Decontamination of prion protein (BSE301V) using a genetically engineered protease

Journal of Hospital Infection

Volumn 72, Issue 1, 2009, Pages 65-70

  Dickinson, J ^a   Murdoch, H ^a   Dennis, M J ^a   Hall, G A ^a   Bott, R ^b   Crabb, W D ^b   Penet, C ^b   Sutton, J M ^a   Raven, N D H ^a  

^a PUBLIC HEALTH ENGLAND   (United Kingdom)

^b Danisco US Inc   (United States)

Author keywords

Bacillus lentus subtilisin; Bovine spongiform encephalopathy; Inactivation processes; Variant Creutzfeldt Jakob disease

Indexed keywords

ALKALINE PROTEINASE; PRION PROTEIN; PROTEINASE K;

ANIMAL EXPERIMENT; ANIMAL MODEL; ARTICLE; BOVINE SPONGIFORM ENCEPHALOPATHY; BRAIN HOMOGENATE; CONTROLLED STUDY; EGGERTHELLA LENTA; ENZYME KINETICS; GENETIC ENGINEERING; MOUSE; NONHUMAN; PH; SURVIVAL RATE; THERMOSTABILITY; VIRUS INACTIVATION;

ANIMALS; BACILLUS; CATTLE; DECONTAMINATION; ENCEPHALOPATHY, BOVINE SPONGIFORM; HYDROGEN-ION CONCENTRATION; KINETICS; MICE; PRIONS; RECOMBINANT PROTEINS; SUBTILISIN; SURVIVAL ANALYSIS;

EID: 63249118899     PISSN: 01956701     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jhin.2008.12.007     Document Type: Article

References (39)

