Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation

Murayama, Yuichi; Yoshioka, Miyako; Horii, H.; Takata, Masuhiro; Yokoyama, Takashi; Sudo, Takashi; Sato, Koichi; Shinagawa, Morikazu; Mohri, Satoshi

doi:10.1016/j.bbrc.2006.07.130

Cited by 33 publications

(24 citation statements)

References 14 publications

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“…The PMCA assay has a wide dynamic range of sensitivity (31). This assay considerably reduces the time required for generating results (i.e., 3 days) compared to animal bioassay models (several months to more than a year), and studies examining heat sterilization of PrP Sc demonstrated that results obtained by PMCA correlated with animal infectivity (22,36).…”

mentioning

confidence: 99%

Inactivation of Template-Directed Misfolding of Infectious Prion Protein by Ozone

Ding

Neumann

Price

et al. 2012

Appl Environ Microbiol

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Misfolded prions (PrP Sc ) are well known for their resistance to conventional decontamination processes. The potential risk of contamination of the water environment, as a result of disposal of specified risk materials (SRM), has raised public concerns. Ozone is commonly utilized in the water industry for inactivation of microbial contaminants and was tested in this study for its ability to inactivate prions (263K hamster scrapie ‫؍‬ PrP Sc ). Treatment variables included initial ozone dose (7.6 to 25.7 mg/liter), contact time (

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mentioning

confidence: 99%

Inactivation of Template-Directed Misfolding of Infectious Prion Protein by Ozone

Ding

Neumann

Price

et al. 2012

Appl Environ Microbiol

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“…Although most of the work by Soto's group concerns a hamster model infected by strain 263K, significant amplification has been achieved with the PrP Sc produced by various mammalian species, including mice [47,72], sheep, goats and cattle [72], cervids [38] and humans [36]. The PrP Sc newly formed by PMCA has all the properties of the original PrP Sc , notably its infectious character [14,82].…”

Section: Protein Misfolding Cyclic Amplificationmentioning

confidence: 99%

Progress and limits of TSE diagnostic tools

et al. 2008

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-Following the two "mad cow" crises of 1996 and 2000, there was an urgent need for rapid and sensitive diagnostic methods to identify animals infected with the bovine spongiform encephalopathy (BSE) agent. This stimulated research in the field of prion diagnosis and led to the establishment of numerous so-called "rapid tests" which have been in use in Europe since 2001 for monitoring at-risk populations (rendering plants) and animals slaughtered for human consumption (slaughterhouse). These rapid tests have played a critical role in the management of the mad cow crisis by allowing the removal of prion infected carcasses from the human food chain, and by allowing a precise epidemiological monitoring of the BSE epizootic. They are all based on the detection of the abnormal form of the prion protein (PrP Sc or PrP res ) in brain tissues and consequently are only suitable for post-mortem diagnosis. Since it is now very clear that variant Creutzfeldt-Jakob disease (vCJD) can be transmitted by blood transfusion, the development of a blood test for the diagnosis of vCJD is a top priority. Although significant progress has been made in this direction, including the development of the protein misfolding cyclic amplification (PMCA) technology, at the time this paper was written, this objective had not yet been achieved. This is the most important challenge for the years to come in this field of prion research.

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“…The brains of hamsters at the terminal stage of the disease, titrating 5 Â 10 8:5 LD 50 per gram by bioassay, 16) were pooled together and homogenized at a concentration of 20% (w/v) in phosphatebuffered saline (PBS). The homogenate was mixed with an equal volume of 0.2% (w/v) FeCl 2 -PBS solution in the presence of 5% (v/v) H 2 O 2 .…”

Section: Prpmentioning

confidence: 99%

“…The PMCA procedure followed was based on that reported in our previous study. 16) Briefly, the treated sample was diluted 1:10 in 10% uninfected brain homogenate, and one round of the PMCA reaction was performed by applying 40 cycles of sonication, followed by incubation at 37 C for 1 h. Next, the process diluting the PMCA product to 1:10 and its subsequent amplification was repeated two times. With regard to the PMCA products, samples (10 ml) collected before and after each round of amplification were mixed with 10 ml PK solution (100 mg/ml) and incubated at 37…”

Section: Prpmentioning

confidence: 99%

Assessment of Prion Inactivation by Fenton Reaction Using Protein Misfolding Cyclic Amplification and Bioassay

Suyama¹,

Yoshioka²,

Akagawa³

et al. 2007

Bioscience, Biotechnology, and Biochemistry

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Protein misfolding cyclic amplification as a rapid test for assessment of prion inactivation

Cited by 33 publications

References 14 publications

Inactivation of Template-Directed Misfolding of Infectious Prion Protein by Ozone

Inactivation of Template-Directed Misfolding of Infectious Prion Protein by Ozone

Progress and limits of TSE diagnostic tools

Assessment of Prion Inactivation by Fenton Reaction Using Protein Misfolding Cyclic Amplification and Bioassay

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