PUBLIC RELEASE: 15-FEB-2018
Amyloid protein transmission through neurosurgery UNIVERSITY COLLEGE LONDON
Amyloid beta pathology - protein deposits in the brain - might have been transmitted by contaminated neurosurgical instruments, suggests a new UCL-led study.
For the paper, published today in Acta Neuropathologica, researchers studied the medical records of four people who had brain bleeds caused by amyloid beta build-up in the blood vessels of the brain.
They found that all four people had undergone neurosurgery two or three decades earlier as children or teenagers, raising the possibility that amyloid beta deposition may be transmissible through neurosurgical instruments in a similar way to prion proteins which are implicated in prion dementias such as Creutzfeldt-Jakob disease.
Amyloid beta is best known for being one of the hallmark proteins of Alzheimer's disease, but the researchers did not find evidence of Alzheimer's in this study.
"It is well known that the abnormal proteins seen in Creutzfeldt-Jakob disease have been transmitted between patients by certain medical and surgical procedures. We have been investigating whether the same can be true for amyloid beta," said the study's lead author, Professor Sebastian Brandner (UCL Institute of Neurology).
The researchers looked in the pathology archive at the National Hospital for Neurology and Neurosurgery for biopsy and autopsy materials of young adult patients with confirmed amyloid beta pathology, which can lead to brain bleeds or harmful plaques, in the brain's blood vessels. These deposits of the amyloid protein occur increasingly frequently in older individuals but only very rarely in younger people.
Four cases were identified - three of them were in their 30s, and one was aged 57 - all of whom had experienced brain bleeds caused by amyloid deposits in brain blood vessels. None had any known genetic causes that predispose to this pathology in younger people.
A separate review of the medical literature supported the discovery by identifying four other case studies with similar pathology and past surgical history. As these patients were all men with a history of head trauma, research teams had previously speculated that those were correlated.
The new study suggests otherwise, as all patients had a history of childhood neurosurgery, three were women and only one had a history of head trauma.
In a comparison group of 50 people of similar ages from the same archives, the researchers did not find any amyloid beta pathology and only three had a recorded history of childhood neurosurgery.
Previous work in laboratory animals has shown that tiny amounts of abnormal amyloid beta protein can stick to steel wires and transmit pathology into the animals' brains, but this paper is the first to suggest the same may be possible in humans.
The new study follows reports in recent years of amyloid beta pathology in brain blood vessels following treatment with cadaver-derived human growth hormone in childhood.
"We have found new evidence that amyloid beta pathology may be transmissible. This does not mean that Alzheimer's disease can be transmitted, as we did not find any significant amount of pathological tau protein which is the other hallmark protein of Alzheimer's disease," said Professor Brandner.
"Our findings relate to neurosurgical procedures done a long time ago. Nevertheless, the possibility of pathological protein transmission, while rare, should factor into reviews of sterilisation and safety practices for surgical procedures," he said.
"Neurosurgery is becoming increasingly common in older individuals. As amyloid beta pathology increases in brains with age, this raises the potential for onward transmission of protein pathology to other individuals in the same hospital," said the study's first author, Dr Zane Jaunmuktane (UCL Institute of Neurology).
As this study was small and retrospective, the authors hope their findings stimulate others to explore these ideas further. They are currently expanding their study by looking at more archives across the UK.
"There are several reasonable alternative explanations for our findings that we cannot yet rule out. Further research is required to clarify things. A large epidemiological study would be particularly useful," said co-author Professor Simon Mead (MRC Prion Unit at UCL).
###
The study was conducted by researchers at UCL, UCLH, Centro Hospitalar Universitario do Porto, Centro Hospitalar de Lisboa Ocidental and the University of Leuven, and was funded by the National Institute for Health Research University College London Hospitals Biomedical Research Centre and the Queen Square Dementia Biomedical Research Unit.
Disclaimer: AAAS and EurekAlert! are not responsible for the accuracy of news releases posted to EurekAlert! by contributing institutions or for the use of any information through the EurekAlert system.
https://www.eurekalert.org/pub_releases/2018-02/ucl-apt021418.php
Amyloid protein transmission through neurosurgery
15 February 2018
Amyloid beta pathology – protein deposits in the brain – might have been transmitted by contaminated neurosurgical instruments, suggests a new UCL-led study.
For the paper, published today in Acta Neuropathologica, researchers studied the medical records of four people who had brain bleeds caused by amyloid beta build-up in the blood vessels of the brain.
They found that all four people had undergone neurosurgery two or three decades earlier as children or teenagers, raising the possibility that amyloid beta deposition may be transmissible through neurosurgical instruments in a similar way to prion proteins which are implicated in prion dementias such as Creutzfeldt-Jakob disease.
Amyloid beta is best known for being one of the hallmark proteins of Alzheimer’s disease, but the researchers did not find evidence of Alzheimer’s in this study.
“It is well known that the abnormal proteins seen in Creutzfeldt-Jakob disease have been transmitted between patients by certain medical and surgical procedures. We have been investigating whether the same can be true for amyloid beta,” said the study’s lead author, Professor Sebastian Brandner (UCL Institute of Neurology).
The researchers looked in the pathology archive at the National Hospital for Neurology and Neurosurgery for biopsy and autopsy materials of young adult patients with confirmed amyloid beta pathology, which can lead to brain bleeds or harmful plaques, in the brain’s blood vessels. These deposits of the amyloid protein occur increasingly frequently in older individuals but only very rarely in younger people.
Four cases were identified – three of them were in their 30s, and one was aged 57 – all of whom had experienced brain bleeds caused by amyloid deposits in brain blood vessels. None had any known genetic causes that predispose to this pathology in younger people.
A separate review of the medical literature supported the discovery by identifying four other case studies with similar pathology and past surgical history. As these patients were all men with a history of head trauma, research teams had previously speculated that those were correlated.
The new study suggests otherwise, as all patients had a history of childhood neurosurgery, three were women and only one had a history of head trauma.
In a comparison group of 50 people of similar ages from the same archives, the researchers did not find any amyloid beta pathology and only three had a recorded history of childhood neurosurgery.
Previous work in laboratory animals has shown that tiny amounts of abnormal amyloid beta protein can stick to steel wires and transmit pathology into the animals’ brains, but this paper is the first to suggest the same may be possible in humans.
The new study follows reports in recent years of amyloid beta pathology in brain blood vessels following treatment with cadaver-derived human growth hormone in childhood.*
“We have found new evidence that amyloid beta pathology may be transmissible. This does not mean that Alzheimer’s disease can be transmitted, as we did not find any significant amount of pathological tau protein which is the other hallmark protein of Alzheimer’s disease,” said Professor Brandner.
“Our findings relate to neurosurgical procedures done a long time ago. Nevertheless, the possibility of pathological protein transmission, while rare, should factor into reviews of sterilisation and safety practices for surgical procedures,” he said.
“Neurosurgery is becoming increasingly common in older individuals. As amyloid beta pathology increases in brains with age, this raises the potential for onward transmission of protein pathology to other individuals in the same hospital,” said the study’s first author, Dr Zane Jaunmuktane (UCL Institute of Neurology).
As this study was small and retrospective, the authors hope their findings stimulate others to explore these ideas further. They are currently expanding their study by looking at more archives across the UK.
