CWD continues to spread Disease of cervids causing local population declines

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Originally Posted by streaker69

Thank you, makes sense. Now, what's the solution? Should those scent products, that are effectively bait, be banned? If it's endangering large populations it would make sense. IMO, it isn't very sporting to be using "bait" to begin with.

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This is one of those situations where the regulatory agency and the legislature need to not fuck around and take the steps necessary to prevent the spread of CWD. If it means that deer urine industry takes a hit, so be it. Economically that is a far more acceptable outcome than having the entire industry surrounding hunting in PA take a hit. It will also push the deer urine industry to work with researchers to come up with a test for prions in order to certify their product safe for use.

We haven't yet had a documented case of a human comtracting CWD from consuming or butchering a deer or elk, but it is only a matter of time. It has happened with BSE (mad cow) and, based on their mechanism of infection, there is no logical reason NOT to expect it with CWD. We already have BSE, CJD, and Kuru as human prion diseases. It isn't unrealistic to expect CWD to behave similarly.

And quite frankly, prions are scary as fuck! They make pathogenic viruses look like anemic weaklings. Most viruses die very quickly outside of a host. Prions can take being frozen, dried out, and only stop being pathogenic when the proteins are denatured by high heat. Unlike viruses, they can't die, because they aren't alive. They can even be taken up by plants and passed along to grazers who eat the plants.

Half measures for something like this won't work. A population that is infected needs to be destroyed and burned like Europe did with several MILLION cattle suspected of having BSE. Because prion disease is scary like rabies. By the time that symptoms show up, it's past being too late.

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Originally Posted by Sandcut

This is one of those situations where the regulatory agency and the legislature need to not fuck around and take the steps necessary to prevent the spread of CWD. If it means that deer urine industry takes a hit, so be it. Economically that is a far more acceptable outcome than having the entire industry surrounding hunting in PA take a hit. It will also push the deer urine industry to work with researchers to come up with a test for prions in order to certify their product safe for use.

We haven't yet had a documented case of a human comtracting CWD from consuming or butchering a deer or elk, but it is only a matter of time. It has happened with BSE (mad cow) and, based on their mechanism of infection, there is no logical reason NOT to expect it with CWD. We already have BSE, CJD, and Kuru as human prion diseases. It isn't unrealistic to expect CWD to behave similarly.

And quite frankly, prions are scary as fuck! They make pathogenic viruses look like anemic weaklings. Most viruses die very quickly outside of a host. Prions can take being frozen, dried out, and only stop being pathogenic when the proteins are denatured by high heat. Unlike viruses, they can't die, because they aren't alive. They can even be taken up by plants and passed along to grazers who eat the plants.

Half measures for something like this won't work. A population that is infected needs to be destroyed and burned like Europe did with several MILLION cattle suspected of having BSE. Because prion disease is scary like rabies. By the time that symptoms show up, it's past being too late.

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I just got done reading Prions for Dummies (The wikipage), wow, that's some scary shit right there. I found it theory that prions may be causing other types of disorders interesting, like ALS, Parkinson's and Huntington's. I didn't understand the the "folding" part of it, as I'm not a hippie micro-biologist.

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Originally Posted by streaker69

I just got done reading Prions for Dummies (The wikipage), wow, that's some scary shit right there. I found it theory that prions may be causing other types of disorders interesting, like ALS, Parkinson's and Huntington's. I didn't understand the the "folding" part of it, as I'm not a hippie micro-biologist.

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if that prion for dummies on wikipage about prions and ALS, Prkinsons's, and Huntington's scared you, then this ought to scare you as well. i said it about 15 years ago too, tse prions, Iatrogenic, and Alzheimer's, what if?

Alzheimer’s disease, iatrogenic, and Transmissible Spongiform Encephalopathy TSE Prion disease, that is the question ???

>>> The only tenable public line will be that "more research is required’’ <<<

>>> possibility on a transmissible prion remains open<<<

O.K., so it’s about 23 years later, so somebody please tell me, when is "more research is required’’ enough time for evaluation ?

