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Research Paper

Rapid chemical decontamination of infectious CJD and scrapie particles parallels treatments known to disrupt microbes and biofilms

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Pages 787-801 | Received 17 Apr 2015, Accepted 16 Sep 2015, Published online: 14 Dec 2015

References

  • Prusiner SB. Molecular biology of prion diseases. Science 1991; 252:1515-22; PMID:1675487; http://dx.doi.org/10.1126/science.1675487
  • Prusiner S. Prions. Proc Natl Acad Sci USA 1998; 95:13363-83; PMID:9811807; http://dx.doi.org/10.1073/pnas.95.23.13363
  • Manuelidis L, Chakrabarty T, Miyazawa K, Nduom NA, Emmerling K. The kuru infectious agent is a unique geographic isolate distinct from Creutzfeldt-Jakob disease and scrapie agents. Proc Natl Acad Sci U S A 2009; 106:13529-34; PMID:19633190; http://dx.doi.org/10.1073/pnas.0905825106
  • Manuelidis L. Infectious particles, stress, and induced prion amyloids: a unifying perspective. Virulence 2013; 4:373-83; PMID:23633671; http://dx.doi.org/10.4161/viru.24838
  • Kimberlin RH, Walker CA, Fraser H. The genomic identity of different strains of mouse scrapie is expressed in hamsters and preserved on reisolation in mice. J Gen Virol 1989; 70:2017-25; PMID:2504883; http://dx.doi.org/10.1099/0022-1317-70-8-2017
  • Manuelidis L, Lu ZY. Virus-like interference in the latency and prevention of Creutzfeldt-Jakob disease. Proc Natl Acad Sci USA 2003; 100:5360-5; PMID:12692308; http://dx.doi.org/10.1073/pnas.0931192100
  • Liu Y, Sun R, Chakrabarty T, Manuelidis L. A rapid accurate culture assay for infectivity in Transmissible Encephalopathies. J Neurovirol 2008; 14:352-61; PMID:18989813; http://dx.doi.org/10.1080/13550280802105283
  • Edgeworth JA, Jackson GS, Clarke AR, Weissmann C, Collinge J. Highly sensitive, quantitative cell-based assay for prions adsorbed to solid surfaces. Proc Natl Acad Sci U S A 2009; 106:3479-83; PMID:19204279; http://dx.doi.org/10.1073/pnas.0813342106
  • Manuelidis L. A 25 nm virion is the likely cause of Transmissible Spongiform Encephalopathies. J Cell Biochem 2007; 100:897-915; PMID:17044041; http://dx.doi.org/10.1002/jcb.21090
  • Timmes AG, Moore RA, Fischer ER, Priola SA. Recombinant prion protein refolded with lipid and RNA has the biochemical hallmarks of a prion but lacks in vivo infectivity. PLoS One 2013; 8:e71081; PMID:23936256; http://dx.doi.org/10.1371/journal.pone.0071081
  • Ladner-Keay CL, Griffith BJ, Wishart DS. Shaking alone induces de novo conversion of recombinant prion proteins to β-sheet rich oligomers and fibrils. PLoS One 2014; 9:e98753; PMID:24892647; http://dx.doi.org/10.1371/journal.pone.0098753
  • Miyazawa K, Kipkorir T, Tittman S, Manuelidis L. Continuous production of prions after infectious particles are eliminated: implications for Alzheimer's disease. PLoS One 2012; 7:e35471; PMID:22509412; http://dx.doi.org/10.1371/journal.pone.0035471
  • Simoneau S, Thomzig A, Ruchoux MM, Vignier N, Daus ML, Poleggi A, Lebon P, Freire S, Durand V, Graziano S, et al. Synthetic Scrapie Infectivity: Interaction between Recombinant PrP and Scrapie Brain-Derived RNA. Virulence 2015; 6:132-44
  • Manuelidis L, Yu ZX, Barquero N, Mullins B. Cells infected with scrapie and Creutzfeldt-Jakob disease agents produce intracellular 25-nm virus-like particles. Proc Natl Acad Sci USA 2007; 104:1965-70; PMID:17267596; http://dx.doi.org/10.1073/pnas.0610999104
  • Bignami A, Parry H. Aggregations of 35-nanometer particles associated with neuronal cytopathic changes in natural scrapie. Science 1971; 171:389-90; PMID:5099604; http://dx.doi.org/10.1126/science.171.3969.389
  • David-Ferreira J, David-Ferreira K, Gibbs C, Morris J. Scrapie in mice: ultrastructural observations in the cerebral cortex. Proc Soc Exp Biol Med 1968; 127:313-20; PMID:5689462; http://dx.doi.org/10.3181/00379727-127-32680
