you cannot cook the CWD TSE prion disease out of meat.
you can take the ash and mix it with saline and inject that ash into a mouse, and the mouse will go down with TSE.
Prion Infected Meat-and-Bone Meal Is Still Infectious after Biodiesel Production as well.
the TSE prion agent also survives Simulated Wastewater Treatment Processes.
IN fact, you should also know that the CWD TSE Prion agent will survive in the environment for years, if not decades.
you can bury it and it will not go away.
CWD TSE agent is capable of infected your water table i.e. Detection of protease-resistant cervid prion protein in water from a CWD-endemic area.
it’s not your ordinary pathogen you can just cook it out and be done with.
that’s what’s so worrisome about Iatrogenic mode of transmission, a simple autoclave will not kill this TSE prion agent.
New studies on the heat resistance of hamster-adapted scrapie agent: Threshold survival after ashing at 600°C suggests an inorganic template of replication
Paul Brown*,dagger , Edward H. RauDagger , Bruce K. Johnson*, Alfred E. Bacote*, Clarence J. Gibbs Jr.*, and D. Carleton Gajdusek§ * Laboratory of Central Nervous System Studies, National Institute of Neurological Disorders and Stroke, and Dagger Environmental Protection Branch, Division of Safety, Office of Research Services, National Institutes of Health, Bethesda, MD 20892; and § Institut Alfred Fessard, Centre National de la Recherche Scientifique, 91198 Gif sur Yvette, France Contributed by D. Carleton Gajdusek, December 22, 1999
see full text:
Prion Infected Meat-and-Bone Meal Is Still Infectious after Biodiesel Production
Cathrin E. Bruederle,1* Robert M. Hnasko,1 Thomas Kraemer,2 Rafael A. Garcia,3 Michael J. Haas,3 William N. Marmer,3 and John Mark Carter1 1USDA-ARS WRRC, Foodborne Contaminants Research Unit, Albany, California, United States of America 2Forensic Toxicology, Institute of Legal Medicine, Saarland University, Homburg/Saar, Germany 3USDA-ARS ERRC, Fats, Oils and Animal Coproducts Research Unit, Wyndmoor, Pennsylvania, United States of America Neil Mabbott, EditorUniversity of Edinburgh, United Kingdom *
Wednesday, October 14, 2009
Detection of protease-resistant cervid prion protein in water from a CWD-endemic area
T.A. Nichols,1,2 Bruce Pulford,1 A. Christy Wyckoff,1,2 Crystal Meyerett,1 Brady Michel,1 Kevin Gertig,3 Edward A. Hoover,1 Jean E. Jewell,4 Glenn C. Telling5 and Mark D. Zabel1,*
1Department of Microbiology, Immunology and Pathology; College of Veterinary Medicine and Biomedical Sciences; Colorado State University; Fort Collins, CO USA; 2National Wildlife Research Center; Wildlife Services; United States Department of Agriculture; Fort Collins, CO USA; 3Fort Collins Utilities; Fort Collins; CO USA; 4Department of Veterinary Sciences; Wyoming State Veterinary Laboratory; University of Wyoming; Laramie, WY USA; 5Department of Microbiology, Immunology, Molecular Genetics and Neurology; Sanders Brown Center on Aging; University of Kentucky; Lexington, KY USA
The data presented here demonstrate that sPMCA can detect low levels of PrPCWD in the environment, corroborate previous biological and experimental data suggesting long term persistence of prions in the environment2,3 and imply that PrPCWD accumulation over time may contribute to transmission of CWD in areas where it has been endemic for decades. This work demonstrates the utility of sPMCA to evaluate other environmental water sources for PrPCWD, including smaller bodies of water such as vernal pools and wallows, where large numbers of cervids congregate and into which prions from infected animals may be shed and concentrated to infectious levels.
snip...see more here ;
Monday, August 8, 2011
Susceptibility of Domestic Cats to CWD Infection
Oral.29: Susceptibility of Domestic Cats to CWD Infection
for those interested, you can see the program here ;
PrioNet Canada and the Alberta Prion Research Institute are proud to co-host the world’s largest international prion research conference, PRION 2011, in Montreal, Quebec from May 16-19. This is the first time this conference is being presented outside of Europe. This international PRION 2011 congress will follow in the same tradition as past PRION conferences and aims to welcome over 600 attendees from around the world. PRION 2011 anticipates over 55 speakers and will include an outstanding list of plenary lectures, special sessions, “hot topic” panels, networking activities, and poster presentations.