“There are several reasonable alternative explanations for our findings that we cannot yet rule out. Further research is required to clarify things. A large epidemiological study would be particularly useful,” said co-author Professor Simon Mead (MRC Prion Unit at UCL).
The study was conducted by researchers at UCL, UCLH, Centro Hospitalar Universitario do Porto, Centro Hospitalar de Lisboa Ocidental and the University of Leuven, and was funded by the National Institute for Health Research University College London Hospitals Biomedical Research Centre and the Queen Square Dementia Biomedical Research Unit.
Original Article
Molecular Psychiatry , (31 October 2017) | doi:10.1038/mp.2017.204
Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies
X-L Bu, Y Xiang, W-S Jin, J Wang, L-L Shen, Z-L Huang, K Zhang, Y-H Liu, F Zeng, J-H Liu, H-L Sun, Z-Q Zhuang, S-H Chen, X-Q Yao, B Giunta, Y-C Shan, J Tan, X-W Chen, Z-F Dong, H-D Zhou, X-F Zhou, W Song and Y-J Wang
Abstract
The amyloid-β protein (Aβ) protein plays a pivotal role in the pathogenesis of Alzheimer’s disease (AD). It is believed that Aβ deposited in the brain originates from the brain tissue itself. However, Aβ is generated in both brain and peripheral tissues. Whether circulating Aβ contributes to brain AD-type pathologies remains largely unknown. In this study, using a model of parabiosis between APPswe/PS1dE9 transgenic AD mice and their wild-type littermates, we observed that the human Aβ originated from transgenic AD model mice entered the circulation and accumulated in the brains of wild-type mice, and formed cerebral amyloid angiopathy and Aβ plaques after a 12-month period of parabiosis. AD-type pathologies related to the Aβ accumulation including tau hyperphosphorylation, neurodegeneration, neuroinflammation and microhemorrhage were found in the brains of the parabiotic wild-type mice. More importantly, hippocampal CA1 long-term potentiation was markedly impaired in parabiotic wild-type mice. To the best of our knowledge, our study is the first to reveal that blood-derived Aβ can enter the brain, form the Aβ-related pathologies and induce functional deficits of neurons. Our study provides novel insight into AD pathogenesis and provides evidence that supports the development of therapies for AD by targeting Aβ metabolism in both the brain and the periphery.
WEDNESDAY, NOVEMBER 1, 2017
Blood-derived amyloid-β protein induces Alzheimer’s disease pathologies
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.]
snip...see full Singeltary Nature comment here;
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
>>> 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;
Alzheimer's disease
let's not forget the elephant in the room. curing Alzheimer's would be a great and wonderful thing, but for starters, why not start with the obvious, lets prove the cause or causes, and then start to stop that. think iatrogenic, friendly fire, or the pass it forward mode of transmission. think medical, surgical, dental, tissue, blood, related transmission. think transmissible spongiform encephalopathy aka tse prion disease aka mad cow type disease...
Commentary: Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
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
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.
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
*** 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/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8006664&dopt=Abstract
2012 Singeltary on CJD and Alzheimer’s and iatrogenic threat
Proposal ID: 29403
Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ?
Background
Alzheimer’s disease and Transmissible Spongiform Encephalopathy disease have both been around a long time, and was discovered in or around the same time frame, early 1900’s. Both disease, and it’s variants, in many cases are merely names of the people that first discovered them. Both diseases are incurable and debilitating brain disease, that are in the end, 100% fatal, with the incubation/clinical period of the Alzheimer’s disease being longer than the TSE prion disease. Symptoms are very similar, and pathology is very similar. I propose that Alzheimer’s is a TSE disease of low dose, slow, and long incubation disease, and that Alzheimer’s is Transmissible, and is a threat to the public via the many Iatrogenic routes and sources. It was said long ago that the only thing that disputes this, is Alzheimer’s disease transmissibility, or the lack of. today, there is enough documented science (some confidential), that shows that indeed Alzheimer’s is transmissible. The risk factor for friendly fire, and or the pass-it-forward mode i.e. Iatrogenic transmission is a real threat, and one that needs to be addressed immediately.
Methods
Through years of research, as a layperson, of peer review journals, transmission studies, and observations of loved ones and friends that have died from both Alzheimer’s and the TSE prion disease i.e. Heidenhain Variant Creutzfelt Jakob Disease CJD.
Results
The likelihood of many victims of Alzheimer’s disease from the many different Iatrogenic routes and modes of transmission as with the TSE prion disease. TSE prion disease survives ashing to 600 degrees celsius, that’s around 1112 degrees farenheit. you cannot cook the 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 TSE Prion agent will survive in the environment for years, if not decades. you can bury it and it will not go away. TSE prion 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.
Conclusions
There should be a Global Congressional Science round table event (one of scientist and doctors et al only, NO CORPORATE, POLITICIANS ALLOWED) set up immediately to address these concerns from the many potential routes and sources of the TSE prion disease, including Alzheimer’s disease, and a emergency global doctrine put into effect to help combat the spread of Alzheimer’s disease via the medical, surgical, dental, tissue, and blood arena’s. All human and animal TSE prion disease, including Alzheimer’s should be made reportable in every state, and Internationally, WITH NO age restrictions. Until a proven method of decontamination and autoclaving is proven, and put forth in use universally, in all hospitals and medical, surgical arena’s, or the TSE prion agent will continue to spread. IF we wait until science and corporate politicians wait until politics let science _prove_ this once and for all, and set forth regulations there from, we will all be exposed to the TSE Prion agents, if that has not happened already. what’s the use of science progressing human life to the century mark, if your brain does not work?
combined cannot exceed 350 Words
shortened to proper word count ;
Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ?
Background
Alzheimer’s disease and Transmissible Spongiform Encephalopathy disease have both been around a long time, and was discovered in or around the same time frame, early 1900’s. Both diseases are incurable and debilitating brain disease, that are in the end, 100% fatal, with the incubation/clinical period of the Alzheimer’s disease being longer (most of the time) than the TSE prion disease. Symptoms are very similar, and pathology is very similar.
Methods
Through years of research, as a layperson, of peer review journals, transmission studies, and observations of loved ones and friends that have died from both Alzheimer’s and the TSE prion disease i.e. Heidenhain Variant Creutzfelt Jakob Disease CJD.
Results
I propose that Alzheimer’s is a TSE disease of low dose, slow, and long incubation disease, and that Alzheimer’s is Transmissible, and is a threat to the public via the many Iatrogenic routes and sources. It was said long ago that the only thing that disputes this, is Alzheimer’s disease transmissibility, or the lack of. The likelihood of many victims of Alzheimer’s disease from the many different Iatrogenic routes and modes of transmission as with the TSE prion disease.
Conclusions
There should be a Global Congressional Science round table event set up immediately to address these concerns from the many potential routes and sources of the TSE prion disease, including Alzheimer’s disease, and a emergency global doctrine put into effect to help combat the spread of Alzheimer’s disease via the medical, surgical, dental, tissue, and blood arena’s. All human and animal TSE prion disease, including Alzheimer’s should be made reportable in every state, and Internationally, WITH NO age restrictions. Until a proven method of decontamination and autoclaving is proven, and put forth in use universally, in all hospitals and medical, surgical arena’s, or the TSE prion agent will continue to spread. IF we wait until science and corporate politicians wait until politics lets science _prove_ this once and for all, and set forth regulations there from, we will all be exposed to the TSE Prion agents, if that has not happened already.
end...tss
Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ?
source references ...end...tss
Hello Nicole,
by all means, please do use my poster. but I thought this was already taken care of, and I could not attend for my poster presentation, therefore, it was not going to be presented. I have some health issues and could not make the trip.
please see old correspondence below...
