Deduction of the evaluation limit and termination timing of multi-round protein misfolding cyclic amplification from a titration curve

Microbiology and Immunology

Volumn 55, Issue 7, 2011, Pages 502-509

  Takeuchi, Atsuko ^a   Komiya, Mayumi ^b   Kitamoto, Tetsuyuki ^a   Morita, Masanori ^b  

^a TOHOKU UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^b Benesis Corporation   (Japan)

Author keywords

Disinfectant; Evaluation; Prion; Protein misfolding cyclic amplification

Indexed keywords

DETERGENT; DISINFECTANT AGENT; DODECYL SULFATE SODIUM; PRION PROTEIN; SODIUM HYDROXIDE;

ANALYTIC METHOD; ANIMAL TISSUE; ARTICLE; BIOASSAY; BRAIN INFECTION; CONTROLLED STUDY; DILUTION; MISFOLDING CYCLIC AMPLIFICATION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN DEGRADATION; SCRAPIE; SCRAPIE AGENT; SIGNAL TRANSDUCTION; VALIDATION PROCESS;

ANIMALS; BRAIN CHEMISTRY; CHEMISTRY TECHNIQUES, ANALYTICAL; CRICETINAE; DISINFECTANTS; ENDOPEPTIDASE K; PRIONS; PROTEIN FOLDING; VIROLOGY;

CRICETINAE;

EID: 79959730262     PISSN: 03855600     EISSN: 13480421     Source Type: Journal    
DOI: 10.1111/j.1348-0421.2011.00340.x     Document Type: Article

References (17)

1. Prusiner S.B. (1998) Prions. Proc Natl Acad Sci U S A 95: 13, 363-83.
2. Saborio G.P., Permanne B., Soto C. (2001) Sensitive detection of pathological prion protein by cyclic amplification of protein misfolding. Nature 411: 810-3.
3. Saá P., Castilla J., Soto C. (2006) Ultra-efficient replication of infectious prions by automated protein misfolding cyclic amplification. J Biol Chem 281: 35, 245-52.
4. Castilla J., Saá P., Hetz C., Soto C. (2005) In vitro generation of infectious scrapie prions. Cell 121: 195-206.
5. Murayama Y., Yoshioka M., Horii H., Takata M., Yokoyama T., Sudo T., Sato K., Shinagawa M., Mohri S. (2006) Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation. Biochem Biophys Res Commun 348: 758-62.
6. Suyama K., Yoshioka M., Akagawa M., Murayama Y., Horii H., Takata M., Yokoyama T., Mohri S. (2007) Prion inactivation by the Maillard reaction. Biochem Biophys Res Commun 356: 245-8.
7. World Health Organization. (2000) WHO Infection Control Guidelines for Transmissible Spongiform Encephalopathies.
8. Baier M., Schwarz A., Mielke M. (2004) Activity of an alkaline 'cleaner' in the inactivation of the scrapie agent. J Hosp Infect 57: 80-4.
9. Tateishi J., Tashima T., Kitamoto T. (1988) Inactivation of the Creutzfeldt-Jakob disease agent. Ann Neurol 24: 466.
10. Tateishi J., Tashima T., Kitamoto T. (1991) Practical methods for chemical inactivation of Creutzfeldt-Jakob disease pathogen. Microbiol Immunol 35: 163-6.
11. Ikeda S., Kobayashi A., Kitamoto T. (2008) Thr but Asn of the N-glycosylation sites of PrP is indispensable for its misfolding. Biochem Biophys Res Commun 369: 1195-8.
12. Baier M., Schwarz A., Mielke M. (2004) Activity of an alkaline 'cleaner' in the inactivation of the scrapie agent. J Hosp Infect 57: 80-4.
13. Tamai Y., Taguchi F., Miura S. (1988) Inactivation of the Creutzfeldt-Jakob disease agent. Ann Neurol 24: 466-7.
14. Brown P., Rohwer R.G., Gajdusek D.C. (1986) Newer data on the inactivation of scrapie virus or Creutzfeldt-Jakob disease virus in brain tissue. J Infect Dis 153: 1145-8.
15. Taylor D.M., Fraser H., McConnell I., Brown D.A., Brown K.L., Lamza K.A., Smith G.R. (1994) Decontamination studies with the agents of bovine spongiform encephalopathy and scrapie. Arch Virol 139: 313-26.
16. Deleault N.R., Harris B.T., Rees J.R., Supattapone S. (2007) Formation of native prions from minimal components in vitro. Proc Natl Acad Sci U S A 104: 9741-6.
17. Chen B., Morales R., Barria M.A., Soto C. (2010) Estimating prion concentration in fluids and tissues by quantitative PMCA. Nat Methods 7: 519-20.