Prion diseases know no borders, and this congress represents the one annual event to bring together experts from around the world to discuss a broad spectrum of topics, from surveillance and control, to prion structure and function, to diagnostics and therapeutics, ultimately with the goal to enhance the pace of prion research to mitigate the negative impacts of prion disease on society. This meeting will also cover the new connections between prion diseases and other human misfolding protein diseases such as Alzheimer’s, Parkinson’s and others. Prion-like propagation of protein misfolding will be one of four special themes of the meeting.
We look forward to your participation!
The PRION 2011 Steering Committee
Thursday, February 17, 2011
Environmental Sources of Scrapie Prions
Saturday, May 14, 2011
Modeling Routes of Chronic Wasting Disease Transmission: Environmental Prion Persistence Promotes Deer Population Decline and Extinction
Tuesday, December 18, 2012
A Growing Threat How deer breeding could put public trust wildlife at risk
Friday, November 09, 2012
Chronic Wasting Disease CWD in cervidae and transmission to other species
Sunday, November 11, 2012
Susceptibilities of Nonhuman Primates to Chronic Wasting Disease November 2012
Friday, December 14, 2012
Susceptibility Chronic Wasting Disease (CWD) in wild cervids to Humans 2005 - December 14, 2012
International Prion Congress: From agent to disease September 8–11, 2010 Salzburg, Austria
PRION 2010 is the top Global Annual TSE Conference in prion research, following a sequence of PRION meetings that were originally organized by the EU Network of Excellence NeuroPrion. In this proud tradition, PRION 2010 covers all aspects of this fascinating scientific area. PRION 2010 is a meeting of greatest interest for neuroscientists, protein structural biologists, geneticists, medical specialists including neurologists, neuropathologists, hygiene experts and blood product providers, veterinarians, epidemiologists, laboratory technicians, industry developers, risk assessors and managers. An outstanding list of Plenary Lecture, Symposia and Workshop Speakers is complemented by the plethora of original input from Poster Presentations. Special consideration is given this year to two areas of major interest: the renewed discussion about the zoonotic potential of animal prion diseases, given the emergence of atypical BSE and scrapie strains, and the breakthrough work on synthetic prions by several groups simultaneously.
Survival and Limited Spread of TSE Infectivity after Burial
Karen Fernie, Allister Smith and Robert A. Somerville The Roslin Institute and R(D)SVS; University of Edinburgh; Roslin, Scotland UK
Scrapie and chronic wasting disease probably spread via environmental routes, and there are also concerns about BSE infection remaining in the environment after carcass burial or waste 3disposal. In two demonstration experiments we are determining survival and migration of TSE infectivity when buried for up to five years, as an uncontained point source or within bovine heads. Firstly boluses of TSE infected mouse brain were buried in lysimeters containing either sandy or clay soil. Migration from the boluses is being assessed from soil cores taken over time. With the exception of a very small amount of infectivity found 25 cm from the bolus in sandy soil after 12 months, no other infectivity has been detected up to three years. Secondly, ten bovine heads were spiked with TSE infected mouse brain and buried in the two soil types. Pairs of heads have been exhumed annually and assessed for infectivity within and around them. After one year and after two years, infectivity was detected in most intracranial samples and in some of the soil samples taken from immediately surrounding the heads. The infectivity assays for the samples in and around the heads exhumed at years three and four are underway. These data show that TSE infectivity can survive burial for long periods but migrates slowly. Risk assessments should take into account the likely long survival rate when infected material has been buried.
The authors gratefully acknowledge funding from DEFRA.
