1887

Abstract

Assays for the agent of Creutzfeldt–Jakob disease (CJD) include measurement of infectivity in different animal systems, such as wild-type or transgenic mice, and detection of PrP by different methods and formats. The various assays could be best calibrated against each other by use of uniform readily available materials, and samples of four human brains, two from sporadic CJD patients, one from a variant CJD patient and one from a non-CJD patient, have been prepared as 10 % homogenates dispensed in 2000 vials each for this purpose. Results of methods, particularly immunoblot assays, were compared in the first collaborative study described here. While dilution end-points varied, the minimum detectable volume was surprisingly uniform for most assays and differences in technical procedure, other than the sample volume tested, had no detectable systematic effect. The two specimens from sporadic CJD cases contained both type 1 and type 2 prion proteins in approximately equal proportions. The materials have been given the status of reference reagents by the World Health Organization and are available for further study and assessment of other or assay procedures.

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2004-06-01
2019-12-07
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References

  1. Barnard, G., Helmick, B., Maden, S., Gilbourne, C. & Patel, R. ( 2000; ). The measurement of prion protein in bovine brain tissue using differential extraction and DELFIA as a diagnostic test for BSE. Luminescence 15, 1–6.[CrossRef]
    [Google Scholar]
  2. Bellon, A., Seyfort-Brandt, W., Lang, H., Baron, H. & Vey, M. ( 2003; ). Improved conformation-dependent immunoassay: suitability for human prion detection with enhanced sensitivity. J Gen Virol 84, 1921–1925.[CrossRef]
    [Google Scholar]
  3. Collinge, J., Sidle, K. C. L., Meads, J., Ironside, J. & Hill, A. F. ( 1996; ). Molecular analysis of prion strain variation and the aetiology of new variant CJD. Nature 383, 685–690.[CrossRef]
    [Google Scholar]
  4. Kascsak, R. J., Rubenstein, R., Merz, P. A., Tonna-DeMasi, M., Ferska, R., Carp, R. I., Wisniewski, H. M. & Diringer, H. ( 1987; ). Mouse polyclonal and monoclonal antibody to scrapie-associated fibril protein. J Virol 61, 3688–3693.
    [Google Scholar]
  5. Korth, C., Stierli, P., Moser, M. & 13 other authors ( 1997; ). Prion (PrPSc)-specific epitope defined by a monoclonal antibody. Nature 390, 74–77.[CrossRef]
    [Google Scholar]
  6. Kovacs, G. G., Head, M. W., Hegyi, M. D. & 8 other authors ( 2002; ). Immunohistochemistry for the prion protein: comparison of different monoclonal antibodies in human prion disease subtypes. Brain Pathol 12, 1–11.
    [Google Scholar]
  7. Palmer, M. S., Dryden, A. J., Hughes, J. T. & Collinge, J. ( 1991; ). Homozygous prion protein genotype predisposes to sporadic Creutzfeldt–Jakob disease. Nature 352, 340–342.[CrossRef]
    [Google Scholar]
  8. Parchi, P., Castellani, R. & Capellari, S. ( 1996; ). Molecular basis of phenotypic variability in sproradic Creutzfeldt–Jakob disease. Ann Neurol 39, 767–778.[CrossRef]
    [Google Scholar]
  9. Prusiner, S. B. ( 1991; ). Molecular biology of prion diseases. Science 252, 1515–1522.[CrossRef]
    [Google Scholar]
  10. Prusiner, S. B. ( 1997; ). Prion disease and the BSE crisis. Science 278, 245–251.[CrossRef]
    [Google Scholar]
  11. Puoti, G., Giaccone, G., Rossi, G., Cancianti, B., Bugiani, O. & Tagliavini, F. ( 1999; ). Sporadic Creutzfeldt–Jakob disease: co-occurrence of different types of PrPSc in the same brain. Neurology 53, 2173–2176.[CrossRef]
    [Google Scholar]
  12. Safar, J., Wille, H., Itri, U., Groth, D., Serban, H., Torchia, M., Cohen, F. E. & Prusiner, S. B. ( 1998; ). Eight prion strains have PrPSc molecules with different conformations. Nat Med 4, 1157–1165.[CrossRef]
    [Google Scholar]
  13. Wadsworth, J. D. F., Hill, A. F., Joiner, S., Jackson, G. S., Clarke, A. R. & Collinge, J. ( 1999; ). Strain-specific prion-protein conformation determined by metal ions. Nat Cell Biol 1, 55–59.[CrossRef]
    [Google Scholar]
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