Resistance of bovine spongiform encephalopathy (BSE) prions to inactivation

PLoS Pathogens

Volumn 4, Issue 11, 2008, Pages

  Giles, Kurt ^a   Glidden, David V ^b   Beckwith, Robyn ^a   Seoanes, Rose ^a   Peretz, David ^a,c   DeArmond, Stephen J ^a,b   Prusiner, Stanley B ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Novartis Vaccines and Diagnostics   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DODECYL SULFATE SODIUM; PRION PROTEIN; PROTEINASE K;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BIOASSAY; BOVINE SPONGIFORM ENCEPHALOPATHY; CATTLE; CONTROLLED STUDY; INFECTION SENSITIVITY; MATHEMATICAL MODEL; MOUSE; NONHUMAN; PH; PRION DISEASE; TEMPERATURE; TRANSGENIC MOUSE; VIRUS INACTIVATION; WESTERN BLOTTING; ANIMAL; CELL LINE; CHEMISTRY; CREUTZFELDT JAKOB DISEASE; HAMSTER; HUMAN; PRION; PROTEIN DENATURATION; SPECIES DIFFERENCE;

BOS; BOVINAE; CRICETINAE; MUS MUSCULUS;

ANIMALS; CATTLE; CELL LINE; CREUTZFELDT-JAKOB SYNDROME; CRICETINAE; ENCEPHALOPATHY, BOVINE SPONGIFORM; HUMANS; HYDROGEN-ION CONCENTRATION; MICE; MICE, TRANSGENIC; PRIONS; PROTEIN DENATURATION; SODIUM DODECYL SULFATE; SPECIES SPECIFICITY; TEMPERATURE;

EID: 57149118018     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1000206     Document Type: Article

References (62)