[9. Whilst this matter is not at the moment directly concerned with the iatrogenic CJD cases from hgH, there remains a possibility of litigation here, and this presents an added complication. There are also results to be made available shortly (1) concerning a farmer with CJD who had BSE animals, (2) on the possible transmissibility of Alzheimer’s and (3) a CMO letter on prevention of iatrogenic CJD transmission in neurosurgery, all of which will serve to increase media interest.]

http://collections.europarchive.org/...1/04001001.pdf

http://web.archive.org/web/200403150...2/16005001.pdf

http://web.archive.org/web/200307142...2/16005001.pdf

http://collections.europarchive.org/...1/04001001.pdf

snip...see full Singeltary Nature comment here;

http://www.nature.com/nature/journal...html#/comments

see Singeltary comments to Plos ;

Subject: 1992 IN CONFIDENCE TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES POSSIBILITY ON A TRANSMISSIBLE PRION REMAINS OPEN

BSE101/1 0136

IN CONFIDENCE

CMO

From: . Dr J S Metiers DCMO

4 November 1992

TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES

1. Thank you for showing me Diana Dunstan's letter. I am glad that MRC have recognised the public sensitivity of these findings and intend to report them in their proper context. 'This hopefully will avoid misunderstanding and possible distortion by the media to portray the results as having more greater significance than the findings so far justify.

2. Using a highly unusual route of transmission (intra-cerebral injection) the researchers have demonstrated the transmission of a pathological process from two cases one of severe Alzheimer's disease the other of Gerstmann-Straussler disease to marmosets. However they have not demonstrated the transmission of either clinical condition as the "animals were behaving normally when killed". As the report emphasises the unanswered question is whether the disease condition would have revealed itself if the marmosets had lived longer. They are planning further research to see if the conditions, as opposed to the partial pathological process, is transmissible.

what are the implications for public health?

3. The route 'of transmission is very specific and in the natural state of things highly unusual. However it could be argued that the results reveal a potential risk, in that brain tissue from these two patients has been shown to transmit a pathological process. Should therefore brain tissue from such cases be regarded as potentially infective? Pathologists, morticians, neuro surgeons and those assisting at neuro surgical procedures and others coming into contact with "raw" human brain tissue could in theory be at risk. However, on a priori grounds given the highly specific route of transmission in these experiments that risk must be negligible if the usual precautions for handling brain tissue are observed.

1

92/11.4/1.1

BSE101/1 0137

4. The other dimension to consider is the public reaction. To some extent the GSS case demonstrates little more than the transmission of BSE to a pig by intra-cerebral injection. If other prion diseases can be transmitted in this way it is little surprise that some pathological findings observed in GSS were also transmissible to a marmoset. But the transmission of features of Alzheimer's pathology is a different matter, given the much greater frequency of this disease and raises the unanswered question whether some cases are the result of a transmissible prion. The only tenable public line will be that "more research is required’’ before that hypothesis could be evaluated. The possibility on a transmissible prion remains open. In the meantime MRC needs carefully to consider the range and sequence of studies needed to follow through from the preliminary observations in these two cases. Not a particularly comfortable message, but until we know more about the causation of Alzheimer's disease the total reassurance is not practical.

J S METTERS Room 509 Richmond House Pager No: 081-884 3344 Callsign: DOH 832 llllYc!eS 2 92/11.4/1.2

http://collections.europarchive.org/...1/04001001.pdf

>>> The only tenable public line will be that "more research is required’’ <<<

>>> possibility on a transmissible prion remains open<<<

O.K., so it’s about 23 years later, so somebody please tell me, when is "more research is required’’ enough time for evaluation ?

Re-Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy

Nature 525, 247?250 (10 September 2015) doi:10.1038/nature15369 Received 26 April 2015 Accepted 14 August 2015 Published online 09 September 2015 Updated online 11 September 2015 Erratum (October, 2015)

snip...see full Singeltary Nature comment here;

http://www.nature.com/nature/journal...html#/comments

Self-Propagative Replication of Ab Oligomers Suggests Potential Transmissibility in Alzheimer Disease

*** Singeltary comment PLoS ***

Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ?

