Persistence of pathogenic prion protein during simulated wastewater treatment processes

Environmental Science and Technology

Volumn 42, Issue 14, 2008, Pages 5254-5259

  Hinckley, Glen T ^a,d   Johnson, Christopher J ^b,e   Jacobson, Kurt H ^a   Bartholomay, Christian ^b,f   Mcmahon, Katherine D ^a   Mckenzie, Debbie ^b   Aiken, Judd M ^b   Pedersen, Joel A ^a,c  

^a University of Wisconsin Madison   (United States)

^b UNIVERSITY OF WISCONSIN MADISON   (United States)

^c UNIVERSITY OF WISCONSIN MADISON   (United States)

^d ELMHURST COLLEGE   (United States)

^e NATIONAL WILDLIFE HEALTH CENTER   (United States)

^f IOWA STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

MAMMALS; WASTEWATER RECLAMATION; WATER TREATMENT;

MAMMALIAN SPECIES; NEURO-DEGENERATIVE DISEASE; PRION DISEASES; PRION PROTEIN (PRP); SIMULATED WASTEWATER; TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES (TSE);

WASTEWATER TREATMENT;

PRION PROTEIN;

ACTIVATED SLUDGE; DISINFECTION; HYDROLOGICAL MODELING; PATHOGEN; PROTEIN; WASTE TREATMENT; WASTEWATER;

ACTIVATED SLUDGE; ANAEROBIC DIGESTION; ARTICLE; BIOSOLID; LANDFILL; SEPTIC TANK; SEWER; SLUDGE DIGESTION; WASTE WATER MANAGEMENT;

ANAEROBIOSIS; ANIMALS; BIODEGRADATION, ENVIRONMENTAL; CRICETINAE; CRICETULUS; HUMANS; PRION DISEASES; PRIONS; SEWAGE; WASTE MANAGEMENT;

MAMMALIA;

EID: 48249106986     PISSN: 0013936X     EISSN: None     Source Type: Journal    
DOI: 10.1021/es703186e     Document Type: Article

References (42)