  • Liberski P, Jeffrey M. Tubulovesicular structures—the ultrastructural hallmark for transmissible spongiform encephalopathies (prion diseases). Folia Neuropathologica 2004; 42 Supplement B:96-108; PMID:16903145
  • 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 Commun 2004; 317:1165-70; PMID:15094392; http://dx.doi.org/10.1016/j.bbrc.2004.03.168
  • Miyazawa K, Emmerling K, Manuelidis L. High CJD infectivity remains after prion protein is destroyed. J Cell Biochem 2011; 112:3630-7; PMID:21793041; http://dx.doi.org/10.1002/jcb.23286
  • Kipkorir T, Tittman S, Botsios S, Manuelidis L. Highly Infectious CJD Particles Lack Prion Protein but Contain Many Viral-Linked Peptides by LC-MS/MS. J Cell Biochem 2014; 115:2012-21; PMID:24933657
  • McDonnell G, Dehen C, Perrin A, Thomas V, Igel-Egalon A, Burke PA, Deslys JP, Comoy E. Cleaning, disinfection and sterilization of surface prion contamination. J Hospital Infect 2013; 85:268-73; PMID:24074640; http://dx.doi.org/10.1016/j.jhin.2013.08.003
  • Jackson GS, McKintosh E, Flechsig E, Prodromidou K, Hirsch P, Linehan J, Brandner S, Clarke AR, Weissmann C, Collinge J. An enzyme-detergent method for effective prion decontamination of surgical steel. J General Virol 2005; 86:869-78; PMID:15722550; http://dx.doi.org/10.1099/vir.0.80484-0
  • Jeffrey M, Gonzalez L, Espenes A, Press C, Martin S, Chaplin M, Davis L, Landsverk T, MacAldowie C, Eaton S, et al. Transportation of prion protein across the intestinal mucosa of scrapie-susceptible and scrapie-resistant sheep. J Pathol 2006; 209:4-14; PMID:16575799; http://dx.doi.org/10.1002/path.1962
  • Scherbel C, Pichner R, Groschup MH, Mueller-Hellwig S, Scherer S, Dietrich R, Maertlbauer E, Gareis M. Infectivity of Scrapie Prion Protein (PrPSc) Following In vitro Digestion with Bovine Gastrointestinal Microbiota. Zoonoses Public Health 2007; 54:185-90; PMID:17542960; http://dx.doi.org/10.1111/j.1863-2378.2007.01040.x
  • Dobie K, Barron R. Dissociation between transmissible spongiform encephalopathy (TSE) infectivity and proteinase K-resistant PrP(Sc) levels in peripheral tissue from a murine transgenic model of TSE disease. J Virol 2013; 87:5895-903; PMID:23487470; http://dx.doi.org/10.1128/JVI.03469-12
  • Barron RM, Campbell SL, King D, Bellon A, Chapman KE, Williamson RA, Manson JC. High titers of transmissible spongiform encephalopathy infectivity associated with extremely low levels of PrPSc in vivo. J Biol Chem 2007; 282:35878-86; PMID:17923484; http://dx.doi.org/10.1074/jbc.M704329200
  • Baker CA, Martin D, Manuelidis L. Microglia from CJD brain are infectious and show specific mRNA activation profiles. J Virol 2002; 76:10905-13; PMID:12368333; http://dx.doi.org/10.1128/JVI.76.21.10905-10913.2002
  • Hawkins SA, Simmons HA, Gough KC, Maddison BC. Persistence of ovine scrapie infectivity in a farm environment following cleaning and decontamination. Vet Rec 2015; 176:99; PMID:25362003; http://dx.doi.org/10.1136/vr.102743
  • Bernoulli C, Siegfried J, Baumgartner G, Regli F, Rabinowicz T, Gajdusek DC, CJ G. Danger of accidental person-to-person transmission of Creutzfeldt-Jakob disease by surgery. Lancet 1977; 8009:478-9; http://dx.doi.org/10.1016/S0140-6736(77)91958-4
  • Will RG. Acquired prion disease: iatrogenic CJD, variant CJD, kuru. Br Med Bull 2003; 66:255-65; PMID:14522863; http://dx.doi.org/10.1093/bmb/66.1.255
  • Manuelidis L. Decontamination of Creutzfeldt-Jakob Disease and other transmissible agents. J NeuroVirol 1997; 3:62-5; PMID:9147822; http://dx.doi.org/10.3109/13550289709015793
  • Peretz D, Supattapone S, Giles K, Vergara J, Freyman Y, Lessard P, Safar JG, Glidden DV, McCulloch C, Nguyen HO, et al. Inactivation of prions by acidic sodium dodecyl sulfate. J Virol 2006; 80:322-31; PMID:16352557; http://dx.doi.org/10.1128/JVI.80.1.322-331.2006
