Detection of protease-resistant cervid prion protein in water from a CWD-endemic area

Nichols, Tracy A.; Pulford, Bruce; Wyckoff, A. Christy; Meyerett, Crystal; Michel, Brady; Gertig, Kevin R.; Hoover, Edward A.; Jewell, Jean E.; Telling, Glenn C.; Zabel, Mark D.

doi:10.4161/pri.3.3.9819

Cited by 112 publications

(103 citation statements)

References 41 publications

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“…Thus, infectious prions can be transmitted from excreta or body fluids (e.g. urine, faeces, saliva, blood) of live animals, as well as carcasses, to infect susceptible animals or contaminate environments and fomites (Brown et al, 2001;Mathiason et al, 2006;Nichols et al, 2009;Notari et al, 2010;Gilch et al, 2011;Saunders et al, 2012). One distinctive feature of prions is that they are extremely resistant to degradation; therefore, environmental contamination is a serious concern.…”

Section: Introductionmentioning

confidence: 99%

In utero transmission and tissue distribution of chronic wasting disease-associated prions in free-ranging Rocky Mountain elk

Selariu

Powers

Nalls

et al. 2015

Journal of General Virology

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The presence of disease-associated prions in tissues and bodily fluids of chronic wasting disease (CWD)-infected cervids has received much investigation, yet little is known about mother-to-offspring transmission of CWD. Our previous work demonstrated that motherto-offspring transmission is efficient in an experimental setting. To address the question of relevance in a naturally exposed free-ranging population, we assessed maternal and fetal tissues derived from 19 elk dam-calf pairs collected from free-ranging Rocky Mountain elk from north-central Colorado, a known CWD endemic region. Conventional immunohistochemistry identified three of 19 CWD-positive dams, whereas a more sensitive assay [serial protein misfolding cyclic amplification (sPMCA)] detected CWD prion seeding activity (PrP stage. These findings demonstrated that PrP CWD is more abundant in peripheral tissues of CWD-exposed elk than current diagnostic methods suggest, and that transmission of prions from mother to offspring may contribute to the efficient transmission of CWD in naturally exposed cervid populations.

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Section: Introductionmentioning

confidence: 99%

In utero transmission and tissue distribution of chronic wasting disease-associated prions in free-ranging Rocky Mountain elk

Selariu

Powers

Nalls

et al. 2015

Journal of General Virology

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“…Results reported by Brown and Gajdusek (5) demonstrated that PrP Sc infectivity remained in soil for 3 years, and both soil and the aqueous extracts from contaminated soil were infectious in animal models (33). Recently, the prion agent of CWD in cervids was detected in one surface water sample from an area in the United States where CWD is endemic (23). The authors of that study suggested that the persistence and accumulation of prions in the environment may promote the transmission of CWD (23).…”

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confidence: 99%

“…Recently, the prion agent of CWD in cervids was detected in one surface water sample from an area in the United States where CWD is endemic (23). The authors of that study suggested that the persistence and accumulation of prions in the environment may promote the transmission of CWD (23). Water and wastewater may act as transport agents for prions from liquid wastes from slaughtering houses, rendering plants, agricultural digesters, and some septic systems (27).…”

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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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“…The prion agent is able to withstand harsh environmental conditions and remain infectious 16,17 . However, the amount of PrP Sc in the environment is too small to be detected using conventional techniques such WB.…”

Section: Discussionmentioning

confidence: 99%

“…However, the amount of PrP Sc in the environment is too small to be detected using conventional techniques such WB. PMCA has been used to amplify and calculate the approximate amount of PrP Sc the environment, such as soil and water 16,17,20,21 .…”

Section: Discussionmentioning

confidence: 99%

Protein Misfolding Cyclic Amplification of Prions

Saunders

Bartz

Shikiya

2012

JoVE

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Prions are infectious agents that cause the inevitably fatal transmissible spongiform encephalopathy (TSE) in animals and humans 9,18 . The prion protein has two distinct isoforms, the non-infectious host-encoded protein (PrP . This technique has proven to effectively recapitulate the species and strain specificity of PrP Sc conversion from PrP C , to emulate prion strain interference, and to amplify very low levels of PrP Sc from infected tissues, fluids, and environmental samples 6,7,16,23 . This paper details the PMCA protocol, including recommendations for minimizing contamination, generating consistent results, and quantifying those results. We also discuss several PMCA applications, including generation and characterization of infectious prion strains, prion strain interference, and the detection of prions in the environment. Video LinkThe video component of this article can be found at

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Detection of protease-resistant cervid prion protein in water from a CWD-endemic area

Cited by 112 publications

References 41 publications

In utero transmission and tissue distribution of chronic wasting disease-associated prions in free-ranging Rocky Mountain elk

In utero transmission and tissue distribution of chronic wasting disease-associated prions in free-ranging Rocky Mountain elk

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

Protein Misfolding Cyclic Amplification of Prions

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