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Cryo-EM structure and polymorphic maturation of a viral transduction enhancing amyloid fibril

Author

Listed:
  • Thomas Heerde

    (Ulm University)

  • Desiree Schütz

    (Ulm University Medical Center)

  • Yu-Jie Lin

    (Ulm University)

  • Jan Münch

    (Ulm University Medical Center)

  • Matthias Schmidt

    (Ulm University)

  • Marcus Fändrich

    (Ulm University)

Abstract

Amyloid fibrils have emerged as innovative tools to enhance the transduction efficiency of retroviral vectors in gene therapy strategies. In this study, we used cryo-electron microscopy to analyze the structure of a biotechnologically engineered peptide fibril that enhances retroviral infectivity. Our findings show that the peptide undergoes a time-dependent morphological maturation into polymorphic amyloid fibril structures. The fibrils consist of mated cross-β sheets that interact by the hydrophobic residues of the amphipathic fibril-forming peptide. The now available structural data help to explain the mechanism of retroviral infectivity enhancement, provide insights into the molecular plasticity of amyloid structures and illuminate the thermodynamic basis of their morphological maturation.

Suggested Citation

  • 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.
    • Handle: RePEc:nat:natcom:v:14:y:2023:i:1:d:10.1038_s41467-023-40042-1
    DOI: 10.1038/s41467-023-40042-1
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    References listed on IDEAS

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    1. Michael R. Sawaya & Shilpa Sambashivan & Rebecca Nelson & Magdalena I. Ivanova & Stuart A. Sievers & Marcin I. Apostol & Michael J. Thompson & Melinda Balbirnie & Jed J. W. Wiltzius & Heather T. McFar, 2007. "Atomic structures of amyloid cross-β spines reveal varied steric zippers," Nature, Nature, vol. 447(7143), pages 453-457, May.
    2. 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.
    3. Rebecca Nelson & Michael R. Sawaya & Melinda Balbirnie & Anders Ø. Madsen & Christian Riekel & Robert Grothe & David Eisenberg, 2005. "Structure of the cross-β spine of amyloid-like fibrils," Nature, Nature, vol. 435(7043), pages 773-778, June.
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