Posted by flounder on 05 Nov 2014 at 21:27 GMT

http://www.plosone.org/annotation/li...ion?root=82860

Ann N Y Acad Sci. 1982;396:131-43.

Alzheimer's disease and transmissible virus dementia (Creutzfeldt-Jakob disease).

Brown P, Salazar AM, Gibbs CJ Jr, Gajdusek DC.

Abstract

Ample justification exists on clinical, pathologic, and biologic grounds for considering a similar pathogenesis for AD and the spongiform virus encephalopathies. However, the crux of the comparison rests squarely on results of attempts to transmit AD to experimental animals, and these results have not as yet validated a common etiology. Investigations of the biologic similarities between AD and the spongiform virus encephalopathies proceed in several laboratories, and our own observation of inoculated animals will be continued in the hope that incubation periods for AD may be even longer than those of CJD.

http://onlinelibrary.wiley.com/doi/1...849.x/abstract

Sunday, November 22, 2015

*** Effect of heating on the stability of amyloid A (AA) fibrils and the intra- and cross-species transmission of AA amyloidosis Abstract

Amyloid A (AA) amyloidosis is a protein misfolding disease characterized by extracellular deposition of AA fibrils. AA fibrils are found in several tissues from food animals with AA amyloidosis. For hygienic purposes, heating is widely used to inactivate microbes in food, but it is uncertain whether heating is sufficient to inactivate AA fibrils and prevent intra- or cross-species transmission. We examined the effect of heating (at 60 °C or 100 °C) and autoclaving (at 121 °C or 135 °C) on murine and bovine AA fibrils using Western blot analysis, transmission electron microscopy (TEM), and mouse model transmission experiments. TEM revealed that a mixture of AA fibrils and amorphous aggregates appeared after heating at 100 °C, whereas autoclaving at 135 °C produced large amorphous aggregates. AA fibrils retained antigen specificity in Western blot analysis when heated at 100 °C or autoclaved at 121 °C, but not when autoclaved at 135 °C. Transmissible pathogenicity of murine and bovine AA fibrils subjected to heating (at 60 °C or 100 °C) was significantly stimulated and resulted in amyloid deposition in mice. Autoclaving of murine AA fibrils at 121 °C or 135 °C significantly decreased amyloid deposition. Moreover, amyloid deposition in mice injected with murine AA fibrils was more severe than that in mice injected with bovine AA fibrils. Bovine AA fibrils autoclaved at 121 °C or 135 °C did not induce amyloid deposition in mice. These results suggest that AA fibrils are relatively heat stable and that similar to prions, autoclaving at 135 °C is required to destroy the pathogenicity of AA fibrils. These findings may contribute to the prevention of AA fibril transmission through food materials to different animals and especially to humans.

Purchase options Price * Issue Purchase USD 511.00 Article Purchase USD 54.00

http://www.tandfonline.com/doi/abs/1...nalCode=iamy20

http://betaamyloidcjd.blogspot.com/2...bility-of.html

*** Transmission of Creutzfeldt-Jakob disease to a chimpanzee by electrodes contaminated during neurosurgery ***

Gibbs CJ Jr, Asher DM, Kobrine A, Amyx HL, Sulima MP, Gajdusek DC. Laboratory of Central Nervous System Studies, National Institute of Neurological Disorders and Stroke, National Institutes of Health, Bethesda, MD 20892.