From: Nicole Sanders Sent: Tuesday, April 10, 2012 5:37 PM To: Terry S. Singeltary Sr. Subject: RE: re-submission
Dear Terry,
The decline of proposal number 30756 is registered in the system. Thank you for your consideration.
Best Regards,
Nicole
Nicole Sanders
Senior Specialist, Membership & Conference Programming
______________________________________
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.
From: xxxx
To: Terry Singeltary
Sent: Saturday, December 05, 2009 9:09 AM
Subject: 14th ICID - abstract accepted for 'International Scientific Exchange'
Your preliminary abstract number: 670
Dear Mr. Singeltary,
On behalf of the Scientific Committee, I am pleased to inform you that your abstract
'Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009'
WAS accepted for inclusion in the INTERNATIONAL SCIENTIFIC EXCHANGE (ISE) section of the 14th International Congress on Infectious Diseases. Accordingly, your abstract will be included in the "Intl. Scientific Exchange abstract CD-rom" of the Congress which will be distributed to all participants.
Abstracts accepted for INTERNATIONAL SCIENTIFIC EXCHANGE are NOT PRESENTED in the oral OR poster sessions.
Your abstract below was accepted for: INTERNATIONAL SCIENTIFIC EXCHANGE
#0670: Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009
Author: T. Singeltary; Bacliff, TX/US
Topic: Emerging Infectious Diseases Preferred type of presentation: International Scientific Exchange
This abstract has been ACCEPTED.
#0670: Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009
Authors: T. Singeltary; Bacliff, TX/US
Title: Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009
Body: Background
An update on atypical BSE and other TSE in North America. Please remember, the typical U.K. c-BSE, the atypical l-BSE (BASE), and h-BSE have all been documented in North America, along with the typical scrapie's, and atypical Nor-98 Scrapie, and to date, 2 different strains of CWD, and also TME. All these TSE in different species have been rendered and fed to food producing animals for humans and animals in North America (TSE in cats and dogs ?), and that the trading of these TSEs via animals and products via the USA and Canada has been immense over the years, decades.
Methods
12 years independent research of available data
Results
I propose that the current diagnostic criteria for human TSEs only enhances and helps the spreading of human TSE from the continued belief of the UKBSEnvCJD only theory in 2009. With all the science to date refuting it, to continue to validate this old myth, will only spread this TSE agent through a multitude of potential routes and sources i.e. consumption, medical i.e., surgical, blood, dental, endoscopy, optical, nutritional supplements, cosmetics etc.
Conclusion
I would like to submit a review of past CJD surveillance in the USA, and the urgent need to make all human TSE in the USA a reportable disease, in every state, of every age group, and to make this mandatory immediately without further delay. The ramifications of not doing so will only allow this agent to spread further in the medical, dental, surgical arena's. Restricting the reporting of CJD and or any human TSE is NOT scientific. Iatrogenic CJD knows NO age group, TSE knows no boundaries.
I propose as with Aguzzi, Asante, Collinge, Caughey, Deslys, Dormont, Gibbs, Gajdusek, Ironside, Manuelidis, Marsh, et al and many more, that the world of TSE Transmissible Spongiform Encephalopathy is far from an exact science, but there is enough proven science to date that this myth should be put to rest once and for all, and that we move forward with a new classification for human and animal TSE that would properly identify the infected species, the source species, and then the route.
Keywords: Transmissible Spongiform Encephalopathy Creutzfeldt Jakob Disease Prion
page 114 ;
http://ww2.isid.org/Downloads/14th_ICID_ISE_Abstracts.pdf
http://www.isid.org/14th_icid/
http://www.isid.org/publications/ICID_Archive.shtml
http://ww2.isid.org/Downloads/IMED2009_AbstrAuth.pdf
Your preliminary abstract number: 670
Dear Mr. Singeltary,
On behalf of the Scientific Committee, I am pleased to inform you that your abstract
'Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009'
WAS accepted for inclusion in the INTERNATIONAL SCIENTIFIC EXCHANGE (ISE) section of the 14th International Congress on Infectious Diseases. Accordingly, your abstract will be included in the "Intl. Scientific Exchange abstract CD-rom" of the Congress which will be distributed to all participants.
Abstracts accepted for INTERNATIONAL SCIENTIFIC EXCHANGE are NOT PRESENTED in the oral OR poster sessions.
Your abstract below was accepted for: INTERNATIONAL SCIENTIFIC EXCHANGE
#0670: Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009
Author: T. Singeltary; Bacliff, TX/US
Topic: Emerging Infectious Diseases Preferred type of presentation: International Scientific Exchange
This abstract has been ACCEPTED.
#0670: Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009
Authors: T. Singeltary; Bacliff, TX/US
Title: Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009
Body: Background
An update on atypical BSE and other TSE in North America. Please remember, the typical U.K. c-BSE, the atypical l-BSE (BASE), and h-BSE have all been documented in North America, along with the typical scrapie's, and atypical Nor-98 Scrapie, and to date, 2 different strains of CWD, and also TME. All these TSE in different species have been rendered and fed to food producing animals for humans and animals in North America (TSE in cats and dogs ?), and that the trading of these TSEs via animals and products via the USA and Canada has been immense over the years, decades.
Methods
12 years independent research of available data
Results
I propose that the current diagnostic criteria for human TSEs only enhances and helps the spreading of human TSE from the continued belief of the UKBSEnvCJD only theory in 2009. With all the science to date refuting it, to continue to validate this old myth, will only spread this TSE agent through a multitude of potential routes and sources i.e. consumption, medical i.e., surgical, blood, dental, endoscopy, optical, nutritional supplements, cosmetics etc.
Conclusion
I would like to submit a review of past CJD surveillance in the USA, and the urgent need to make all human TSE in the USA a reportable disease, in every state, of every age group, and to make this mandatory immediately without further delay. The ramifications of not doing so will only allow this agent to spread further in the medical, dental, surgical arena's. Restricting the reporting of CJD and or any human TSE is NOT scientific. Iatrogenic CJD knows NO age group, TSE knows no boundaries.
I propose as with Aguzzi, Asante, Collinge, Caughey, Deslys, Dormont, Gibbs, Gajdusek, Ironside, Manuelidis, Marsh, et al and many more, that the world of TSE Transmissible Spongiform Encephalopathy is far from an exact science, but there is enough proven science to date that this myth should be put to rest once and for all, and that we move forward with a new classification for human and animal TSE that would properly identify the infected species, the source species, and then the route.