Enzymatic Digestion of Chronic Wasting Disease Prions Bound to Soil
Samuel E. Saunders,1 Jason C. Bartz,2 Kurt C. Vercauteren3 and Shannon L. Bartelt-Hunt1 1Department of Civil Engineering; University of Nebraska-Lincoln; Peter Kiewit Institute; Omaha, Nebraska USA; 2Department of Medical Microbiology and Immunology; Creighton University; Omaha, Nebraska USA; 3USDA; Animal and Plant Health Inspection Service; Wildlife Services; National Wildlife Research Center; Fort Collins, CO USA
Chronic wasting disease (CWD) and sheep scrapie can be transmitted via indirect environmental routes, and it is known that soil can serve as a reservoir of prion infectivity. Given the strong interaction between the prion protein (PrP) and soil, we hypothesized that binding to soil enhances prion resistance to enzymatic digestion, thereby facilitating prion longevity in the environment and providing protection from host degradation. We characterized the performance of a commercially available subtilisin enzyme, the Prionzyme, to degrade soil-bound and unbound CWD and HY TME PrP as a function of pH, temperature, and treatment time. The subtilisin enzyme effectively degraded PrP adsorbed to a wide range of soils and soil minerals below the limits of detection. Signal loss occurred rapidly at high pH (12.5) and within 7 d under conditions representative of the natural environment (pH 7.4, 22°C). Serial PMCA of treated soil samples suggests a greater than 6-log decrease in infectious titer compared with controls. We observed no apparent difference in enzyme effectiveness between bound and unbound CWD PrP. Our results show that although adsorbed prions do retain relative resistance to enzymatic digestion compared with other brain homogenate proteins, they can be effectively degraded when bound to soil. Our results also suggest a topical application of a subtilisin enzyme solution may be an effective decontamination method to limit disease transmission via environmental ‘hot spots’ of prion infectivity.
Degradation of Pathogenic Prion Protein and Prion Infectivity by Lichens
Christopher J. Johnson,1 James P. Bennett,1 Steven M. Biro,1,2 Cynthia M. Rodriguez,1,2 Richard A. Bessen3 and Tonie E. Rocke1
1USGS National Wildlife Health Center; 2Department of Bacteriology; University of Wisconsin, Madison; 3Department of Veterinary Molecular Biology; Montana State University; Bozeman, MT USA
Key words: prion, lichen, bioassay, protease, degradation
Few biological systems have been identified that degrade the transmissible spongiform encephalopathy (TSE)-associated form of the prion protein (PrPTSE) and TSE infectivity. Stability of the TSE agent allows scrapie and chronic wasting disease agents to persist in the environment and cause disease for years. Naturally-occurring or engineered processes that reduce infectivity in the environment could aid in limiting environmental TSE transmission. We have previously identified that species of at least three lichens, unusual, symbiotic organisms formed from a fungus and photosynthetic partner, contain a serine protease capable of degrading PrPTSE under gentle conditions. We tested the hypothesis that lichen extracts from these three species reduce TSE infectivity by treating infected brain homogenate with extracts and examining infectivity in mice. We found lichen extracts diminished TSE infectious titer by factors of 100 to 1,000 and that reductions in infectivity were not well-correlated with the extent of PrPTSE degradation observed by immunoblotting. For example, treatment of brain homogenate with Cladonia rangiferina extract caused <100-fold activity="" after="" agents.="" also="" and="" anti-prion="" but="" characterization="" cladonia="" closely="" clusters="" comparison="" data="" decrease="" degradation="" degrade="" div="" do="" extract="" favors="" focus="" fold="" for="" forms="" genera="" has="" immunoreactivity="" in="" indicate="" infectious="" infectivity="" known="" lichen="" more="" necessarily="" not="" of="" on="" or="" our="" phylogeny="" prion-degrading="" protease="" prp="" prptse.="" prptse="" reduction="" related="" remaining="" rendered="" searches="" some="" species-specificity="" species="" suggesting="" that="" the="" those="" to="" treatment="" uninfectious="" usnea="" was="" which="" with="" within="" yielded="">
