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Antibodies to a scrapie prion protein

Nature volume 310, pages 418–421 (1984)Cite this article

Abstract

Scrapie is a slow infection of the nervous system which progresses in the absence of any apparent immune response1–8. The recent development of a large-scale purification protocol for scrapie prion9 made it possible to obtain substantial quantities of electrophoretically purified prion protein (PrP 27–30) and we report here on the successful production of a rabbit antiserum to PrP 27–30. The antiserum reacted with PrP 27–30 and several lower molecular weight proteins as shown by Western blots; it did not react with protein preparations from uninfected brains. Discrete structures in the subependymal region of scrapie-infected hamster brains were stained immunocytochemically. These same structures also stained with Congo red dye and showed green birefringence with polarized light, a characteristic of purified prion rods9. This staining pattern suggests that they are amyloid plaques.

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Authors and Affiliations

  1. Department of Neurology, University of California, San Francisco, California, 94143, USA

    Paul E. Bendheim, Ronald A. Barry & Stanley B. Prusiner

  2. Department of Biochemistry and Biophysics, University of California, San Francisco, California, 94143, USA

    Stanley B. Prusiner

  3. Department of Pathology, University of California, San Francisco, California, 94143, USA

    Stephen J. DeArmond

  4. Department of Laboratory Medicine, University of California, San Francisco, California, 94143, USA

    Daniel P. Stites

Authors
  1. Paul E. Bendheim
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  2. Ronald A. Barry
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  3. Stephen J. DeArmond
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  4. Daniel P. Stites
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  5. Stanley B. Prusiner
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Bendheim, P., Barry, R., DeArmond, S. et al. Antibodies to a scrapie prion protein. Nature 310, 418–421 (1984). https://doi.org/10.1038/310418a0

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