期刊论文详细信息
BMC Veterinary Research
Exposure of RML scrapie agent to a sodium percarbonate-based product and sodium dodecyl sulfate renders PrPSc protease sensitive but does not eliminate infectivity
Justin J Greenlee1  Gregory H Foster1  Eric M Nicholson1  Jodi D Smith1 
[1]Virus and Prion Research Unit, National Animal Disease Center, USDA, Agricultural Research Service, 1920 Dayton Ave, Ames, IA 50010, USA
关键词: Sodium percarbonate;    Sodium dodecyl sulfate;    Scrapie;    Prion;    Inactivation;   
Others  :  1119630
DOI  :  10.1186/1746-6148-9-8
 received in 2012-09-18, accepted in 2013-01-08,  发布年份 2013
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【 摘 要 】

Background

Prions, the causative agents of the transmissible spongiform encephalopathies, are notoriously difficult to inactivate. Current decontamination recommendations by the World Health Organization include prolonged exposure to 1 N sodium hydroxide or > 20,000 ppm sodium hypochlorite, or autoclaving. For decontamination of large stainless steel surfaces and equipment as in abattoirs, for example, these methods are harsh or unsuitable. The current study was designed to evaluate the effectiveness of a commercial product containing sodium percarbonate to inactivate prions. Samples of mouse brain infected with a mouse-adapted strain of the scrapie agent (RML) were exposed to a sodium percarbonate-based product (SPC-P). Treated samples were evaluated for abnormal prion protein (PrPSc)-immunoreactivity by western blot analysis, and residual infectivity by mouse bioassay.

Results

Exposure to a 21% solution of SPC-P or a solution containing either 2.1% or 21% SPC-P in combination with sodium dodecyl sulfate (SDS) resulted in increased proteinase K sensitivity of PrPSc. Limited reductions in infectivity were observed depending on treatment condition. A marginal effect on infectivity was observed with SPC-P alone, but an approximate 2–3 log10 reduction was observed with the addition of SDS, though exposure to SDS alone resulted in an approximate 2 log10 reduction.

Conclusions

This study demonstrates that exposure of a mouse-adapted scrapie strain to SPC-P does not eliminate infectivity, but does render PrPSc protease sensitive.