1. DeArmond, S. J.; Bouzamondo, E. Fundamentals of prion biology and diseases. Toxicol. 2002, 181-182, 9-16.
2. Prusiner, S. B. Novel proteinaceous infectious particles causes scrapie. Science 1982, 216, 136-144.
3. Silveria, J. R.; Raymond, G. J.; Hughson, A. G.; Race, R. E.; Sim, V. L.; Hayes, S. F.; Caughey, B. The most infectious prion protein particles. Nature 2005, 437, 257-261.
4. Prusiner, S. B.; Scott, M.; Foster, D.; Pan, K. M.; Groth, D.; Mirenda, C.; Torchia, M.; Yang, S. L.; Serban, D.; Carlson, G. A. Transgenic studies implicate interactions between homologous PrP isoforms in scrapie prion replication. Cell 1990, 63, 673-686.
5. Caughey, B.; Raymond, G. L. The scrapie-associated form of PrP is made from a cell surface precursor that is both protease-and phospholipase-sensitive. J. Biol. Chem. 1991, 266, 18217-18223.
6. Pan, K. M.; Baldwin, M.; Nguyen, J.; Gasset, M.; Serban, D.; Groth, D.; Mehlhorn, I.; Huang, Z.; Fletterick, R. J.; Cohen, F. E.; Prusiner, S. B. Conversion of alpha-helices into beta-sheets features in the formation of the scrapie prion proteins. Proc. Natl. Acad. Sci. USA 1993, 90, 10962-10966.
7. Prusiner, S. B. Prions. Proc. Natl. Acad. Sci. U. S. A. 1998, 95, 13363-13383.
8. Caughey, B. W.; Dong, A.; Bhat, K. S.; Ernst, D.; Hayes, S. F.; Caughey, W. S. Secondary structure analysis of the scrapie-associated protein PrP 27-30 in water by infrared spectroscopy. Biochem. 1991, 30, 7672-7680.
9. Taylor, D. M. Inactivation of transmissible degenerative encephalopathy agents: a review. Vet. J. 2000, 159, 10-17.
10. Baldwin, M. A. Mass spectrometric analysis of prion proteins. In Advances in Protein Chemistry, Volume 57, Prion Proteins; Caughey, B., Ed.; Academic Press: San Diego, CA, 2001; pp 29-54.
11. Pedersen, J. A.; McMahon, K. D.; Benson, C. H. Prions: Novel pathogens of environmental concern? J. Environ. Eng. 2006, 132, 967-969.
12. Gale, P.; Stanfield, G. Towards a quantitative risk assessment for BSE in sewage sludge. J. Appl. Microbiol. 2001, 91, 563-569.
13. Gale, P.; Young, C.; Stanfield, G.; Oakes, D. Development of a risk assesment for BSE in the aquatic environment. J. App. Microbiol. 1998, 84, 467-477.
14. Yamamoto, T.; Kobayashi, S.; Nishiguchi, A.; Nonaka, T.; Tsutsui, T. Evaluation of bovine spongiform encephalopathy (BSE) infection risk of cattle via sewage sludge from wastewater treatment facilities in slaughterhouses in Japan. J. Vet. Med. Sci. 2006, 68, 137-142.
15. Sc) by the gastrointestinal microbiota of cattle. Vet. Res. 2006, 37, 695-703.
16. Sc in hamster brain homogenates by foodborne bacteria. Syst. Appl. Microbiol. 2006, 29, 165-171.
17. Kirchmayr, R.; Reichl, H. E.; Schildorfer, H.; Braun, R.; Somerville, R. A. Prion protein: detection in 'spiked' anaerobic sludge and degradation experiments under anaerobic conditions. Water Sci. Technol. 2006, 53, 91-98.
18. Johnson, C. J.; Phillips, K. E.; Schramm, P. T.; McKenzie, D.; Aiken, J. M.; Pedersen, J. A. Prions adhere to soil minerals and remain infectious. PLoS Pathogens 2006, 2, 296-302.
19. Silverman, G. J. Sterilization and preservation by ionizing radiation. In Disinfection Sterilization and Preservation, 4th ed.; Block, S. S., Ed.; Lea and Febiger: Philadelphia, PA, 1991; pp 556-579.
20. Wolf, D. C.; Dao, T. H.; Scott, H. D.; Lavy, T. L. Influence of sterilization methods on selected soil microbiological, physical, and chemical properties. J. Environ. Qual. 1989, 18, 39-44.
21. Gautam, S.; Shah, M. R.; Sabharwal, S.; Sharma, A. Gamma irradiation of municipal sludge for safe disposal and agricultural use. Water Environ. Res. 2005, 77, 472-479.
22. Lichstein, H. C. Studies of the effect of sodium azide on microbic growth and respiration: III. The effect of sodium azide on the gas metabolism of B. subtilis and P. aeruginosa and the influence of pyocyanine on the gas exchange of a pyocyanine-free strain of P. aeruginosa in the presence of sodium azide. J. Bacteriol. 1944, 47, 239-251.
23. Lichstein, H. C.; Soule, M. H. Studies of the effect of sodium azide on microbic growth and respiration: I. The action of sodium azide on microbic growth. J. Bacteriol. 1944, 47, 221-230.
24. Lichstein, H. C.; Soule, M. H. Studies of the effect of sodium azide on microbic growth and respiration: II. The action of sodium azide on bacterial catalase. J. Bacteriol. 1944, 47, 231-238.
25. Bessen, R. A.; Marsh, R. F. Identification of two biologically distinct strains of transmissible mink encephalopathy in hamsters. J. Gen. Virol. 1992, 73, 329-334.
26. Lerch, R. N.; Barabarick, K. A.; Azari, P.; Sommers, L. E.; Westfall, D. G. Sewage sludge proteins: I. Extraction methodology. J. Environ. Qual. 1993, 22, 620-624.
27. Bolton, D. C.; Bendheim, P. E.; Marmorstein, A. D.; Potempska, A. Isolation and structural studies of the intact scrapie agent protein. Arch. Biochem. Biophys. 1987, 258, 579-590.
28. Diringer, H.; Hilmert, H.; Simon, D.; Werner, E.; Ehlers, B. Towards purification of the scrapie agent. Eur. J. Biochem. 1983, 134, 555-560.
29. Sc fraction. Biochem. 2006, 45, 15710-15717.
30. Raskin, L.; Zheng, D.; Griffin, M. E.; Stroot, P. G.; Misra, P. Characterization of microbial communities in anaerobic bioreactors using molecular probes. Antonie van Leeuwenhoek 1995, 68, 297-308.
31. Forget, A.; Fredette, V. Sodium azide selective medium for the primary isolation of anaerobic bacteria. J. Bacteriol. 1962, 89, 1217-1223.
32. Shaked, G. M.; Shaked, Y.; Kariv-Inbal, Z.; Halimi, M.; Avraham, I.; Gabizon, R. A protease-resistant prion protein isoform is present in urine of animals and humans affected with prion diseases. J. Biol. Chem. 2001, 276, 31479-31482.
33. Sc as a diagnostic test for sporadic, variant, and familial CJD. Neurology 2005, 64, 1794.
34. Furukawa, H.; Doh-Ura, K.; Okuwaki, R.; Shirabe, S.; Yamamoto, K.; Udono, H.; Ito, T.; Katamine, S.; Niwa, M. Apitfall in diagnosis of human prion diseases using detection of protease-resistant prion protein in urine - Contamination with bacterial outer membrane proteins. J. Biol. Chem. 2004, 279, 23661-23667.
35. Seeger, H.; Heikenwalder, M.; Zeller, N.; Kranich, J.; Schwarz, P.; Gaspert, A.; Burkhardt, S.; Miele, G.; Aguzzi, A. Coincident scrapie infection and nephritis lead to urinary prion excretion. Science 2005, 310, 324-326.
36. Pedersen, N. S.; Smith, E. Prion diseases: Epidemiology in man. APMIS 2002, 110, 14-22.
37. Kimberlin, R. H.; Walker, C. A. Pathogenesis of scrapie in mice after intragastric infection. Virus. Res. 1989, 12, 213-220.
38. LaGoy, P. K. Estimated soil ingestion rates for use in risk assessment. Risk Anal. 1987, 7, 355-359.
39. Johnson, C. J.; Pedersen, J. A.; Chappell, R. J.; McKenzie, D.; Aiken, J. M. Oral transmissibility of prion disease is enhanced by binding to soil particles. PLoS Pathogens 2007, 3, 874-881.
40. Onisko, B.; Dynin, I.; Requena, J. R.; Silva, C. J.; Erickson, M.; Carter, J. M. Mass spectrometric detection of attomole amounts of the prion protein by nanoLC-MS-MS. J. Am. Soc. Mass Spectrom. 2007, 18, 1070-1079.
41. Saá, P.; Castilla, J.; Soto, C. Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J. Biol. Chem. 2006, 281, 35245-35252.
42. Atarashi, R.; Wilham, J. M.; Christensen, L.; Hughson, A. G.; Moore, R. A.; Johnson, L. M.; Onwubiko, H. A.; Priola, S. A.; Caughey, B. Simplified ultrasensitive prion detection by recombinant PrP conversion with shaking. Nature Methods 2008, 5, 211-212.