Keywords: Transmissible Spongiform Encephalopathy Creutzfeldt Jakob Disease Prion
page 114 ;
http://ww2.isid.org/Downloads/14th_ICID_ISE_Abstracts.pdf
http://www.isid.org/14th_icid/
http://www.isid.org/publications/ICID_Archive.shtml
http://ww2.isid.org/Downloads/IMED2009_AbstrAuth.pdf
Creutzfeldt Jakob Disease CJD National Prion Disease Pathology Surveillance Center Cases Examined to December 14, 2017
Tuesday, December 12, 2017
Neuropathology of iatrogenic Creutzfeldt–Jakob disease and immunoassay of French cadaver-sourced growth hormone batches suggest possible transmission of tauopathy and long incubation periods for the transmission of Abeta pathology
MONDAY, OCTOBER 02, 2017
Creutzfeldt Jakob Disease United States of America USA and United Kingdom UK Increasing and Zoonotic Pontential From Different Species
THURSDAY, AUGUST 17, 2017
*** Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States revisited 2017
Singeltary et al
TUESDAY, AUGUST 03, 2010
Variably protease-sensitive prionopathy: A new sporadic disease of the prion protein
Here we go folks. AS predicted. THIS JUST OUT !
Saturday, June 13, 2009
Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States 2003 revisited 2009
Sunday, August 09, 2009
CJD...Straight talk with...James Ironside...and...Terry Singeltary... 2009
FRIDAY, AUGUST 11, 2017
Infectivity in bone marrow from sporadic CJD patients
Bioassays in transgenic mice expressing the human prion protein revealed the presence of unexpectedly high levels of infectivity in the bone marrow from seven out of eight sCJD cases. These findings may explain the presence of blood-borne infectivity in sCJD patients. They also suggest that the distribution of prion infectivity in peripheral tissues in sCJD patients could be wider than currently believed, with potential implications for the iatrogenic transmission risk of this disease.
*** 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/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8006664&dopt=Abstract
THURSDAY, AUGUST 10, 2017
*** Minimise transmission risk of CJD and vCJD in healthcare settings Updated 10 August 2017
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.
SPORADIC CREUTZFELDT JAKOB DISEASE s CJD ZOONOSIS OF TSE PRION DISEASE
O.05: Transmission of prions to primates after extended silent incubation periods: Implications for BSE and scrapie risk assessment in human populations
Emmanuel Comoy, Jacqueline Mikol, Valerie Durand, Sophie Luccantoni, Evelyne Correia, Nathalie Lescoutra, Capucine Dehen, and Jean-Philippe Deslys Atomic Energy Commission; Fontenay-aux-Roses, France
Prion diseases (PD) are the unique neurodegenerative proteinopathies reputed to be transmissible under field conditions since decades. The transmission of Bovine Spongiform Encephalopathy (BSE) to humans evidenced that an animal PD might be zoonotic under appropriate conditions. Contrarily, in the absence of obvious (epidemiological or experimental) elements supporting a transmission or genetic predispositions, PD, like the other proteinopathies, are reputed to occur spontaneously (atpical animal prion strains, sporadic CJD summing 80% of human prion cases). Non-human primate models provided the first evidences supporting the transmissibiity of human prion strains and the zoonotic potential of BSE. Among them, cynomolgus macaques brought major information for BSE risk assessment for human health (Chen, 2014), according to their phylogenetic proximity to humans and extended lifetime. We used this model to assess the zoonotic potential of other animal PD from bovine, ovine and cervid origins even after very long silent incubation periods.
*** We recently observed the direct transmission of a natural classical scrapie isolate to macaque after a 10-year silent incubation period,
***with features similar to some reported for human cases of sporadic CJD, albeit requiring fourfold long incubation than BSE. Scrapie, as recently evoked in humanized mice (Cassard, 2014),
***is the third potentially zoonotic PD (with BSE and L-type BSE),
***thus questioning the origin of human sporadic cases.
We will present an updated panorama of our different transmission studies and discuss the implications of such extended incubation periods on risk assessment of animal PD for human health.
===============
***thus questioning the origin of human sporadic cases***
===============
***our findings suggest that possible transmission risk of H-type BSE to sheep and human. Bioassay will be required to determine whether the PMCA products are infectious to these animals.
==============
Transmission data also revealed that several scrapie prions propagate in HuPrP-Tg mice with efficiency comparable to that of cattle BSE. While the efficiency of transmission at primary passage was low, subsequent passages resulted in a highly virulent prion disease in both Met129 and Val129 mice. Transmission of the different scrapie isolates in these mice leads to the emergence of prion strain phenotypes that showed similar characteristics to those displayed by MM1 or VV2 sCJD prion. These results demonstrate that scrapie prions have a zoonotic potential and raise new questions about the possible link between animal and human prions.
PRION 2016 TOKYO
Saturday, April 23, 2016
SCRAPIE WS-01: Prion diseases in animals and zoonotic potential 2016
Prion. 10:S15-S21. 2016 ISSN: 1933-6896 printl 1933-690X online
Taylor & Francis
Prion 2016 Animal Prion Disease Workshop Abstracts
WS-01: Prion diseases in animals and zoonotic potential
Juan Maria Torres a, Olivier Andreoletti b, J uan-Carlos Espinosa a. Vincent Beringue c. Patricia Aguilar a,
Natalia Fernandez-Borges a. and Alba Marin-Moreno a
"Centro de Investigacion en Sanidad Animal ( CISA-INIA ). Valdeolmos, Madrid. Spain; b UMR INRA -ENVT 1225 Interactions Holes Agents Pathogenes. ENVT. Toulouse. France: "UR892. Virologie lmmunologie MolécuIaires, Jouy-en-Josas. France
Dietary exposure to bovine spongiform encephalopathy (BSE) contaminated bovine tissues is considered as the origin of variant Creutzfeldt Jakob (vCJD) disease in human. To date, BSE agent is the only recognized zoonotic prion. Despite the variety of Transmissible Spongiform Encephalopathy (TSE) agents that have been circulating for centuries in farmed ruminants there is no apparent epidemiological link between exposure to ruminant products and the occurrence of other form of TSE in human like sporadic Creutzfeldt Jakob Disease (sCJD). However, the zoonotic potential of the diversity of circulating TSE agents has never been systematically assessed. The major issue in experimental assessment of TSEs zoonotic potential lies in the modeling of the ‘species barrier‘, the biological phenomenon that limits TSE agents’ propagation from a species to another. In the last decade, mice genetically engineered to express normal forms of the human prion protein has proved essential in studying human prions pathogenesis and modeling the capacity of TSEs to cross the human species barrier.
To assess the zoonotic potential of prions circulating in farmed ruminants, we study their transmission ability in transgenic mice expressing human PrPC (HuPrP-Tg). Two lines of mice expressing different forms of the human PrPC (129Met or 129Val) are used to determine the role of the Met129Val dimorphism in susceptibility/resistance to the different agents.
These transmission experiments confirm the ability of BSE prions to propagate in 129M- HuPrP-Tg mice and demonstrate that Met129 homozygotes may be susceptible to BSE in sheep or goat to a greater degree than the BSE agent in cattle and that these agents can convey molecular properties and neuropathological indistinguishable from vCJD. However homozygous 129V mice are resistant to all tested BSE derived prions independently of the originating species suggesting a higher transmission barrier for 129V-PrP variant.
