Structural Properties of Recombinant Human Prion Protein

  • Graham Jackson
  • Andrew Hill
  • Catherine Joseph
  • Anthony Clarke
  • John Collinge
Chapter
Part of the NATO ASI Series book series (NSSA, volume 295)

Abstract

Priori diseases are a group of fatal, neurodegenerative conditions affecting both humans and animals. Previously called transmissible spongiform encephalopathies or slow virus diseases they are unique in that they may have a sporadic, inherited or transmissible origin. The transmissible prion diseases have become an area of increasing public concern because of the epidemic of a novel bovine prion disease, bovine spongiform encephalopathy, and despite recent advances, many uncertainties exist in understanding of the nature of the infectious agent.

Keywords

Tyrosine Amide Titration Polypeptide Hydrochloride 

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Bibliography

  1. Basler, K., Oesch, B., Scott, M., Westaway, D., Walchli, M., Groth, D.F., McKinley, M.P., Prusiner, S.B., and Weissmann, C. (1986). Scrapie and cellular PrP isoforms are encoded by the same chromosomal gene. Cell 46, 417–428.PubMedCrossRefGoogle Scholar
  2. Collinge, J. Human prion diseases and bovine spongiform encephalopathy (BSE). Hum Mol Genetics 6(10): 1699–1705, 1997.CrossRefGoogle Scholar
  3. Pan, K., Baldwin, M.A., Nguyen, J., Gasset, M., Serban, A., Groth, D., Mehlhorn, I., Huang, Z., Fletterick, R.J., Cohen, F.E., and Prusiner, S.B. (1993). Conversion of α-helices into β-sheets features in the formation of the scrapie prion proteins. Proc Natl Acad Sci USA 90, 10962–10966.PubMedCrossRefGoogle Scholar
  4. Hornemann, S. and Glockshuber, R. (1996). Autonomous and reversible folding of a soluble aminoterminally truncated segment of the mouse prion protein. J. Mol. Biol. 262, 614–619.CrossRefGoogle Scholar
  5. Riek, R., Hornemann, S., Wider, G., Billeter, M., Glockshuber, R. and Wuthrich, K. (1996). NMR structure of the mouse prion protein domain PrP(121–231). Nature 382, 180–182.PubMedCrossRefGoogle Scholar
  6. Safar, J., Wang, W., Padgett, M.P., Ceroni, M., Piccardo, P., Zopf, D., Gajdusek, D.C., and Gibbs, C.J.J. (1990). Molecular mass, biochemical composition, and physicochemical behavior of the infectious form of the scrapie precursor protein monomer. Proc. Natl. Acad. Sci. U. S. A. 87, 6373–6377.PubMedCrossRefGoogle Scholar
  7. Stahl, N., Borchelt, D.R., Hsiao, K., and Prusiner, S.B. (1987). Scrapie prion protein contains a phosphatidylinositol glycolipid. Cell 51, 229–240.PubMedCrossRefGoogle Scholar
  8. Staniforth, R.A., Burston, S.G., Smith, C.J., Jackson, G.S., Badcoe, I.G., Atkinson, T., Holbrook, J.J. and Clarke, A.R. (1993). The energetics and cooperativiry of protein folding. A simple experimental analysis based upon the solvation of internal residues. Biochemistry 32, 3842–3851.PubMedCrossRefGoogle Scholar
  9. Turk, E., Teplow, D.B., Hood, L.E., and Prusiner, S.B. (1988). Purification and properties of the cellular and scrapie hamster prion proteins. Eur. J Biochem. 176, 21–30.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 1998

Authors and Affiliations

  • Graham Jackson
    • 1
  • Andrew Hill
    • 1
  • Catherine Joseph
    • 1
  • Anthony Clarke
    • 2
  • John Collinge
    • 1
  1. 1.Neurogenetics UnitImperial College School of Medicine at St Mary’sLondonUK
  2. 2.Department of BiochemistryUniversity of BristolBristolUK

Personalised recommendations