1. Ironside J.W., Bishop M.T., Connolly K., et al. Variant Creutzfeldt-Jakob disease: prion protein genotype analysis of positive appendix tissue samples from a retrospective prevalence study. Br Med J 332 (2006) 1186-1188
2. Hilton D.A., Ghani A.C., Conyers L., et al. Prevalence of lymphoreticular prion protein accumulation in UK tissue samples. J Pathol 203 (2004) 733-739
3. Peden A.H., Head M.W., Ritchie D.L., Bell J.E., and Ironside J.W. Preclinical vCJD after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet 364 (2004) 527-529
4. Bishop M.T., Hart P., Aitchison L., et al. Predicting susceptibility and incubation time of human-to-human transmission of vCJD. Lancet Neurol 5 (2006) 393-398
5. Wadsworth J.D., Asante E.A., Desbruslais M., et al. Human prion protein with valine 129 prevents expression of variant CJD phenotype. Science 306 (2004) 1793-1796
6. Head M.W., Ritchie D., Smith N., et al. Peripheral tissue involvement in sporadic, iatrogenic, and variant Creutzfeldt-Jakob disease: an immunohistochemical, quantitative, and biochemical study. Am J Pathol 164 (2004) 143-153
7. Herzog C., Sales N., Etchegaray N., et al. Tissue distribution of bovine spongiform encephalopathy agent in primates after intravenous or oral infection. Lancet 363 (2004) 422-428
8. Llewelyn C.A., Hewitt P.E., Knight R.S., et al. Possible transmission of variant Creutzfeldt-Jakob disease by blood transfusion. Lancet 363 (2004) 417-421
9. Wroe S.J., Pal S., Siddique D., et al. Clinical presentation and pre-mortem diagnosis of variant Creutzfeldt-Jakob disease associated with blood transfusion: a case report. Lancet 368 (2006) 2061-2067
10. Bernoulli C., Siegfried J., Baumgartner G., et al. Danger of accidental person-to-person transmission of Creutzfeldt-Jakob disease by surgery. Lancet 1 (1977) 478-479
11. Brown P., Preece M., Brandel J.P., et al. Iatrogenic Creutzfeldt-Jakob disease at the millennium. Neurology 55 (2000) 1075-1081
12. Anonymous. Leads from the MMWR. Update: Creutzfeldt-Jakob disease in a patient receiving a cadaveric dura mater graft. J Am Med Assoc 258 (1987) 309-310
13. Brooke F.J., Boyd A., Klug G.M., Masters C.L., and Collins S.J. Lyodura use and the risk of iatrogenic Creutzfeldt-Jakob disease in Australia. Med J Aust 180 (2004) 177-181
14. Swerdlow A.J., Higgins C.D., Adlard P., Jones M.E., and Preece M.A. Creutzfeldt-Jakob disease in United Kingdom patients treated with human pituitary growth hormone. Neurology 61 (2003) 783-791
15. Collins S., Law M.G., Fletcher A., Boyd A., Kaldor J., and Masters C.L. Surgical treatment and risk of sporadic Creutzfeldt-Jakob disease: a case-control study. Lancet 353 (1999) 693-697
16. Ward H.J., Everington D., Croes E.A., et al. Sporadic Creutzfeldt-Jakob disease and surgery: a case-control study using community controls. Neurology 59 (2002) 543-548
17. Peden A.H., Ritchie D.L., Head M.W., and Ironside J.W. Detection and localization of PrPSc in the skeletal muscle of patients with variant, iatrogenic, and sporadic forms of Creutzfeldt-Jakob disease. Am J Pathol 168 (2006) 927-935
18. Herzog C., Riviere J., Lescoutra-Etchegaray N., et al. PrPTSE distribution in a primate model of variant, sporadic, and iatrogenic Creutzfeldt-Jakob disease. J Virol 79 (2005) 14339-14345
19. Taylor D. Practical aspects of decontamination of the unconventional transmissible agents that cause sporadic and variant Creutzfeldt-Jakob disease and other similar human diseases. Ig Sanita Pubbl 60 (2004) 141-150
20. Peretz D., Supattapone S., Giles K., et al. Inactivation of prions by acidic sodium dodecyl sulfate. J Virol 80 (2006) 322-331
21. Anonymous. WHO infection control guidelines for transmissible spongiform encephalopathies. Report of a WHO Consultation, Geneva, Switzerland, 23-26 March 1999. HO/CDS/CSR/APH/2000.3. Geneva: WHO.
22. McLeod A.H., Murdoch H., Dickinson J., et al. Proteolytic inactivation of the bovine spongiform encephalopathy agent. Biochem Biophys Res Commun 317 (2004) 1165-1170
23. 1′ binding sites. J Am Chem Soc 113 (1991) 1026-1030
24. Graycar T.P., Bott R.R., Caldwell R.M., et al. Altering the proteolytic activity of subtilisin through protein engineering. Ann NY Acad Sci 672 (1992) 71-79
25. Lawson V.A., Stewart J.D., and Masters C.L. 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 (2007) 2905-2914
26. Muller-Hellwig S., Groschup M.H., Pichner R., et al. Biochemical evidence for the proteolytic degradation of infectious prion protein PrPsc in hamster brain homogenates by foodborne bacteria. Syst Appl Microbiol 29 (2006) 165-171
27. Yoshioka M., Murayama Y., Miwa T., et al. Assessment of prion inactivation by combined use of Bacillus-derived protease and SDS. Biosci Biotechnol Biochem 71 (2007) 2565-2568
28. Jackson G.S., McKintosh E., Flechsig E., et al. An enzyme-detergent method for effective prion decontamination of surgical steel. J Gen Virol 86 (2005) 869-878
29. Tsiroulnikov K., Rezai H., Bonch-Osmolovskaya E., et al. Hydrolysis of the amyloid prion protein and nonpathogenic meat and bone meal by anaerobic thermophilic prokaryotes and streptomyces subspecies. J Agric Food Chem 52 (2004) 6353-6360
30. Fichet G., Comoy E., Dehen C., et al. Investigations of a prion infectivity assay to evaluate methods of decontamination. J Microbiol Methods 70 (2007) 511-518
31. Lemmer K., Mielke M., Kratzel C., et al. Decontamination of surgical instruments from prions. II. In vivo findings with a model system for testing the removal of scrapie infectivity from steel surfaces. J Gen Virol 89 (2008) 348-358
32. Fichet G., Comoy E., Duval C., et al. Novel methods for disinfection of prion-contaminated medical devices. Lancet 364 (2004) 521-526
33. Fichet G., Antloga K., Comoy E., Deslys J.P., and McDonnell G. Prion inactivation using a new gaseous hydrogen peroxide sterilisation process. J Hosp Infect 67 (2007) 278-286
34. Baxter H.C., Campbell G.A., Whittaker A.G., et al. Elimination of transmissible spongiform encephalopathy infectivity and decontamination of surgical instruments by using radio-frequency gas-plasma treatment. J Gen Virol 86 (2005) 2393-2399
35. Yan Z.X., Stitz L., Heeg P., Pfaff E., and Roth K. Infectivity of prion protein bound to stainless steel wires: a model for testing decontamination procedures for transmissible spongiform encephalopathies. Infect Control Hosp Epidemiol 25 (2004) 280-283
36. Taylor D.M., Fernie K., Steele P.J., McConnell I., and Somerville R.A. 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 (2002) 3199-3204
37. Kuczius T., and Groschup M.H. Differences in proteinase K resistance and neuronal deposition of abnormal prion proteins characterize bovine spongiform encephalopathy (BSE) and scrapie strains. Mol Med 5 (1999) 406-418
38. Zobeley E., Flechsig E., Cozzio A., Enari M., and Weissmann C. Infectivity of scrapie prions bound to a stainless steel surface. Mol Med 5 (1999) 240-243
39. Langeveld J.P., Wang J.J., Van de Wiel D.F., et al. Enzymatic degradation of prion protein in brain stem from infected cattle and sheep. J Infect Dis 188 (2003) 1782-1789