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AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils

Author

Listed:
  • Akanksha Bansal

    (Ulm University)

  • Matthias Schmidt

    (Ulm University)

  • Matthies Rennegarbe

    (Ulm University)

  • Christian Haupt

    (Ulm University)

  • Falk Liberta

    (Ulm University)

  • Sabrina Stecher

    (Ulm University)

  • Ioana Puscalau-Girtu

    (Ulm University)

  • Alexander Biedermann

    (Ulm University)

  • Marcus Fändrich

    (Ulm University)

Abstract

Systemic AA amyloidosis is a world-wide occurring protein misfolding disease of humans and animals. It arises from the formation of amyloid fibrils from serum amyloid A (SAA) protein. Using cryo electron microscopy we here show that amyloid fibrils which were purified from AA amyloidotic mice are structurally different from fibrils formed from recombinant SAA protein in vitro. Ex vivo amyloid fibrils consist of fibril proteins that contain more residues within their ordered parts and possess a higher β-sheet content than in vitro fibril proteins. They are also more resistant to proteolysis than their in vitro formed counterparts. These data suggest that pathogenic amyloid fibrils may originate from proteolytic selection, allowing specific fibril morphologies to proliferate and to cause damage to the surrounding tissue.

Suggested Citation

  • Akanksha Bansal & Matthias Schmidt & Matthies Rennegarbe & Christian Haupt & Falk Liberta & Sabrina Stecher & Ioana Puscalau-Girtu & Alexander Biedermann & Marcus Fändrich, 2021. "AA amyloid fibrils from diseased tissue are structurally different from in vitro formed SAA fibrils," Nature Communications, Nature, vol. 12(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-21129-z
    DOI: 10.1038/s41467-021-21129-z
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    Cited by:

    1. Kartikay Sharma & Fabian Stockert & Jayakrishna Shenoy & Mélanie Berbon & Muhammed Bilal Abdul-Shukkoor & Birgit Habenstein & Antoine Loquet & Matthias Schmidt & Marcus Fändrich, 2024. "Cryo-EM observation of the amyloid key structure of polymorphic TDP-43 amyloid fibrils," Nature Communications, Nature, vol. 15(1), pages 1-8, December.
    2. Sara Karimi-Farsijani & Kartikay Sharma & Marijana Ugrina & Lukas Kuhn & Peter Benedikt Pfeiffer & Christian Haupt & Sebastian Wiese & Ute Hegenbart & Stefan O. Schönland & Nadine Schwierz & Matthias , 2024. "Cryo-EM structure of a lysozyme-derived amyloid fibril from hereditary amyloidosis," Nature Communications, Nature, vol. 15(1), pages 1-9, December.
    3. Thomas Heerde & Desiree Schütz & Yu-Jie Lin & Jan Münch & Matthias Schmidt & Marcus Fändrich, 2023. "Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    4. Martin Wilkinson & Rodrigo U. Gallardo & Roberto Maya Martinez & Nicolas Guthertz & Masatomo So & Liam D. Aubrey & Sheena E. Radford & Neil A. Ranson, 2023. "Disease-relevant β2-microglobulin variants share a common amyloid fold," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    5. Tim Schulte & Antonio Chaves-Sanjuan & Giulia Mazzini & Valentina Speranzini & Francesca Lavatelli & Filippo Ferri & Carlo Palizzotto & Maria Mazza & Paolo Milani & Mario Nuvolone & Anne-Cathrine Vogt, 2022. "Cryo-EM structure of ex vivo fibrils associated with extreme AA amyloidosis prevalence in a cat shelter," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    6. Lynn Radamaker & Sara Karimi-Farsijani & Giada Andreotti & Julian Baur & Matthias Neumann & Sarah Schreiner & Natalie Berghaus & Raoul Motika & Christian Haupt & Paul Walther & Volker Schmidt & Stefan, 2021. "Role of mutations and post-translational modifications in systemic AL amyloidosis studied by cryo-EM," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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