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The most infectious prion protein particles

Author

Listed:
  • Jay R. Silveira

    (Laboratory of Persistent Viral Diseases)

  • Gregory J. Raymond

    (Laboratory of Persistent Viral Diseases)

  • Andrew G. Hughson

    (Laboratory of Persistent Viral Diseases)

  • Richard E. Race

    (Laboratory of Persistent Viral Diseases)

  • Valerie L. Sim

    (Laboratory of Persistent Viral Diseases)

  • Stanley F. Hayes

    (National Institutes of Health)

  • Byron Caughey

    (Laboratory of Persistent Viral Diseases)

Abstract

Prions: form and infectivity The prospects of limiting the spread of transmissible spongiform encephalopathies such as Creutzfeldt–Jakob disease depend in part on identifying the most infectious forms of the prions that carry the diseases. A study of modified scrapie prions shows that clusters of 14 to 28 prion proteins are the most infectious and that clusters of less than six molecules have virtually no infectivity. That could have implications for the treatment of diseases such as Alzheimer's and Parkinson's, characterized by deposition of prion-related amyloid fibrils. It's possible that efforts to alleviate symptoms by destabilizing these large protein aggregates might make things worse by producing smaller, more infective particles. Two other papers in this issue tackle fundamental aspects of the biology of prions and amyloid fibrils. The conversion of the yeast protein Sup35 to its prion form does not need to happen during the synthesis of Sup35 — mature and fully functional molecules can readily join a prion seed. This remodelling of the mature protein is accompanied by the immediate loss of its activity. And a study of a ‘designed’ amyloid fibril made from ribonuclease A reveals that amyloid containing native-like molecules can retain enzyme activity. This involves a domain swap with the neighbouring protein, and supports the ‘zipper-spine model’ for β-amyloid structures.

Suggested Citation

  • Jay R. Silveira & Gregory J. Raymond & Andrew G. Hughson & Richard E. Race & Valerie L. Sim & Stanley F. Hayes & Byron Caughey, 2005. "The most infectious prion protein particles," Nature, Nature, vol. 437(7056), pages 257-261, September.
  • Handle: RePEc:nat:nature:v:437:y:2005:i:7056:d:10.1038_nature03989
    DOI: 10.1038/nature03989
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    Citations

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    Cited by:

    1. Mookyung Cheon & Iksoo Chang & Sandipan Mohanty & Leila M Luheshi & Christopher M Dobson & Michele Vendruscolo & Giorgio Favrin, 2007. "Structural Reorganisation and Potential Toxicity of Oligomeric Species Formed during the Assembly of Amyloid Fibrils," PLOS Computational Biology, Public Library of Science, vol. 3(9), pages 1-12, September.
    2. Juan Manuel Ribes & Mitali P. Patel & Hazim A. Halim & Antonio Berretta & Sharon A. Tooze & Peter-Christian Klöhn, 2023. "Prion protein conversion at two distinct cellular sites precedes fibrillisation," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    3. 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.

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