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Prions and their partners in crime

Author

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  • Byron Caughey

    (National Institute of Allergy and Infectious Disease, National Institutes of Health, Rocky Mountain Laboratories)

  • Gerald S. Baron

    (National Institute of Allergy and Infectious Disease, National Institutes of Health, Rocky Mountain Laboratories)

Abstract

Prions, the infectious agents of transmissible spongiform encephalopathies (TSEs), have defied full characterization for decades. The dogma has been that prions lack nucleic acids and are composed of a pathological, self-inducing form of the host's prion protein (PrP). Recent progress in propagating TSE infectivity in cell-free systems has effectively ruled out the involvement of foreign nucleic acids. However, host-derived nucleic acids or other non-PrP molecules seem to be crucial. Interactions between TSE-associated PrP and its normal counterpart are also pathalogically important, so the physiological functions of normal PrP and how they might be corrupted by TSE infections have been the subject of recent research.

Suggested Citation

  • Byron Caughey & Gerald S. Baron, 2006. "Prions and their partners in crime," Nature, Nature, vol. 443(7113), pages 803-810, October.
    • Handle: RePEc:nat:nature:v:443:y:2006:i:7113:d:10.1038_nature05294
    DOI: 10.1038/nature05294
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    Cited by:

    1. Victoria A Lawson & Brooke Lumicisi & Jeremy Welton & Dorothy Machalek & Katrina Gouramanis & Helen M Klemm & James D Stewart & Colin L Masters & David E Hoke & Steven J Collins & Andrew F Hill, 2010. "Glycosaminoglycan Sulphation Affects the Seeded Misfolding of a Mutant Prion Protein," PLOS ONE, Public Library of Science, vol. 5(8), pages 1-9, August.

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