1887

Abstract

Sodium hydroxide (NaOH) solutions are widely used for the purification of contaminated equipment, as they are known to inactivate a variety of pathogens. However, information about their effect on agents causing transmissible spongiform encephalopathy (TSE) is sparse and contradictory. Scrapie hamster brain homogenate, containing the disease-associated form of the prion protein (PrP), was exposed to NaOH. Kinetics studies showed that treatment of brain homogenate with millimolar concentrations of NaOH rapidly abolished the proteinase K-resistant form of the prion protein (PrP). NaOH treatment converted PrP into a protease-sensitive form, either in solution or when adsorbed to a metallic surface. If infectivity of TSEs is linked with PrP, the results imply that inactivation of TSE occurs more efficiently than currently assumed.

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2003-11-01
2019-12-14
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References

  1. Brown, P., Rohwer, R. G. & Gajdusek, D. C. ( 1984; ). Sodium hydroxide decontamination of Creutzfeldt–Jakob disease virus. N Engl J Med 310, 727.
    [Google Scholar]
  2. Brown, P., Rohwer, R. G. & Gajdusek, D. C. ( 1986; ). Newer data on the inactivation of scrapie virus or Creutzfeldt–Jakob disease virus in brain tissue. J Infect Dis 153, 1145–1148.[CrossRef]
    [Google Scholar]
  3. Caughey, B., Raymond, G. J., Kocisko, D. A. & Lansbury, P. T., Jr ( 1997; ). Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J Virol 71, 4107–4110.
    [Google Scholar]
  4. Di Martino, A., Safar, J., Ceroni, M. & Gibbs, C. J., Jr ( 1993; ). Inactivation of the scrapie agent in a scaled-down procedure for the purification of gangliosides from brain tissue. Dev Biol Stand 80, 187–194.
    [Google Scholar]
  5. Flechsig, E., Hegyi, I., Enari, M., Schwarz, P., Collinge, J. & Weissmann, C. ( 2001; ). Transmission of scrapie by steel-surface-bound prions. Mol Med 7, 679–684.
    [Google Scholar]
  6. Foster, P. R., Welch, A. G., McLean, C., Griffin, B. D., Hardy, J. C., Bartley, A., MacDonald, S. & Bailey, A. C. ( 2000; ). Studies on the removal of abnormal prion protein by processes used in the manufacture of human plasma products. Vox Sang 78, 86–95.[CrossRef]
    [Google Scholar]
  7. Lee, D. C., Stenland, C. J., Hartwell, R. C. & 7 other authors ( 2000; ). Monitoring plasma processing steps with a sensitive Western blot assay for the detection of the prion protein. J Virol Methods 84, 77–89.[CrossRef]
    [Google Scholar]
  8. Lee, D. C., Stenland, C. J., Miller, J. L. & 8 other authors ( 2001; ). A direct relationship between the partitioning of the pathogenic prion protein and transmissible spongiform encephalopathy infectivity during the purification of plasma proteins. Transfusion 41, 449–455; erratum 41, 1079.
    [Google Scholar]
  9. McKinley, M. P., Bolton, D. C. & Prusiner, S. B. ( 1983; ). A protease-resistant protein is a structural component of the scrapie prion. Cell 35, 57–62.[CrossRef]
    [Google Scholar]
  10. Meyer, R. K., McKinley, M. P., Bowman, K. A., Braunfeld, M. B., Barry, R. A. & Prusiner, S. B. ( 1986; ). Separation and properties of cellular and scrapie prion proteins. Proc Natl Acad Sci U S A 83, 2310–2314.[CrossRef]
    [Google Scholar]
  11. Miller, J. L., Petteway, S. R., Jr & Lee, D. C. ( 2001; ). Ensuring the pathogen safety of intravenous immunoglobulin and other human plasma-derived therapeutic proteins. J Allergy Clin Immunol 108 (Suppl. 4), S91–S94.[CrossRef]
    [Google Scholar]
  12. Oesch, B., Doherr, M., Heim, D. & 7 other authors ( 2000; ). Application of Prionics Western blotting procedure to screen for BSE in cattle regularly slaughtered at Swiss abattoirs. Arch Virol 16, 189–195.
    [Google Scholar]
  13. Prusiner, S. B. ( 1998; ). Prions. Proc Natl Acad Sci U S A 95, 13363–13383.[CrossRef]
    [Google Scholar]
  14. Prusiner, S. B., Groth, D. F., McKinley, M. P., Cochran, S. P., Bowman, K. A. & Kasper, K. C. ( 1981; ). Thiocyanate and hydroxyl ions inactivate the scrapie agent. Proc Natl Acad Sci U S A 78, 4606–4610.[CrossRef]
    [Google Scholar]
  15. Race, R., Jenny, A. & Sutton, D. ( 1998; ). Scrapie infectivity and proteinase K-resistant prion protein in sheep placenta, brain, spleen, and lymph node: implications for transmission and antemortem diagnosis. J Infect Dis 178, 949–953.[CrossRef]
    [Google Scholar]
  16. Safar, J., Wang, W., Padgett, M. P., Ceroni, M., Piccardo, P., Zopf, D., Gajdusek, D. C. & Gibbs, C. J., Jr ( 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.[CrossRef]
    [Google Scholar]
  17. Safar, J., Roller, P. P., Gajdusek, D. C. & Gibbs, C. J., Jr ( 1993; ). Conformational transitions, dissociation, and unfolding of scrapie amyloid (prion) protein. J Biol Chem 268, 20276–20284.
    [Google Scholar]
  18. Schaller, O., Fatzer, R., Stack, M. & 9 other authors ( 1999; ). Validation of a Western immunoblotting procedure for bovine PrPSc detection and its use as a rapid surveillance method for the diagnosis of bovine spongiform encephalopathy (BSE). Acta Neuropathol 98, 437–443.[CrossRef]
    [Google Scholar]
  19. Shaked, G. M., Fridlander, G., Meiner, Z., Taraboulos, A. & Gabizon, R. ( 1999; ). Protease-resistant and detergent-insoluble prion protein is not necessarily associated with prion infectivity. J Biol Chem 274, 17981–17986.[CrossRef]
    [Google Scholar]
  20. Somerville, R. A. ( 2002; ). TSE agent strains and PrP: reconciling structure and function. Trends Biochem Sci 27, 606–612.[CrossRef]
    [Google Scholar]
  21. Somerville, R. A., Oberthur, R. C., Havekost, U., MacDonald, F., Taylor, D. M. & Dickinson, A. G. ( 2002; ). Characterization of thermodynamic diversity between transmissible spongiform encephalopathy agent strains and its theoretical implications. J Biol Chem 277, 11084–11089.[CrossRef]
    [Google Scholar]
  22. Tateishi, J., Tashima, T. & Kitamoto, T. ( 1991; ). Practical methods for chemical inactivation of Creutzfeldt–Jakob disease pathogen. Microbiol Immunol 35, 163–166.[CrossRef]
    [Google Scholar]
  23. Taylor, D. M. ( 2000; ). Inactivation of transmissible degenerative encephalopathy agents. Vet J 159, 10–17.[CrossRef]
    [Google Scholar]
  24. Wille, H., Prusiner, S. B. & Cohen, F. E. ( 2000; ). Scrapie infectivity is independent of amyloid staining properties of the N-terminally truncated prion protein. J Struct Biol 130, 323–338.[CrossRef]
    [Google Scholar]
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