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Common transthyretin-derived amyloid fibril structures in patients with hereditary ATTR amyloidosis

Author

Listed:
  • Maximilian Steinebrei

    (Ulm University)

  • Julian Baur

    (Ulm University)

  • Anaviggha Pradhan

    (Ulm University)

  • Niklas Kupfer

    (Ulm University)

  • Sebastian Wiese

    (Ulm University)

  • Ute Hegenbart

    (University Hospital Heidelberg)

  • Stefan O. Schönland

    (University Hospital Heidelberg)

  • Matthias Schmidt

    (Ulm University)

  • Marcus Fändrich

    (Ulm University)

Abstract

Systemic ATTR amyloidosis is an increasingly important protein misfolding disease that is provoked by the formation of amyloid fibrils from transthyretin protein. The pathological and clinical disease manifestations and the number of pathogenic mutational changes in transthyretin are highly diverse, raising the question whether the different mutations may lead to different fibril morphologies. Using cryo-electron microscopy, however, we show here that the fibril structure is remarkably similar in patients that are affected by different mutations. Our data suggest that the circumstances under which these fibrils are formed and deposited inside the body - and not only the fibril morphology - are crucial for defining the phenotypic variability in many patients.

Suggested Citation

  • Maximilian Steinebrei & Julian Baur & Anaviggha Pradhan & Niklas Kupfer & Sebastian Wiese & Ute Hegenbart & Stefan O. Schönland & Matthias Schmidt & Marcus Fändrich, 2023. "Common transthyretin-derived amyloid fibril structures in patients with hereditary ATTR amyloidosis," Nature Communications, Nature, vol. 14(1), pages 1-8, December.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-43301-3
    DOI: 10.1038/s41467-023-43301-3
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    References listed on IDEAS

    as
    1. Lynn Radamaker & Julian Baur & Stefanie Huhn & Christian Haupt & Ute Hegenbart & Stefan Schönland & Akanksha Bansal & Matthias Schmidt & Marcus Fändrich, 2021. "Cryo-EM reveals structural breaks in a patient-derived amyloid fibril from systemic AL amyloidosis," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    2. Irina Iakovleva & Michael Hall & Melanie Oelker & Linda Sandblad & Intissar Anan & A. Elisabeth Sauer-Eriksson, 2021. "Structural basis for transthyretin amyloid formation in vitreous body of the eye," Nature Communications, Nature, vol. 12(1), pages 1-10, December.
    3. Maximilian Steinebrei & Juliane Gottwald & Julian Baur & Christoph Röcken & Ute Hegenbart & Stefan Schönland & Matthias Schmidt, 2022. "Cryo-EM structure of an ATTRwt amyloid fibril from systemic non-hereditary transthyretin amyloidosis," Nature Communications, Nature, vol. 13(1), pages 1-9, December.
    4. Matthias Schmidt & Sebastian Wiese & Volkan Adak & Jonas Engler & Shubhangi Agarwal & Günter Fritz & Per Westermark & Martin Zacharias & Marcus Fändrich, 2019. "Cryo-EM structure of a transthyretin-derived amyloid fibril from a patient with hereditary ATTR amyloidosis," Nature Communications, Nature, vol. 10(1), pages 1-9, December.
    5. Falk Liberta & Sarah Loerch & Matthies Rennegarbe & Angelika Schierhorn & Per Westermark & Gunilla T. Westermark & Bouke P. C. Hazenberg & Nikolaus Grigorieff & Marcus Fändrich & Matthias Schmidt, 2019. "Cryo-EM fibril structures from systemic AA amyloidosis reveal the species complementarity of pathological amyloids," Nature Communications, Nature, vol. 10(1), pages 1-10, December.
    6. Sambhasan Banerjee & Julian Baur & Christoph Daniel & Peter Benedikt Pfeiffer & Manuel Hitzenberger & Lukas Kuhn & Sebastian Wiese & Johan Bijzet & Christian Haupt & Kerstin U. Amann & Martin Zacharia, 2022. "Amyloid fibril structure from the vascular variant of systemic AA amyloidosis," Nature Communications, Nature, vol. 13(1), pages 1-8, December.
    7. Marius Kollmer & William Close & Leonie Funk & Jay Rasmussen & Aref Bsoul & Angelika Schierhorn & Matthias Schmidt & Christina J. Sigurdson & Mathias Jucker & Marcus Fändrich, 2019. "Cryo-EM structure and polymorphism of Aβ amyloid fibrils purified from Alzheimer’s brain tissue," Nature Communications, Nature, vol. 10(1), pages 1-8, December.
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