Transmission data also revealed that several scrapie prions propagate in HuPrP-Tg mice with efficiency comparable to that of cattle BSE. While the efficiency of transmission at primary passage was low, subsequent passages resulted in a highly virulent prion disease in both Met129 and Val129 mice. Transmission of the different scrapie isolates in these mice leads to the emergence of prion strain phenotypes that showed similar characteristics to those displayed by MM1 or VV2 sCJD prion. These results demonstrate that scrapie prions have a zoonotic potential and raise new questions about the possible link between animal and human prions.
why do we not want to do TSE transmission studies on chimpanzees $
5. A positive result from a chimpanzee challenged severly would likely create alarm in some circles even if the result could not be interpreted for man. I have a view that all these agents could be transmitted provided a large enough dose by appropriate routes was given and the animals kept long enough. Until the mechanisms of the species barrier are more clearly understood it might be best to retain that hypothesis.
snip...
R. BRADLEY
Title: Transmission of scrapie prions to primate after an extended silent incubation period)
*** In complement to the recent demonstration that humanized mice are susceptible to scrapie, we report here the first observation of direct transmission of a natural classical scrapie isolate to a macaque after a 10-year incubation period. Neuropathologic examination revealed all of the features of a prion disease: spongiform change, neuronal loss, and accumulation of PrPres throughout the CNS.
*** This observation strengthens the questioning of the harmlessness of scrapie to humans, at a time when protective measures for human and animal health are being dismantled and reduced as c-BSE is considered controlled and being eradicated.
*** Our results underscore the importance of precautionary and protective measures and the necessity for long-term experimental transmission studies to assess the zoonotic potential of other animal prion strains.
Volume 23, Number 9—September 2017
Research Letter Chronic Wasting Disease Prion Strain Emergence and Host Range Expansion
***Thus, emergent CWD prion strains may have higher zoonotic potential than common strains.
2017
Subject: ***CDC Now Recommends Strongly consider having the deer or elk tested for CWD before you eat the meat
CDC Now Recommends Strongly consider having the deer or elk tested for CWD before you eat the meat
Chronic Wasting Disease (CWD)
Prevention
* Strongly consider having the deer or elk tested for CWD before you eat the meat.
* If you have your deer or elk commercially processed, consider asking that your animal be processed individually to avoid mixing meat from multiple animals.
* If your animal tests positive for CWD, do not eat meat from that animal.
> However, to date, no CWD infections have been reported in people.
key word here is 'reported'. science has shown that CWD in humans will look like sporadic CJD. SO, how can one assume that CWD has not already transmitted to humans? they can't, and it's as simple as that. from all recorded science to date, CWD has already transmitted to humans, and it's being misdiagnosed as sporadic CJD. ...terry
LOOKING FOR CWD IN HUMANS AS nvCJD or as an ATYPICAL CJD, LOOKING IN ALL THE WRONG PLACES $$$
*** These results would seem to suggest that CWD does indeed have zoonotic potential, at least as judged by the compatibility of CWD prions and their human PrPC target. Furthermore, extrapolation from this simple in vitro assay suggests that if zoonotic CWD occurred, it would most likely effect those of the PRNP codon 129-MM genotype and that the PrPres type would be similar to that found in the most common subtype of sCJD (MM1).***
TUESDAY, SEPTEMBER 12, 2017
CDC Now Recommends Strongly consider having the deer or elk tested for CWD before you eat the meat
SATURDAY, JANUARY 27, 2018
CDC CHRONIC WASTING DISEASE CWD TSE PRION UPDATE REPORT USA JANUARY 2018
Subject: CDC CHRONIC WASTING DISEASE CWD TSE PRION UPDATE REPORT USA JANUARY 2018
CHRONIC WASTING DISEASE CWD TSE PRION IS THE USA AND NORTH AMERICA'S MAD COW DISEASE.
THE USDA INC ET AL WORKED VERY HARD CONCEALING BSE TSE PRION IN CATTLE. they almost succeeded $$$
BUT CWD TSE PRION IN CERVIDS IS A DIFFERENT BEAST, THE COVER UP THERE, USDA INC COULD NOT CONTAIN.
SPORADIC CJD IS 85%+ OF ALL HUMAN TSE PRION DISEASE.
SPORADIC CJD HAS NOW BEEN LINKED TO TYPICAL AND ATYPICAL BSE, SCRAPIE, AND CWD.
SPORADIC/SPONTANEOUS TSE HAS NEVER BEEN PROVEN.
***Moreover, sporadic disease has never been observed in breeding colonies or primate research laboratories, most notably among hundreds of animals over several decades of study at the National Institutes of Health25, and in nearly twenty older animals continuously housed in our own facility.***
CDC CWD TSE PRION UPDATE USA JANUARY 2018 MAP
CDC CWD TSE PRION UPDATE USA JANUARY 2018
As of January 2018, CWD in free-ranging deer, elk and/or moose has been reported in at least 22 states in the continental United States, as well as two provinces in Canada. In addition, CWD has been reported in reindeer and moose in Norway, and a small number of imported cases have been reported in South Korea. The disease has also been found in farmed deer and elk.
CWD was first identified in captive deer in the late 1960s in Colorado and in wild deer in 1981. By the 1990s, it had been reported in surrounding areas in northern Colorado and southern Wyoming. Since 2000, the area known to be affected by CWD in free-ranging animals has increased to at least 22 states, including states in the Midwest, Southwest, and limited areas on the East Coast. It is possible that CWD may also occur in other states without strong animal surveillance systems, but that cases haven’t been detected yet. Once CWD is established in an area, the risk can remain for a long time in the environment. The affected areas are likely to continue to expand.
Nationwide, the overall occurrence of CWD in free-ranging deer and elk is relatively low. However, in several locations where the disease is established, infection rates may exceed 10 percent (1 in 10), and localized infection rates of more than 25 percent (1 in 4) have been reported. The infection rates among some captive deer can be much higher, with a rate of 79% (nearly 4 in 5) reported from at least one captive herd.
As of January 2018, there were 186 counties in 22 states with reported CWD in free-ranging cervids.
Chronic Wasting Disease Among Free-Ranging Cervids by County, United States, January 2018
snip...
Prion 2017 Conference Abstracts CWD
2017 PRION CONFERENCE
First evidence of intracranial and peroral transmission of Chronic Wasting Disease (CWD) into Cynomolgus macaques: a work in progress
Stefanie Czub1, Walter Schulz-Schaeffer2, Christiane Stahl-Hennig3, Michael Beekes4, Hermann Schaetzl5 and Dirk Motzkus6 1
University of Calgary Faculty of Veterinary Medicine/Canadian Food Inspection Agency; 2Universitatsklinikum des Saarlandes und Medizinische Fakultat der Universitat des Saarlandes; 3 Deutsches Primaten Zentrum/Goettingen; 4 Robert-Koch-Institut Berlin; 5 University of Calgary Faculty of Veterinary Medicine; 6 presently: Boehringer Ingelheim Veterinary Research Center; previously: Deutsches Primaten Zentrum/Goettingen
This is a progress report of a project which started in 2009. 21 cynomolgus macaques were challenged with characterized CWD material from white-tailed deer (WTD) or elk by intracerebral (ic), oral, and skin exposure routes. Additional blood transfusion experiments are supposed to assess the CWD contamination risk of human blood product. Challenge materials originated from symptomatic cervids for ic, skin scarification and partially per oral routes (WTD brain). Challenge material for feeding of muscle derived from preclinical WTD and from preclinical macaques for blood transfusion experiments. We have confirmed that the CWD challenge material contained at least two different CWD agents (brain material) as well as CWD prions in muscle-associated nerves.