【 授权许可】

   
2013 Smith et al; licensee BioMed Central Ltd.

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【 参考文献 】
  • [1]Prusiner SB: Prions. Proc Nat Acad Sci U S A 1998, 95(23):13363-13383.
  • [2]Bruce ME, Will RG, Ironside JW, McConnell I, Drummond D, Suttie A, McCardle L, Chree A, Hope J, Birkett C, Cousens S, Fraser H, Bostock CJ: Transmissions to mice indicate that ‘new variant’ CJD is caused by the BSE agent. Nature 1997, 389(6650):498-501.
  • [3]Collinge J, Sidle KC, Meads J, Ironside J, Hill AF: Molecular analysis of prion strain variation and the aetiology of ‘new variant’ CJD. Nature 1996, 383(6602):685-690.
  • [4]Wilesmith JW, Wells GA, Cranwell MP, Ryan JB: Bovine spongiform encephalopathy: epidemiological studies. Vet Rec 1988, 123(25):638-644.
  • [5]Detwiler LA, Baylis M: The epidemiology of scrapie. Rev Sci Tech 2003, 22(1):121-143.
  • [6]Sigurdson CJ: A prion disease of cervids: chronic wasting disease. Vet Res 2008, 39(4):41.
  • [7]Taylor DM: Inactivation of transmissible degenerative encephalopathy agents: A review. Vet J 2000, 159(1):10-17.
  • [8]WHO: WHO infection control guidelines for transmissible spongiform encephalopathies. Geneva: WHO/CDS/CSR/APH/20003; 1999:29-32.
  • [9]Pilon JL, Nash PB, Arver T, Hoglund D, Vercauteren KC: Feasibility of infectious prion digestion using mild conditions and commercial subtilisin. J Virol Methods 2009, 161(1):168-172.
  • [10]McLeod AH, Murdoch H, Dickinson J, Dennis MJ, Hall GA, Buswell CM, Carr J, Taylor DM, Sutton JM, Raven ND: Proteolytic inactivation of the bovine spongiform encephalopathy agent. Biochem Biophys Res Comm 2004, 317(4):1165-1170.
  • [11]Peretz D, Supattapone S, Giles K, Vergara J, Freyman Y, Lessard P, Safar JG, Glidden DV, McCulloch C, Nguyen HO, Scott M, DeArmond SJ, Prusiner SB: Inactivation of prions by acidic sodium dodecyl sulfate. J Virol 2006, 80(1):322-331.
  • [12]Yao HL, Han J, Gao JM, Zhang J, Zhang BY, Guo YJ, Nie K, Gao C, Wang XF, Dong XP: Comparative study of the effects of several chemical and physical treatments on the activity of protease resistance and infectivity of scrapie strain 263 K. J Vet Med B, Infect Dis Vet Public Health 2005, 52(10):437-443.
  • [13]Fichet G, Antloga K, Comoy E, Deslys JP, McDonnell G: Prion inactivation using a new gaseous hydrogen peroxide sterilisation process. J Hosp Infect 2007, 67(3):278-286.
  • [14]Solassol J, Pastore M, Crozet C, Perrier V, Lehmann S: A novel copper-hydrogen peroxide formulation for prion decontamination. J Infect Dis 2006, 194(6):865-869.
  • [15]Fichet G, Comoy E, Duval C, Antloga K, Dehen C, Charbonnier A, McDonnell G, Brown P, Lasmezas CI, Deslys JP: Novel methods for disinfection of prion-contaminated medical devices. Lancet 2004, 364(9433):521-526.
  • [16]Walker AS, Inderlied CB, Kingsbury DT: Conditions for the chemical and physical inactivation of the K. Fu. strain of the agent of Creutzfeldt-Jakob disease. Am J Public Health 1983, 73(6):661-665.
  • [17]Millson GC, Hunter GD, Kimberlin RH: The physico-chemical nature of the scrapie agent. In Slow Virus Diseases of Animals and Man. Volume 44. Edited by Kimberlin RH. Amsterdam: North-Holland; 1976:243-264.
  • [18]Fischer M, Rulicke T, Raeber A, Sailer A, Moser M, Oesch B, Brandner S, Aguzzi A, Weissmann C: Prion protein (PrP) with amino-proximal deletions restoring susceptibility of PrP knockout mice to scrapie. EMBO J 1996, 15(6):1255-1264.
  • [19]Brown P, Rohwer RG, Gajdusek DC: Newer data on the inactivation of scrapie virus or Creutzfeldt-Jakob disease virus in brain tissue. J Infect Dis 1986, 153(6):1145-1148.
  • [20]Taylor DM, Fraser H, McConnell I, Brown DA, Brown KL, Lamza KA, Smith GR: Decontamination studies with the agents of bovine spongiform encephalopathy and scrapie. Arch Virol 1994, 139(3–4):313-326.