1. Kimberlin RH, Walker CA (1979) Pathogenesis of scrapie: agent multiplication in brain at the first and second passage of hamster scrapie in mice. J Gen Virol 42: 107-117.
2. Kimberlin RH, Cole S, Walker CA (1987) Temporary and permanent modifications to a single strain of mouse scrapie on transmission to rats and hamsters. J Gen Virol 68: 1875-1881.
3. Peretz D, Williamson RA, Legname G, Matsunaga Y, Vergara J, et al. (2002) A change in the conformation of prions accompanies the emergence of a new prion strain. Neuron 34: 921-932.
4. Asante EA, Linehan JM, Desbruslais M, Joiner S, Gowland I, et al. (2002) BSE prions propagate as either variant CJD-like or sporadic CJD-like prion strains in transgenic mice expressing human prion protein. EMBO J 21: 6358-6366.
5. Bruce ME, Dickinson AG (1987) Biological evidence that the scrapie agent has an independent genome. J Gen Virol 68: 79-89.
6. Bessen RA, Marsh RF (1994) Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J Virol 68: 7859-7868.
7. Telling GC, Parchi P, DeArmond SJ, Cortelli P, Montagna P, et al. (1996) Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274: 2079-2082.
8. Sc molecules with different conformations. Nat Med 4: 1157-1165.
9. Peretz D, Scott M, Groth D, Williamson A, Burton D, et al. (2001) Strain-specified relative conformational stability of the scrapie prion protein. Protein Sci 10: 854-863.
10. Legname G, Nguyen H-OB, Peretz D, Cohen FE, DeArmond SJ, et al. (2006) Continuum of prion protein structures enciphers a multitude of prion isolate-specified phenotypes. Proc Natl Acad Sci USA 103: 19105-19110.
11. Sc. J Virol 81: 12119-12127.
12. Gordon WS (1946) Advances in veterinary research. Vet Res 58: 516-520.
13. Alper T, Haig DA, Clarke MC (1966) The exceptionally small size of the scrapie agent. Biochem Biophys Res Commun 22: 278-284.
14. Alper T, Cramp WA, Haig DA, Clarke MC (1967) Does the agent of scrapie replicate without nucleic acid? Nature 214: 764-766.
15. Prusiner SB, Bolton DC, Groth DF, Bowman KA, Cochran SP, et al. (1982) Further purification and characterization of scrapie prions. Biochemistry 21: 6942-6950.
16. Millson GC, Manning EJ (1979) The effect of selected detergents on scrapie infectivity. In: Prusiner SB, Hadlow WJ, eds. Slow Transmissible Diseases of the Nervous System, Vol 2. New York: Academic Press. pp 409-424.
17. Prusiner SB, Groth DF, McKinley MP, Cochran SP, Bowman KA, et al. (1981) Thiocyanate and hydroxyl ions inactivate the scrapie agent. Proc Natl Acad Sci USA 78: 4606-4610.
18. Prusiner SB, McKinley MP, Bolton DC, Bowman KA, Groth DF, et al. (1984) Prions: methods for assay, purification and characterization. In: Maramorosch K, Koprowski H, eds. Methods in Virology. New York: Academic Press. pp 293-345.
19. World Health Organization (1999) WHO infection control guidelines for transmissible spongiform encephalopathies. Geneva. 38 p.
20. Brown SA, Merritt K, Woods TO, Busick DN (2005) Effects on instruments of the World Health Organization-recommended protocols for decontamination after possible exposure to transmissible spongiform encephalopathy-contaminated tissue. J Biomed Mater Res B Appl Biomater 72: 186-190.
21. Sonntag D, Peters OA (2007) Effect of prion decontamination protocols on nickel-titanium rotary surfaces. J Endod 33: 442-446.
22. Korth C, Kaneko K, Groth D, Heye N, Telling G, et al. (2003) Abbreviated incubation times for human prions in mice expressing a chimeric mouse - human prion protein transgene. Proc Natl Acad Sci USA 100: 4784-4789.
23. Peretz D, Supattapone S, Giles K, Vergara J, Freyman Y, et al. (2006) Inactivation of prions by acidic sodium dodecyl sulfate. J Virol 80: 322-331.
24. Fraser H, Bruce ME, Chree A, McConnell I, Wells GAH (1992) Transmission of bovine spongiform encephalopathy and scrapie to mice. J Gen Virol 73: 1891-1897.
25. Bruce M, Chree A, McConnell I, Foster J, Pearson G, et al. (1994) Transmission of bovine spongiform encephalopathy and scrapie to mice: strain variation and the species barrier. Philos Trans R Soc Lond B Biol Sci 343: 405-411.
26. McLeod AH, Murdoch H, Dickinson J, Dennis MJ, Hall GA, et al. (2004) Proteolytic inactivation of the bovine spongiform encephalopathy agent. Biochem Biophys Res Commun 317: 1165-1170.
27. Kimberlin RH, Marsh RF (1975) Comparison of scrapie and transmissible mink encephalopathy in hamsters. I. Biochemical studies of brain during development of disease. J Infect Dis 131: 97-103.
28. Marsh RF, Kimberlin RH (1975) Comparison of scrapie and transmissible mink encephalopathy in hamsters. II. Clinical signs, pathology and pathogenesis. J Infect Dis 131: 104-110.
29. Carlson GA, Ebeling C, Yang S-L, Telling G, Torchia M, et al. (1994) Prion isolate specified allotypic interactions between the cellular and scrapie prion proteins in congenic and transgenic mice. Proc Natl Acad Sci USA 91: 5690-5694.
30. Scott MR, Safar J, Telling G, Nguyen O, Groth D, et al. (1997) Identification of a prion protein epitope modulating transmission of bovine spongiform encephalopathy prions to transgenic mice. Proc Natl Acad Sci USA 94: 14279-14284.
31. Buschmann A, Gretzschel A, Biacabe AG, Schiebel K, Corona C, et al. (2006) Atypical BSE in Germany-proof of transmissibility and biochemical characterization. Vet Microbiol 117: 103-116.