Stereotactic multicontact electrodes used to probe the cerebral cortex of a middle aged woman with progressive dementia were previously implicated in the accidental transmission of Creutzfeldt-Jakob disease (CJD) to two younger patients. The diagnoses of CJD have been confirmed for all three cases. More than two years after their last use in humans, after three cleanings and repeated sterilisation in ethanol and formaldehyde vapour, the electrodes were implanted in the cortex of a chimpanzee. Eighteen months later the animal became ill with CJD. This finding serves to re-emphasise the potential danger posed by reuse of instruments contaminated with the agents of spongiform encephalopathies, even after scrupulous attempts to clean them.

http://www.ncbi.nlm.nih.gov/entrez/q...&dopt=Abstract

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

Singeltary, Sr et al. JAMA.2001; 285: 733-734. Vol. 285 No. 6, February 14, 2001 JAMA

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

To the Editor: In their Research Letter, Dr Gibbons and colleagues1 reported that the annual US death rate due to Creutzfeldt-Jakob disease (CJD) has been stable since 1985. These estimates, however, are based only on reported cases, and do not include misdiagnosed or preclinical cases. It seems to me that misdiagnosis alone would drastically change these figures. An unknown number of persons with a diagnosis of Alzheimer disease in fact may have CJD, although only a small number of these patients receive the postmortem examination necessary to make this diagnosis. Furthermore, only a few states have made CJD reportable. Human and animal transmissible spongiform encephalopathies should be reportable nationwide and internationally.

Terry S. Singeltary, Sr Bacliff, Tex

1. Gibbons RV, Holman RC, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States: 1979-1998. JAMA. 2000;284:2322-2323.

http://jama.jamanetwork.com/article....icleid=1031186


kind regards, terry

What I don't understand is, if prions are neither alive nor dead, what mechanism is making them replicate once they're inside a body? I'm assuming that they don't replicate while they're in the environment. Is there something in the body that makes them replicate?

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Originally Posted by streaker69

What I don't understand is, if prions are neither alive nor dead, what mechanism is making them replicate once they're inside a body? I'm assuming that they don't replicate while they're in the environment. Is there something in the body that makes them replicate?

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Not being a cell smasher I really couldn't tell you. Since prions don't have any nucleic acids (DNA/RNA) I can't figure it out since ribosomes read messenger RNA during transcription to make amino acids, which make the protein. Since there's no mRNA I don't know how that would work.

These are terrifying. I read to destroy the prions you have to heat them to 600 Celsius. Infected animals shed prions in all bodily fluids and they can last a decade or longer on the ground. If this mutated to effect people it could wipe out the planet. Image a disease that takes 18 months to show symptoms that can be transferred that easily. We would all be dead.

I posted this on another thread but listen to this podcast. Really great information on CWD. It's episode 70 Meat Eater podcast.

http://www.themeateater.com/podcasts/

The solution in the simplest of terms would be create an enzyme that breaks down this improperly folded protein, right?

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Originally Posted by Yoder

These are terrifying. I read to destroy the prions you have to heat them to 600 Celsius. Infected animals shed prions in all bodily fluids and they can last a decade or longer on the ground. If this mutated to effect people it could wipe out the planet. Image a disease that takes 18 months to show symptoms that can be transferred that easily. We would all be dead.

I posted this on another thread but listen to this podcast. Really great information on CWD. It's episode 70 Meat Eater podcast.

http://www.themeateater.com/podcasts/

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So you are saying I have buy a new meat thermometer? My current one does not go up that high.

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Originally Posted by PAjon

I don't know that even experts in the field fully understand how they work, or what the answer is. I'm sure if synthesizing an enzyme was the answer it would have been thought of by now. I speculate the fact that prions themselves are very good at refolding themselves and manipulating other proteins makes it difficult to get an enzyme that will work.

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I'm sure there are smart people out there working on it. I'm just trying to wrap my brain around how these things actually work. Just seems so strange that something that isn't alive, replicates apparently in a mysterious way and can kill 100% of the time. Immune systems apparently don't even notice it's there.

The reason they get past our defenses and don't get digested as food is because they are so similar to human proteins. They have a pass to get through the door even though they are not compatible with what's on the other side. They start functioning as they should...but our brain tissue is unable to really incorporate them... So it gets torn up by them instead. Ever use a metric socket on a nut which has specs in inches? It kinda fits...but doesn't really. And the result is destructive and irreversible.