Here we present first data on a group of animals either challenged ic with steel wires or per orally and sacrificed with incubation times ranging from 4.5 to 6.9 years at postmortem. Three animals displayed signs of mild clinical disease, including anxiety, apathy, ataxia and/or tremor. In four animals wasting was observed, two of those had confirmed diabetes. All animals have variable signs of prion neuropathology in spinal cords and brains and by supersensitive IHC, reaction was detected in spinal cord segments of all animals. Protein misfolding cyclic amplification (PMCA), real-time quaking-induced conversion (RT-QuiC) and PET-blot assays to further substantiate these findings are on the way, as well as bioassays in bank voles and transgenic mice.
At present, a total of 10 animals are sacrificed and read-outs are ongoing. Preclinical incubation of the remaining macaques covers a range from 6.4 to 7.10 years. Based on the species barrier and an incubation time of > 5 years for BSE in macaques and about 10 years for scrapie in macaques, we expected an onset of clinical disease beyond 6 years post inoculation.
PRION 2017 DECIPHERING NEURODEGENERATIVE DISORDERS
Subject: PRION 2017 CONFERENCE DECIPHERING NEURODEGENERATIVE DISORDERS VIDEO
PRION 2017 CONFERENCE DECIPHERING NEURODEGENERATIVE DISORDERS
*** PRION 2017 CONFERENCE VIDEO
TUESDAY, JUNE 13, 2017
PRION 2017 CONFERENCE ABSTRACT
First evidence of intracranial and peroral transmission of Chronic Wasting Disease (CWD) into Cynomolgus macaques: a work in progress
TUESDAY, DECEMBER 12, 2017
*** Chronic Wasting Disease CWD TSE Prion (aka mad deer disease) Update USA December 14, 2017 ***
(zoonosis and environmental risk factors towards the bottom, after state by state reports)
MONDAY, MARCH 13, 2017
CHRONIC WASTING DISEASE CWD TSE PRION UDATE March 13, 2017
SATURDAY, JANUARY 14, 2017
CHRONIC WASTING DISEASE CWD TSE PRION GLOBAL UPDATE JANUARY 14, 2017
FRIDAY, DECEMBER 15, 2017
Canada CFIA updating its national CWD TSE PRION efforts to eradicate disease farmed cervid NOT successful December 14, 2017
TUESDAY, DECEMBER 12, 2017
Bovine Spongiform Encephalopathy BSE TSE Prion (aka mad cow disease) Report December 14, 2017 2017
TUESDAY, DECEMBER 12, 2017
SCRAPIE TSE PRION UPDATE USA DECEMBER 14, 2017
TUESDAY, JANUARY 30, 2018
Chronic Wasting Disease A Time Bomb For Agriculture?
WOW, i am shocked, this came from the PORK farm journal...nice article!
SATURDAY, FEBRUARY 10, 2018
Chronic wasting disease management in ranched elk using rectal biopsy testing Research Paper 09 Feb 2018
CWD TSE PRION STATE BY STATE 2017 POSITIVES HUNT SAMPLES UPDATE
MONDAY, DECEMBER 25, 2017
APHIS USDA Food Safety Research Priorities and the one you missed, the coming storm BSE CWD Scrapie TSE Prion
Subject: CJD, Alzheimer's, one-in-a-million and the USA CJD FOUNDATION CJD Questionnaire (if that is what you want to call it)
Date: Tue, 14 Jan 2003 16:34:10 -0600
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy
To: BSE-L@uni-karlsruhe.de
######## Bovine Spongiform Encephalopathy #########
Greetings list members,
something else i am curious about, i read here where it states;
> 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.
now what about these findings;
IN STRICT CONFIDENCE
TRANSMISSION OF ALZHEIMER-TYPE PLAQUES TO PRIMATES
http://www.bseinquiry.gov.uk/files/yb/1993/01/05004001.pdf
so why not have any of these type studies started? seems from the studies below, this warrants further investigation asap...
1: 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.
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://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6758661&dopt=Abstract
1: Neurology 1980 Sep;30(9):945-50
Evidence for and against the transmissibility of Alzheimer disease.
Goudsmit J, Morrow CH, Asher DM, Yanagihara RT, Masters CL, Gibbs CJ Jr, Gajdusek DC.
Nonhuman primates were inoculated intracerebrally with brain tissue from 52 patients with confirmed Alzheimer disease (AD) in order to investigate the possibility of an infectious etiology. Animals inoculated with brain tissue from two patients with familial AD developed a spongiform encephalopathy that was indistinguishable from Creutzfeldt-Jakob disease (CJD). Seventeen other cases of AD on test for more than 50 months failed to produce similar changes, and 33 cases have not been incubating for a sufficient period of time to ascertain the presence of a transmissible agent. The initial transmission of spongiform encephalopathy with brain tissue from the two familial cases of AD has not been reproduced and the association between AD and an infectious agent has not yet been demonstrated with any reasonable degree of certainty. The frequent overlap of clinical symptoms of AD and CJD, and the occurrence of cases of CJD and AD in the same families indicate the need for continuing research on the relationship between the two diseases.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6775247&dopt=Abstract
1: Neurology 1990 Feb;40(2):226-8
Coexistence of Creutzfeldt-Jakob disease and Alzheimer's disease in the same patient.
Brown P, Jannotta F, Gibbs CJ Jr, Baron H, Guiroy DC, Gajdusek DC.
Laboratory of CNS Studies, NINDS, National Institutes of Health, Bethesda, MD 20892.
We report the case of a 73-year-old patient in whom a diagnosis of Creutzfeldt-Jakob disease, suggested by the clinical course, was verified by the neuropathologic finding of widespread spongiform change and astrogliosis, the presence of proteinase-resistant protein in brain extracts, and the experimental transmission of spongiform encephalopathy to primates inoculated with brain tissue. However, neuropathologic examination also revealed a profusion of senile and neuritic plaques and neurofibrillary tangles that reacted with antibody to the amyloid beta-protein characteristic of Alzheimer's disease, but not with antibody to the scrapie amyloid protein characteristic of Creutzfeldt-Jakob disease.
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=2405293&dopt=Abstract
1: Eur J Epidemiol 1986 Dec;2(4):252-64
Familial Creutzfeldt-Jakob disease in France: epidemiological implications.
Baron H, Cathala F, Brown P, Chatelain J, Gajdusek DC.
Of 329 patients dying of Creutzfeldt-Jakob disease (CJD) in continental France between 1968 and 1982, 19 (6%) were familial cases. Genealogical investigation permitted the identification of 19 additional cases, bringing the total number of familial CJD cases reported here to 38. There are 6 definitely affected families, yielding an average of 6.3 cases per family. Mediterranean Jews account for one-third of all the cases, with Tunisian Jews constituting two-thirds of this ethnic group. Males and females are equally affected. The overall rate of occurrence (47.3%) is consistent with autosomal dominant transmission, but wide variations in individual pedigrees (26.7%-80%) leave this hypothesis open to scrutiny. Age at death is 10 to 15 years lower in familial than in sporadic CJD, suggesting the possible inheritance of "short incubation" genes in certain CJD families. Disease duration is longer in familial than in sporadic CJD, but this could be the effect of ascertainment bias. There is no evidence for maternal lineage. While members of a given family tend to die within the same age bracket, our data fail to discriminate between vertical transmission and common source exposure as hypothetical transmission mechanisms within affected families. CJD occurrence in a woman related by marriage to an unaffected branch of a CJD family, but who was raised in early childhood by the affected branch, argues in favor of horizontal transmission early in life. Analysis of death intervals and geographic/temporal separations suggests minimal incubation periods of up to 43 years. A family combining clinico-pathological features of CJD and the Gerstmann-Straussler syndrome (GSS) indicates a nosological relationship between the two. The "genetic susceptibility" of members of CJD-affected families may be due to accelerated derepression of normally repressed host genes, coding for abnormal amyloid-type proteins. Accumulation of these proteins may play an important role in the pathogenesis of CJD and scrapie, and constitute a common pathogenetic mechanism in several neurological diseases, including Alzheimer's disease (AD) and senile dementia of the Alzheimer type (SDAT).
