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Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

Author

Listed:
  • David R. Booth

    (Royal Postgraduate Medical School, Hammersmith Hospital)

  • Margaret Sunde

    (Oxford Centre for Molecular Sciences, University of Oxford)

  • Vittorio Bellotti

    (Royal Postgraduate Medical School, Hammersmith Hospital
    Università di Pavia)

  • Carol V. Robinson

    (Oxford Centre for Molecular Sciences, University of Oxford)

  • Winston L. Hutchinson

    (Royal Postgraduate Medical School, Hammersmith Hospital)

  • Paul E. Fraser

    (University of Toronto)

  • Philip N. Hawkins

    (Royal Postgraduate Medical School, Hammersmith Hospital)

  • Christopher M. Dobson

    (Oxford Centre for Molecular Sciences, University of Oxford)

  • Sheena E. Radford

    (Oxford Centre for Molecular Sciences, University of Oxford
    University of Leeds)

  • Colin C. F. Blake

    (Oxford Centre for Molecular Sciences, University of Oxford)

  • Mark B. Pepys

    (Royal Postgraduate Medical School, Hammersmith Hospital)

Abstract

Tissue deposition of soluble proteins as amyloid fibrils underlies a range of fatal diseases. The two naturally occurring human lysozyme variants are both amyloidogenic, and are shown here to be unstable. They aggregate to form amyloid fibrils with transformation of the mainly helical native fold, observed in crystal structures, to the amyloid fibril cross-β fold. Biophysical studies suggest that partly folded intermediates are involved in fibrillogenesis, and this may be relevant to amyloidosis generally.

Suggested Citation

  • David R. Booth & Margaret Sunde & Vittorio Bellotti & Carol V. Robinson & Winston L. Hutchinson & Paul E. Fraser & Philip N. Hawkins & Christopher M. Dobson & Sheena E. Radford & Colin C. F. Blake & M, 1997. "Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis," Nature, Nature, vol. 385(6619), pages 787-793, February.
    • Handle: RePEc:nat:nature:v:385:y:1997:i:6619:d:10.1038_385787a0
    DOI: 10.1038/385787a0
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    Cited by:

    1. 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.
    2. Emily G. Saccuzzo & Mubark D. Mebrat & Hailee F. Scelsi & Minjoo Kim & Minh Thu Ma & Xinya Su & Shannon E. Hill & Elisa Rheaume & Renhao Li & Matthew P. Torres & James C. Gumbart & Wade D. Van Horn & , 2024. "Competition between inside-out unfolding and pathogenic aggregation in an amyloid-forming β-propeller," Nature Communications, Nature, vol. 15(1), pages 1-14, December.

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