  • [21]Unal A, Thyer J, Uren E, Middleton D, Braun M, Maher D: Investigation by bioassay of the efficacy of sodium hydroxide treatment on the inactivation of mouse-adapted scrapie. Biologicals 2007, 35(3):161-164.
  • [22]Bruederle CE, Hnasko RM, Kraemer T, Garcia RA, Haas MJ, Marmer WN, Carter JM: Prion infected meat-and-bone meal is still infectious after biodiesel production. PLoS ONE 2008, 3(8):e2969.
  • [23]Miyazawa K, Emmerling K, Manuelidis L: High CJD infectivity remains after prion protein is destroyed. J Cell Biochem 2011, 112(12):3630-3637.
  • [24]Smith JD, Greenlee JJ, Foster GH, Nicholson EM: Acetone precipitation of the scrapie agent results in successful recovery of PrPSc but decreased infectivity. J Agric Food Chem 2012, 60(18):4758-4762.
  • [25]Manuelidis L: A 25 nm virion is the likely cause of transmissible spongiform encephalopathies. J Cell Biochem 2007, 100(4):897-915.
  • [26]Gonzalez L, Thorne L, Jeffrey M, Martin S, Spiropoulos J, Beck KE, Lockey RW, Vickery CM, Holder T, Terry L: Infectious titres of sheep scrapie and bovine spongiform encephalopathy agents cannot be accurately predicted from quantitative laboratory test results. J Gen Virol 2012, 93(Pt 11):2518-2527.
  • [27]Gambetti P, Dong Z, Yuan J, Xiao X, Zheng M, Alshekhlee A, Castellani R, Cohen M, Barria MA, Gonzalez-Romero D, Belay ED, Schonberger LB, Marder K, Harris C, Burke JR, Montine T, Wisniewski T, Dickson DW, Soto C, Hulette CM, Mastrianni JA, Kong Q, Zou WQ: A novel human disease with abnormal prion protein sensitive to protease. Ann Neurol 2008, 63(6):697-708.
  • [28]Head MW, Knight R, Zeidler M, Yull H, Barlow A, Ironside JW: A case of protease sensitive prionopathy in a patient in the UK. Neuropathol Applied Neurobiol 2009, 35(6):628-632.
  • [29]Giles K, Glidden DV, Beckwith R, Seoanes R, Peretz D, DeArmond SJ, Prusiner SB: Resistance of bovine spongiform encephalopathy (BSE) prions to inactivation. PLoS Pathog 2008, 4(11):e1000206.
  • [30]Lax AJ, Millson GC, Manning EJ: Can scrapie titres be calculated accurately from incubation periods? J Gen Virol 1983, 64(Pt 4):971-973.
  • [31]Taylor DM, Fernie K: Exposure to autoclaving or sodium hydroxide extends the dose–response curve of the 263 K strain of scrapie agent in hamsters. J Gen Virol 1996, 77(Pt 4):811-813.
  • [32]Yun SW, Gerlach M, Riederer P, Klein MA: Oxidative stress in the brain at early preclinical stages of mouse scrapie. Exp Neurol 2006, 201(1):90-98.
  • [33]Pamplona R, Naudi A, Gavin R, Pastrana MA, Sajnani G, Ilieva EV, Del Rio JA, Portero-Otin M, Ferrer I, Requena JR: Increased oxidation, glycoxidation, and lipoxidation of brain proteins in prion disease. Free Rad Biol Med 2008, 45(8):1159-1166.
  • [34]Singh N, Singh A, Das D, Mohan ML: Redox control of prion and disease pathogenesis. Antioxid Redox Signal 2010, 12(11):1271-1294.
  • [35]Brown P, Rohwer RG, Green EM, Gajdusek DC: Effect of chemicals, heat, and histopathologic processing on high-infectivity hamster-adapted scrapie virus. J Infect Dis 1982, 145(5):683-687.
  • [36]Brown P, Gibbs CJ Jr, Amyx HL, Kingsbury DT, Rohwer RG, Sulima MP, Gajdusek DC: Chemical disinfection of Creutzfeldt-Jakob disease virus. New Engl J Med 1982, 306(21):1279-1282.
  • [37]Taylor DM: Resistance of the ME7 scrapie agent to peracetic acid. Vet Microbiol 1991, 27(1):19-24.
  • [38]Chandler RL: Encephalopathy in mice produced by inoculation with scrapie brain material. Lancet 1961, 1(7191):1378-1379.
  • [39]Fraser H, Dickinson AG: The sequential development of the brain lesion of scrapie in three strains of mice. J Comp Pathol 1968, 78(3):301-311.
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