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=3542553&dopt=Abstract
1: 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.
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://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=6758661&dopt=Abstract
Greetings again list members,
i believe if the USA had any _real_ CJD surveillance, except the token prion unit at Case Western, with no disrespect to Dr. Gambetti, but he is working either directly or indirectly for the CDC/NIH, if you look at it from a funding/grants prospect. plus, his prospects of finding any CJD with a CJD Questionnaire that ask no questions as to route/source, and CJD/TSEs _not_ reportable nationally, i just do not understand how any surveillance can be done this way. it kinda reminds me of the extensive 13 year old USA BSE Surveillance program. could someone please explain to me, how anyone could figure out the route and source of the TSE agent with a questionnaire like (see below), especially since the new findings by Collinge et al, that BSE transmission to the 129-methionine genotype can lead to an alternate phenotype which is indistinguishable from type 2 PrPSc, the commonest sporadic CJD. would these new findings even further warrant immediate actions as to making CJD reportable nationally and having a CJD questionnaire that ask _real_ questions pertaining to route/source? seems to me, with a CJD Questionnaire such as this, and the questions they ask, the only thing they want to find out is, how it was diagnosed, probably to just find a flaw in any confirmed cases, to negate the confirmation, to hold at one-in-a-million. OR, it could be part of the Presidents new anti-terrorist anit-public information program (re-FOIA). i am just thinking out loud here, but why no questions pertaining to route and source, is this not a very important factor?
CJD FOUNDATION QUESTIONNAIRE
REPORT FOR DATA BASE OF PATIENTS WITH CREUTZFELDT--JAKOB DISEASE (CJD) OR OTHER TRANSMISSIBLE SPONGIFORM ENCEPHALOPATHIES (TSE's)
Name of Patient*: (not required; if provided, must be with express consent of family member)
Date form filled out: / / (mm/dd/yy)
Person filling out form:
Relationship of person filling out form to patient:
Location where patient died: State: County: City:
Location where patient resided: State: County: City:
Sex of patient: male female unknown
Race of patient: white African-American -- Asian/Pacific Islander American-Indian/Alaskan Native Other (please identify: Unknown
Patient's date of birth: (mm/dd/yy)
Age of patient at onset of symptoms:
Date of patient's initial symptoms: (mm/dd/yy)
Age of patient at time of death:
Patient's date of death: (mm/dd/yy)
Duration of illness: months
Was this case referred to the National Prion Disease Pathology Surveillance Center at Case Western Reserve University in Cleveland, Ohio? yes no unknown
If yes, by whom was this case referred? Pathologist -- Neuropathologist -- Neurologist Other Physician (please identify which kind: Unknown
Who made initial diagnosis of CJD or other TSE?
Pathologist - Neuropathologist - Neurologist Other Physician (please identify which kind: ) Unknown
Please describe the clinical neurological presentation of the illness (list the symptoms or signs):
at onset of the illness:
during the course of illness:
Was an EEG (electroencephalogram) performed? yes -- no -- unknown
If yes,
how long after onset was the EEG performed?
how many times was the EEG performed?
can you indicate the results?
- slow periodic sharp waves (PSW)
- unilateral periodic sharp waves (LSW)
- not reported
- other
Was the cerebrospinal fluid tested for the 14-3-3 protein? yes - no - unknown
If yes, what was the result? positive - negative - unknown
Was a brain biopsy performed? - yes - no - unknown
If yes, what was the result?_____positive for____
______negative for CJD and other TSE's
______unknown
Was an autopsy performed? yes - no - unknown
If yes, what was the result? _____positive for____
______negative for CJD and other TSE's
______unknown
Was the neuropathology of this case consistent with new variant CJD? yes - no - unknown
What was the final diagnosis of this case?
___CJD, probably sporadic
___Familial (hereditary) CJD
___Iatrogenic (by infection) CJD; please specify_______________
___Gerstmann-Strausster-Scheinker Syndrome (GSS)
___Fatal Familial Insomnia (FFI)
___Other
___Unknown
* I hereby give consent to the Creutzfeldt-Jakob Disease Foundation, Inc. to use the above information, including name of patient if supplied, in connection with activities to promote the research, education and awareness of Creutzfeldt-Jakob Disease and related transmissible spongiform encephalopathies.
-4-
END ====================================================
4.5 MILLION DEMENTED ALZHEIMER'S, HOW MANY ARE CJD/TSEs?
how can on-in-a-million be accurate when CJD is not reportable, when the elderly rarely if ever get autopsied?
Subject: Re: Hello Dr. Manuelidis Date: Fri, 22 Dec 2000 17:47:09 -0500 From: laura manuelidis Reply-To: laura.manuelidis@yale.edu Organization: Yale Medical School To: "Terry S. Singeltary Sr." References: <39b5561a .87b84a28="" wt.net=""> <39b64574 .a4835745="" yale.edu=""> <39b680d8 .3872535b="" wt.net=""> <39b66ef1 .4ce25685="" yale.edu=""> <39bbb812 .425109f="" wt.net=""> <39be84cb .d7c0c16b="" yale.edu=""> <3a3ba197 .7f60d376="" wt.net="">
Dear Terry,
One of our papers (in Alzheimer's Disease Related Disord. 3:100-109, 1989) in text cites 6 of 46 (13%) of clinical AD as CJD. There may be a later paper from another lab showing the same higher than expected incidence but I can't put my hands on it right now. We also have a lot of papers from 1985 on stating that there are likely many silent (non-clinical) CJD infections, i.e. much greater than the "tip of the iceberg" of long standing end-stage cases with clinical symptoms. Hope this helps.
best wishes for the new year laura manuelidis
also;
Occasional PrP plaques are seen in cases of Alzheimer’s Disease, where they coexist with the more usual beta amyloid plaques. (Ref. Baker H. F. Ridley R.M. Duchen L.W. Crow T.J. Bruton C.J. Induction of beta (A4) amyloid in primates by injection of Alzheimer’s disease brain homogenate. Mol. Neurobiol (1994) 8: 25-39.) (J/MN/8/25)
re-alzheimer's disease
(note a substantial increase on a yearly basis)
http://www.bseinquiry.gov.uk/files/yb/1988/07/08014001.pdf
Diagnosis of dementia: Clinicopathologic correlations
Francois Boller, MD, PhD; Oscar L. Lopez, MD; and John Moossy, MD
Article abstract--Based on 54 demented patients consecutively autopsied at the University of Pittsburgh, we studied the accuracy of clinicians in predicting the pathologic diagnosis. Thirty-nine patients (72.2%) had Alzheimer's disease, while 15 (27.7%) had other CNS diseases (four multi-infarct dementia; three Creutzfeldt-Jakob disease; two thalamic and subcortical gliosis; three Parkinson's disease; one progressive supranuclear palsy; one Huntington's disease; and one unclassified). Two neurologists independently reviewed the clinical records of each patient without knowledge of the patient's identity or clinical or pathologic diagnoses; each clinician reached a clinical diagnosis based on criteria derived from those of the NINCDS/ADRDA. In 34 (63 %) cases both clinicians were correct, in nine (17%) one was correct, and in 11 (20%) neither was correct. These results show that in patients with a clinical diagnosis of dementia, the etiology cannot be accurately predicted during life.
