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The Formation of Scrapie-Associated Prion Protein In Vitro

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Bovine Spongiform Encephalopathy

Part of the book series: Serono Symposia USA Norwell, Massachusetts ((SERONOSYMP))

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Abstract

The formation of the abnormal protease-resistant, amyloidogenic isoform of PrP (PrP-res) appears to play a central role in the pathogenesis of scrapie and other transmissible spongiform encephalopathies (TSEs). Thus, it is important to understand the process by which the normal, protease-sensitive PrP (PrP-sen) is converted to the protease-resistant state. To define the cellular and molecular details of this process and how it might be inhibited, we have performed in vitro studies using both scrapie-infected tissue culture cells and cell-free reactions. This chapter summarizes the recent results from these studies.

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Authors
  1. Byron Caughey
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  2. Suzette Priola
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  3. David Kocisko
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  4. Gregory Raymond
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  5. Jon Come
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  6. Santosh Nandan
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  7. Bruce Chesebro
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  8. Peter Lansbury
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Editor information

Editors and Affiliations

  1. Laboratory of Central Nervous System Studies Basic Neurosciences Program Division of Intramural Research, National Institute of Neurological Disorders and Stroke National Institutes of Health, Bethesda, MD, 20892-4122, USA

    Clarence J. Gibbs Jr. Ph.D.

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© 1996 Springer-Verlag New York, Inc.

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Caughey, B. et al. (1996). The Formation of Scrapie-Associated Prion Protein In Vitro. In: Gibbs, C.J. (eds) Bovine Spongiform Encephalopathy. Serono Symposia USA Norwell, Massachusetts. Springer, New York, NY. https://doi.org/10.1007/978-1-4612-2406-8_22

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  • DOI: https://doi.org/10.1007/978-1-4612-2406-8_22

  • Publisher Name: Springer, New York, NY

  • Print ISBN: 978-1-4612-7527-5

  • Online ISBN: 978-1-4612-2406-8

  • eBook Packages: Springer Book Archive

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