, part of Springer Nature https://doi.org/10.25358/openscience-566	text	January 2018
Exploring the Structural Diversity in Inhibitors of α-Synuclein Amyloidogenic Folding, Aggregation, and Neurotoxicity Das, Sukanya; Pukala, Tara L.; Smid, Scott D. Frontiers in Chemistry, Vol. 6 https://doi.org/10.3389/fchem.2018.00181	journal	May 2018
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Different Heat Shock Proteins Bind α-Synuclein With Distinct Mechanisms and Synergistically Prevent Its Amyloid Aggregation Jia, Chunyu; Ma, Xiaojuan; Liu, Zhenying Frontiers in Neuroscience, Vol. 13 https://doi.org/10.3389/fnins.2019.01124	journal	November 2019
Structure-Based Peptide Inhibitor Design of Amyloid-β Aggregation Lu, Jinxia; Cao, Qin; Wang, Chuchu Frontiers in Molecular Neuroscience, Vol. 12 https://doi.org/10.3389/fnmol.2019.00054	journal	March 2019
Effects of the Toxic Metals Arsenite and Cadmium on α-Synuclein Aggregation In Vitro and in Cells Lorentzon, Emma; Horvath, Istvan; Kumar, Ranjeet International Journal of Molecular Sciences, Vol. 22, Issue 21 https://doi.org/10.3390/ijms222111455	journal	October 2021
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