32. Scott M, Foster D, Mirenda C, Serban D, Coufal F, et al. (1989) Transgenic mice expressing hamster prion protein produce species-specific scrapie infectivity and amyloid plaques. Cell 59: 847-857.
33. Safar JG, DeArmond SJ, Kociuba K, Deering C, Didorenko S, et al. (2005) Prion clearance in bigenic mice. J Gen Virol 86: 2913-2923.
34. Supattapone S, Nguyen H-OB, Cohen FE, Prusiner SB, Scott MR (1999) Elimination of prions by branched polyamines and implications for therapeutics. Proc Natl Acad Sci USA 96: 14529-14534.
35. Safar JG, Scott M, Monaghan J, Deering C, Didorenko S, et al. (2002) Measuring prions causing bovine spongiform encephalopathy or chronic wasting disease by immunoassays and transgenic mice. Nat Biotechnol 20: 1147-1150.
36. Scott MR, Köhler R, Foster D, Prusiner SB (1992) Chimeric prion protein expression in cultured cells and transgenic mice. Protein Sci 1: 986-997.
37. Giles K, Supattapone S, Peretz D, Glidden DV, Baron H, et al. (2007) Disinfection of prions. In: Zhu PC, ed. New Biocides Development: The Combined Approach of Chemistry and Microbiology. Washington, D.C.: American Chemical Society. pp 52-74.
38. Kaplan EL, Meier P (1958) Nonparametric estimation from incomplete observations. J Am Stat Assoc 53: 457-481.
39. Brookmeyer R, Crowley J (1982) A confidence interval for the median survival time. Biometrics 38: 29-41.
40. Cox DR (1972) Regression models and life-tables. J R Stat Soc Ser A Method 34: 187-220.
41. Cox DR, Oakes D (1984) Analysis of Survival Data. New York: Chapman & Hall/CRC. 208 p.
42. Holt JD, Prentice RL (1974) Survival analyses in twin studies and matched pair experiments. Biometrika 61: 17-30.
43. Therneau TM, Grambsch PM (2000) Modeling Survival Data: Extending the Cox Model. New York: Springer-Verlag. 350 p.
44. Ernst DR, Race RE (1993) Comparative analysis of scrapie agent inactivation methods. J Virol Methods 41: 193-202.
45. Fichet G, Comoy E, Duval C, Antloga K, Dehen C, et al. (2004) Novel methods for disinfection of prion-contaminated medical devices. Lancet 364: 521-526.
46. Jackson GS, McKintosh E, Flechsig E, Prodromidou K, Hirsch P, et al. (2005) An enzyme-detergent method for effective prion decontamination of surgical steel. J Gen Virol 86: 869-878.
47. Taguchi F, Tamai Y, Uchida K, Kitajima R, Kojima H, et al. (1991) Proposal for a procedure for complete inactivation of the Creutzfeldt-Jakob disease agent. Arch Virol 119: 297-301.
48. Manuelidis L (1997) Decontamination of Creutzfeldt-Jakob disease and other transmissible agents. J Neurovirol 3: 62-65.
49. Brown P, Gibbs CJ Jr, Amyx HL, Kingsbury DT, Rohwer RG, et al. (1982) Chemical disinfection of Creutzfeldt-Jakob disease virus. N Engl J Med 306: 1279-1282.
50. Parchi P, Zou W, Wang W, Brown P, Capellari S, et al. (2000) Genetic influence on the structural variations of the abnormal prion protein. Proc Natl Acad Sci USA 97: 10168-10172.
51. Howells LC, Anderson S, Coldham NG, Sauer MJ (2008) Transmissible spongiform encephalopathy strain-associated diversity of N-terminal proteinase K cleavage sites of PrP(Sc) from scrapie-infected and bovine spongiform encephalopathy-infected mice. Biomarkers 13: 393-412.
52. Stack MJ, Chaplin MJ, Clark J (2002) Differentiation of prion protein glycoforms from naturally occurring sheep scrapie, sheep-passaged scrapie strains (CH1641 and SSBP1), bovine spongiform encephalopathy (BSE) cases and Romney and Cheviot breed sheep experimentally inoculated with BSE using two monoclonal antibodies. Acta Neuropathol (Berl) 104: 279-286.
53. McKinley MP, Bolton DC, Prusiner SB (1983) A protease-resistant protein is a structural component of the scrapie prion. Cell 35: 57-62.
54. Sc conformers induced by a synthetic peptide and several prion strains. J Virol 78: 2088-2099.
55. Colby DW, Zhang Q, Wang S, Groth D, Legname G, et al. (2007) Prion detection by an amyloid seeding assay. Proc Natl Acad Sci USA 104: 20914-20919.
56. Taylor DM, Fernie K, Steele PJ, McConnell I, Somerville RA (2002) Thermostability of mouse-passaged BSE and scrapie is independent of host PrP genotype: implications for the nature of the causal agents. J Gen Virol 83: 3199-3204.
57. Lawson VA, Stewart JD, Masters CL (2007) Enzymatic detergent treatment protocol that reduces protease-resistant prion protein load and infectivity from surgical-steel monofilaments contaminated with a human-derived prion strain. J Gen Virol 88: 2905-2914.
58. Scott MR, Will R, Ironside J, Nguyen H-OB, Tremblay P, et al. (1999) Compelling transgenetic evidence for transmission of bovine spongiform encephalopathy prions to humans. Proc Natl Acad Sci USA 96: 15137-15142.
59. Philipp WJ, Groth D, Giles K, Vodrazka P, Schimmel H, et al. (2007) Transgenic mouse brains for evaluation and quality control of BSE tests. Biol Chem 388: 349-354.
60. Zobeley E, Flechsig E, Cozzio A, Enari M, Weissmann C (1999) Infectivity of scrapie prions bound to a stainless steel surface. Mol Med 5: 240-243.
61. Lemmer K, Mielke M, Pauli G, Beekes M (2004) Decontamination of surgical instruments from prion proteins: in vitro studies on the detachment, destabilization and degradation of PrPSc bound to steel surfaces. J Gen Virol 85: 3805-3816.
62. Weissmann C, Enari M, Klohn PC, Rossi D, Flechsig E (2002) Transmission of prions. Proc Natl Acad Sci USA 99: 16378-16383.