The Anti-prion Activity of Soil Organic Compounds Humic and Fulvic Acids
Joanna Narkiewicz,1,2 Ai H.N. Tran,1 Gabriele Giachin,1 Liviana Leita2 and Giuseppe Legname1, 1Neurobiology Sector; Scuola Internazionale Superiore di Studi Avanzati; International School for Advanced Studies; Bonomea, Trieste Italy; 2Agricultural Research Council (CRA); Research Centre for Soil-Plant System; Trieste, Gorizia Italy
A notable feature of prion diseases, as scrapie in sheep and chronic wasting disease in mule deer and elk, is horizontal transmission between grazing animals, suggesting that contaminated environment may contribute significantly to disease transmission. Increasing evidence suggests that soil may present natural reservoir of prion infectivity. Recent studies have shown that prions may persist in contaminated soil and remain infectious for years. As the mechanism of prion retention and persistence in soil is unknown, it is necessary to understand which soil components may interact with prions and thus contribute to disease transmission. Several reports indicate that prion have potential to interact with soil minerals, however the contribution of soil organic fraction in adsorption to prions has been neglected. Here, we present strong evidence for soil humic substances (HS) interaction with prions. We show that two HS, classified as humic and fulvic acids, interact with recombinant prion proteins in vitro. Moreover, we show that both HS possess anti-prion activity, both in vivo and in vitro. Both compounds induced elimination of PrPSc from chronically scrapie-infected GT1 mouse hypothalamic cells (ScGT1) in a dose-dependent manner. ScGT1 cells treatment with HS at concentration of 20mg/mL eliminated more than 95% of PrPSc and did not affect cell viability. Moreover, both HS induced inhibition of prion fibril formation in vitro, as determined by thioflavin T assay. Our results suggest that HS may contribute significantly to prion inactivation in natural soil environments.
Detection of PrPCWD in Rocky Mountain Elk Feces Using Protein Misfolding Cyclic Amplification
Bruce E Pulford,1 Terry Spraker,1 Jenny Powers,2 Margaret Wild2 and Mark D. Zabel1 1Department of Microbiology; Immunology and Pathology; College of Veterinary Medicine and Biomedical Sciences; Colorado State University; 2Biological Resource Management Division; United States National Park Service; CO, USA
Key words: CWD, feces, PMCA, elk
Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy affecting cervids, including mule and white-tailed deer (Odocoileus hemionus and virginianus), elk (Cervus elaphus nelsoni) and moose (Alces alces shirasi). The method of CWD transmission between hosts is unclear, though there is evidence that feces excreted by infected animals may play a role. Recently, CWD prions was detected in feces using bioassays in cervidized mice, which took many months to produce results. In this study, we use a more rapid procedure, protein misfolding cyclic amplification (PMCA), to test elk feces for the presence of PK-resistant cervid PrP (PrPCWD). Feces were collected from symptomatic and asymptomatic elk in several northern Colorado locations, homogenized, mixed with normal brain homogenate from Tg5037 mice (expressing cervid PrP) and subjected to up to 9 rounds of PMCA (1 round = 40 secs sonication/30 mins at 70% maximum power, 24 hours). Western blots were used to detect PrPCWD using BAR-224 anti-PrP antibody. Rectal and CNS tissue from the elk were IHC-labeled and examined for the presence of PrPCWD. Fecal samples from symptomatic and asymptomatic elk that tested positive by IHC showed characteristic PrPCWD bands on western blots following PMCA. In addition, PMCA detected PrPCWD in 25% of fecal samples from IHC-negative animals. These data suggest that PMCA may (1) prove useful as a non-invasive method to supplement or even replace IHC testing of cervids for CWD, and (2) identify additional asymptomatic carriers of CWD, the prevalence of which may be underestimated using IHC.
see full text and more ;
Friday, February 25, 2011
Soil clay content underlies prion infection odds
UPDATED DATA ON 2ND CWD STRAIN
Wednesday, September 08, 2010
CWD PRION CONGRESS SEPTEMBER 8-11 2010