  • Eisler P. Deadly bacteria outbreak inflames disinfection concerns. USA Today 2015
  • CDC. Healthcare Infection Control Practices Advisory Committee (HICPAC);Concerns. Centers for Disease Control and Infection 2009
  • Radebold K, Chernyak M, Martin D, Manuelidis L. Blood borne transit of CJD from brain to gut at early stages of infection. BMC Infect Dis 2001; 1:20-5; PMID:11716790; http://dx.doi.org/10.1186/1471-2334-1-20
  • Shlomchik MJ, Radebold K, Duclos N, Manuelidis L. Neuroinvasion by a Creutzfeldt-Jakob disease agent in the absence of B cells and follicular dendritic cells. Proc Natl Acad Sci U S A 2001; 98:9289-94; PMID:11470899; http://dx.doi.org/10.1073/pnas.161055198
  • McKinnon D. Thirty new cases of Hepatitis B found. All had EEGs at six clinics, officials say. Toronto Star 1996: SC4
  • Gabizon R, McKinley MP, Prusiner SB. Purified prion proteins and scrapie infectivity copartition into liposomes. Proc Natl Acad Sci U S A 1987; 84:4017-21; PMID:3108886; http://dx.doi.org/10.1073/pnas.84.12.4017
  • Prusiner SB, Groth D, Serban A, Stahl N, Gabizon R. Attempts to restore scrapie prion infectivity after exposure to protein denaturants. Proc Natl Acad Sci 1993; 90:2793-7; PMID:8464892; http://dx.doi.org/10.1073/pnas.90.7.2793
  • Prusiner SB, Groth DF, Bolton DC, Kent SB, Hood LE. Purification and structural studies of a major scrapie prion protein. Cell 1984; 38:127-34; PMID:6432339; http://dx.doi.org/10.1016/0092-8674(84)90533-6
  • Manuelidis L, Sklaviadis T, Akowitz A, Fritch W. Viral particles are required for infection in neurodegenerative Creutzfeldt-Jakob disease. Proc Natl Acad Sci (USA) 1995; 92:5124-8; http://dx.doi.org/10.1073/pnas.92.11.5124
  • Nishida N, Katamine S, Manuelidis L. Reciprocal interference between specific CJD and scrapie agents in neural cell cultures. Science 2005; 310:493-6; PMID:16239476; http://dx.doi.org/10.1126/science.1118155
  • Arjona A, Simarro L, Islinger F, Nishida N, Manuelidis L. Two Creutzfeldt-Jakob disease agents reproduce prion protein-independent identities in cell cultures. Proc Natl Acad Sci USA 2004; 101:8768-73; PMID:15161970; http://dx.doi.org/10.1073/pnas.0400158101
  • Sun R, Liu Y, Zhang H, Manuelidis L. Quantitative recovery of scrapie agent with minimal protein from highly infectious cultures. Viral Immunol 2008; 21:293-302; PMID:18788938; http://dx.doi.org/10.1089/vim.2008.0039
  • Manuelidis L. Nuclease resistant circular DNAs copurify with infectivity in scrapie and CJD. J Neurovirol 2011; 17:131-45; PMID:21165784; http://dx.doi.org/10.1007/s13365-010-0007-0
  • Kipkorir T, Colangelo CM, Manuelidis L. Proteomic analysis of host brain components that bind to infectious particles in Creutzfeldt-Jakob disease. Proteomics 2015; 15:2983-98; PMID:25930988
  • Klug CS, Su W, Liu J, Klebba PE, Feix JB. Denaturant unfolding of the ferric enterobactin receptor and ligand-induced stabilization studied by site-directed spin labeling. Biochemistry 1995; 34:14230-6; PMID:7578022; http://dx.doi.org/10.1021/bi00043a030
  • Hong H, Tamm LK. Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc Natl Acad Sci U S A 2004; 101:4065-70; PMID:14990786; http://dx.doi.org/10.1073/pnas.0400358101
  • Gordon JA, Jencks WP. The relationship of structure to the effectiveness of denaturing agents for proteins. Biochemistry 1963; 2:47-57; PMID:13949214; http://dx.doi.org/10.1021/bi00901a011
  • Miyazawa K, Emmerling K, Manuelidis L. Replication and spread of CJD, kuru and scrapie agents in vivo and in cell culture. Virulence 2011; 2:188-99; PMID:21527829; http://dx.doi.org/10.4161/viru.2.3.15880
  • Rabilloud T. Use of thiourea to increase the solubility of membrane proteins in two-dimensional electrophoresis. Electrophoresis 1998; 19:758-60; PMID:9511858
  • Natarajan S, Xu C, Caperna TJ, Garrett WM. Comparison of protein solubilization methods suitable for proteomic analysis of soybean seed proteins. Anal Biochem 2005; 342:214-20; PMID:15953580; http://dx.doi.org/10.1016/j.ab.2005.04.046