NEUROLOGY 1989;39:76-79
Evaluation of Cerebral Biopsies for the Diagnosis of Dementia
Christine M. Hulette, MD; Nancy L. Earl, Md; Barbara J. Crain, MD, Phd
· To identify those patients most likely to benefit from a cerebral biopsy to diagnose dementia, we reviewed a series of 14 unselected biopsies performed during a 9-year period (1980 through 1989) at Duke University Medical Center, Durham, NC. Pathognomonic features allowed a definitive diagnosis in seven specimens. Nondiagnostic abnormalities but not diagnostic neuropathologic changes were seen in five additional specimens, and two specimens were normal. Creutzfeldt-Jakob disease was the most frequent diagnosis. One patient each was diagnosed as having Alzheimer's disease, diffuse Lewy body disease, adult-onset Niemann-Pick disease, and anaplastic astrocytoma. We conclude that a substantial proportion of patients presenting clinically with atypical dementia are likely to receive a definitive diagnosis from a cerebral biopsy. However, in those with coexisting hemiparesis, chorea, athetosis, or lower motor neuron signs, cerebral biopsies are less likely to be diagnostic. (Arch Neurol. 1992;49:28-31)
also;
snip...
Comment
Coexistence of Creutzfeldt-Jakob disease (CJD) and AD in some patients has been described but appears mainly related to age in patients proven to have CJD.4 However, since the individuals in the Swiss family died over a long interval and were all similarly affected, it is unlikely that CJD is purely coincidental. On the other hand, familial Gerstmann-Straüssler-Scheinker disease can present a variant with concomitant neurofibrillary tangle and prion-positive plaques, but not [beta] -amyloid-positive plaques. Within this variant, 2 mutations in the gene for the PrP have been identified in 2 different families, and the clinical profile with cerebellar ataxia and extrapyramidal signs5 differs from our findings.2 Base pair deletion in the prion gene segregating as an uncommon polymorphism has been described in a family with a history of late-onset AD, but there is no neuropathological confirmation and the genetic association is uncertain.6
Thus, the data presented herein support the existence of a possible new subtype of familial early-onset AD with a concomitant [beta] -amyloid and prion brain pathology, together with a massive neurofibrillary tangle degeneration. Although all known mutations have been excluded in the coding regions of the AD genes, numerous candidate chromosome sites, either in the AD genes outside the coding regions or in other genes including PrP, must be considered.
G. Leuba, PhD, PD K. Saini, PhD University Psychogeriatrics Hospital Lausanne-Prilly, Switzerland
A. Savioz, PhD Y. Charnay, PhD University of Geneva School of Medicine Geneva, Switzerland
1. Cruts M, Van Broekhoven C. Molecular genetics of Alzheimer's diease. Ann Med. 1998;6:560-565.
2. Savioz A, Leuba G, Forsell C, et al. No detected mutations in the genes for the amyloid precursor protein and presenilins 1 and 2 in a Swiss early-onset Alzheimer's disease family with a dominant mode of inheritance. Dement Geriatr Cogn Disord. 1999;10:431-436. MEDLINE
3. Boris N, Mestre-Frances N, Charnay Y, Tagliavini F. Spontaneous spongiform encephalopathy in a young adult rhesus monkey. Lancet. 1996;348:55. MEDLINE
4. Hainfellner JA, Wanschitz J, Jellinger K, Liberski PP, Gullotta F, Budka H. Coexistence of Alzheimer-type neuropathology in Creutzfeldt-Jakob disease. Acta Neuropathol (Berl). 1998;96:116-122. MEDLINE
5. Ghetti B, Tagliavini F, Giaccone G, et al. Familial Gerstmann-Straüssler-Scheinker disease with neurofibrillary tangles. Mol Neurobiol. 1994;8:41-48. MEDLINE
6. Perry RT, Go RCP, Harrell LE, Acton RT. SSCP analysis and sequencing of the human prion protein gene (PRNP) detects two different 24 bp deletions in an atypical Alzheimer's disease family. Am J Med Genet. 1995;60:12-18. MEDLINE
Funding/Support: This study was supported by grants 3100-045960.95 and 3100-043573.95 from the Swiss National Science Foundation.
my point being;
Diagnosis and Reporting of Creutzfeldt-Jakob Disease T. S. Singeltary, Sr; D. E. Kraemer; R. V. Gibbons, R. C. Holman, E. D. Belay, L. B. Schonberger
TSS
########### http://mailhost.rz.uni-karlsruhe.de/warc/bse-l.html ############
FRIDAY, JANUARY 31, 2014
Confidentiality in preclinical Alzheimer disease studies
snip...
Subject: Lord Lucas asked Her Majesty's Government about insurance company's and CJD???
Date: Thu, 6 Apr 2000 09:49:14 –0700
From: "Terry S. Singeltary Sr."
Reply-To: Bovine Spongiform Encephalopathy
To: BSE-L@uni-karlsruhe.de
######### Bovine Spongiform Encephalopathy #########
Greetings Everyone, I am deeply concerned about the answer given to Lord Lucas on CJD and insurance company's. In Her Majesty's reply, the reason given for insurance company's _not_ being able to require candidates for life insurance to be tested for incipient nvCJD or any human TSE, was because there is no test to date, that would allow them to test. My question to Her Majesty's Court would have been; when such a test is available, will the insurance company's be allowed to test for human TSE's? It seems Lord Lucas question was not answered fully, it seems Her Majesty's Court just went around the question. If in fact, the insurance company's are allowed to do this, once again the people would have been deceived by their government, for the sake of money, greed, and corporate industry$$$ This would be devastating to the people, not only have they been murdered by corporate greed, but they then would be sold out, for corporate greed. It's a no-win situation for public consumers... kind regards,
Terry S. Singeltary Sr., Bacliff, Texas USA
April 4, 2000 Lord Lucas asked Her Majesty's Government: Whether they will permit insurance companies to require that candidates for life insurance be tested for incipient new-variant CJD.[HL1661] Lord Hunt of Kings Heath: Insurance companies would be unable to introduce such a step, as no acceptable test currently exists for the demonstration of infection before the onset of clinical symptoms.
snip...full text ;
Tuesday, May 21, 2013
IS ALZHEIMER’S DISEASE A PRION DISEASE? the possible secondary transmission by blood transfusion are posed
THURSDAY, FEBRUARY 15, 2018
Iatrogenic Creutzfeldt-Jakob disease with Amyloid-β pathology: an international study
Terry S. Singeltary Sr.
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