  • Riesner D, Kellings K, Post K, Wille H, Serban H, Groth D, Baldwin MA, Prusiner SB. Disruption of prion rods generates 10-nm spherical particles having high a-helical content and lacking scrapie infectivity. J Virol 1996; 70:1714-22; PMID:8627692
  • Okoroma EA, Purchase D, Garelick H, Morris R, Neale MH, Windl O, Abiola OO. Enzymatic formulation capable of degrading scrapie prion under mild digestion conditions. PLoS One 2013; 8:e68099; PMID:23874511; http://dx.doi.org/10.1371/journal.pone.0068099
  • Millson G, Hunter G, Kimberlin R. The physico-chemical nature of the scrapie agent. In: Kimberlin R, ed. Slow virus diseases of animals and man. Amsterdam: North-Holland, 1976:243-66
  • Nakamura A, Mrimoto M, Takeuchi K, Fujii T. A Rapid Extraction Procedure of Human Hair Proteins and Identification of Phosphorylated Species. Biol Pharm Bull 2002; 25:569-72; PMID:12033494; http://dx.doi.org/10.1248/bpb.25.569
  • Koga Y, Tanaka S, Sakudo A, Tobiume M, Aranishi M, Hirata A, Takano K, Ikuta K, Kanaya S. Proteolysis of abnormal prion protein with a thermostable protease from Thermococcus kodakarensis KOD1. Appl Microbiol Biotechnol 2014; 98:2113-20; PMID:23880875; http://dx.doi.org/10.1007/s00253-013-5091-7
  • Emadi S, Behzadi M. A comparative study on the aggregating effects of guanidine thiocyanate, guanidine hydrochloride and urea on lysozyme aggregation. Biochem Biophys Res Commun 2014; 450:1339-44; PMID: 25003319; http://dx.doi.org/10.1016/j.bbrc.2014.06.133
  • Caughey B, Raymond GJ, Kocisko DA, Lansbury PT, Jr. Scrapie infectivity correlates with converting activity, protease resistance, and aggregation of scrapie-associated prion protein in guanidine denaturation studies. J Virol 1997; 71:4107-10; PMID:9094691
  • Walker JT, Dickinson J, Sutton JM, Raven ND, Marsh PD. Cleanability of dental instruments–implications of residual protein and risks from Creutzfeldt-Jakob disease. British Dental J 2007; 203:395-401; PMID:17934424; http://dx.doi.org/10.1038/bdj.2007.893
  • Singh S, Zlotnick A. Observed hysteresis of virus capsid disassembly is implicit in kinetic models of assembly. J Biol Chem 2003; 278:18249-55; PMID:12639968; http://dx.doi.org/10.1074/jbc.M211408200
  • Lee KW, Tan WS. Recombinant hepatitis B virus core particles: association, dissociation and encapsidation of green fluorescent protein. J Virol Methods 2008; 151:172-80; PMID:18584885; http://dx.doi.org/10.1016/j.jviromet.2008.05.025
  • Philipson L, Beatrice ST, Crowell RL. A structural model for picornaviruses as suggested from an analysis of urea-degraded virions and procapsids of coxsackievirus B3. Virol 1973; 54:69-79; PMID:4351615; http://dx.doi.org/10.1016/0042-6822(73)90115-3
  • Exner M, Tuschewitzki GJ, Scharnagel J. Influence of biofilms by chemical disinfectants and mechanical cleaning. Zentralbl Bakteriol Mikrobiol Hyg B 1987; 183:549-63; PMID:3109156
  • Mayer C, Moritz R, Kirschner C, Borchard W, Maibaum R, Wingender J, Flemming HC. The role of intermolecular interactions: studies on model systems for bacterial biofilms. Int J Biol Macromol 1999; 26:3-16; PMID:10520951; http://dx.doi.org/10.1016/S0141-8130(99)00057-4
  • Di Maio F, Yu X, Resen, E, Krupovic M, Prangishvili D, Egelman E. Virology. A virus that infects a hyperthermophile encapsidates A-form DNA. Science 2015; 348:914-7; PMID:25999507; http://dx.doi.org/10.1126/science.aaa4181
  • Manuelidis L, Fritch W, Xi YG. Evolution of a strain of CJD that induces BSE-like plaques. Science 1997; 277:94-8; PMID:9204907; http://dx.doi.org/10.1126/science.277.5322.94
  • Sklaviadis TL, Manuelidis EE, Manuelidis L. Physical properties of the Creutzfeldt-Jakob disease agent. J Virol 1989; 63:1212-22; PMID:2492609

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