First autopsy proven case of VPSPr: Variably protease‐sensitive prionopathy in Japan
P2‐105
First autopsy proven case of VPSPr: Variably protease‐sensitive prionopathy in Japan
Kazuko Hasegawa1; Saori Oonuma1; Kanako Komatsu2; Yuko Saito2; Saburo Yagishita1; Tetsuyuki Kitamoto3
1Department of Neurology, Sagamihara National Hospital, National Hospital Organization, Sagamihara, Japan; 2Department of Neuropathology, NCNP, Kodaira, Japan; 3Division of Neurological Science, Tohoku University school of medicine, Sendai, Japan
Introduction: Variably protease‐sensitive prionopathy: VPSPr is a newly described human prion disease in the spectrum of Creutzfeldt‐Jakob disease: CJD in 2008. In UK and USA cohort study in 2013, only 5 cases of VPSPr have been identified (prospectively and retrospectively) in UK, indicating VPSPr as a rare phenotype. Biochemical investigation characterizes that VPSPr shows detectable protease‐sensitive fragments. Some investigators reported that molecular overlaps can be found between usual protease‐resistant prionopathy and VPSPr in sporadic CJD.
Clinical summary: 81 y‐o women admitted to our hospital asked from GP, because of her memory disorder, rt‐sided dysesthesia, and high intensity ribbon‐like appearance in some cortices in DWI. At that time, she had several test: MMSE: 23 points, FAB: 6/30 points, CSF‐QUIC: negative, PSD on EEG: negative. Six months later, she hanged around and admitted into care center, but still she could eat. She died of pneumonia after 3.5 years from disease onset. Pathological findings and immunoblot for anti‐prion protein: Brain weight: 1186g, Macroscopic findings: Generally mild atrophy, but severe in the temporal pole.
Histological findings: Neuronal loss and vacuolation were diffusely detected in the cerebral cortex and the basal ganglia with anti‐prion antibody immunostaining (3F4). Mild neurofibrillary tangles, senile plaques and grains were also detected in the cerebral cortices. In immunoblot, variably protease‐sensitivity was detected as VPSPr.
Conclusion: The first case of sporadic CJD is reported as autopsy and immunochemical detected VPSPr in Japan.
P2‐108
Clinical courses of patients with Creutfeldt‐Jakob disease in Shizuoka Institute of Epilepsy and Neurological Disorders, Japan
Tomokazu Obi1; Takashi Matudaira1; Yasukiyo Araki1; Kinya Yamazaki1; Akira Sugiura1; Tatsuhiro Terada1; Yuta Nakano2; Tetsuyuki Kitamoto2; Shigeo Murayama3
1Department of Neurology, Shizuoka Institute of Epilepsy and Neurological Disorders; 2Department of Neurological Science, Tohoku University Graduate School of Medicine; 3Department of Neuropathology, Tokyo Metropolitan Geriatric Hospital
Background & Objective: From 2002, we have diagnosed and cared forty‐six Creuzfeldt‐Jakob disease (CJD) patients in Shizuoka Institute of Epilepsy and Neurological Disorders (SIEND).
Methods: 46 CJD patients presenting sequentially to SIEND between November 2003 and April 2018 were studied.
Results: All patients were clinically diagnosed as probable CJD based on prion disease medical treatment guidelines in Japan. Initial symptoms were gait disturbance 13, speech disturbance 6, apathy 6, visual disturbance 4, limb palsy 4, agraphia 2, geographical disorientation 2, dizziness 2, involuntary movement 2 and others 5. Onsets were usually acute (25) or subacute (8), but 12 patients abruptly developed neurological symptomes within one day. Mean age of onset was 69.0 years old. Sex was male 19 and female 27. Mean disease duration from onset to death was 86 weeks. Sporadic CJD patients were 33 cases. Genetic CJD patients were 13 cases including eleven E200K and two V180I. 38 CJD patients were cared, and eventually 35 patients died in SIEND. Autopsy was performed in 14 patients. 13 neuropathological findings showed definite diagnosis of CJD. We reported CJD patients having specific neuropathological findings and clinical utility of brain SPECT.
Conclusion: We reviewed 33 probable and 13 definite CJD patients. Abrupt onsets were frequently reported from family members. E200K mutations were very common in Genetic CJD patients. It is important to diagnose correctly and care CJD patients in central Shizuoka, Japan.
Symposium 24: S24‐1
Prion and Prion disease: An overview and challenges
Hidehiro Mizusawa1,2
1National Center of Neurology and Psychiatry; 2Tokyo Medical and Dental University
Prion diseases are devastating neurodegenerative diseases in humans such as Creutzfeldt‐Jakob disease (CJD) and many animal species including sheep, cow, deer and cat. CJD presents rapidly progressive dementia and other symptoms resulting in 100 percent death usually in months without any medicine to treat. Most CJD cases are sporadic and of unknown origin. There are also genetic forms such as genetic CJD, Gerstmann‐Straeussler‐Scheinker syndrome and Fatal Familial Insomnia and, rarely, acquired forms including iatrogenic CJD such as due to human dura mater grafts or human pituitary derived hormones. Prion diseases are caused by conversion of normal prion proteins to transmissible (infective) abnormal prion proteins (prion). Three Nobel Prizes have been awarded in this narrow field of science but mechanisms of conversion, transmission and neuronal degeneration are far from elucidation. Fortunately the outbreak of variant CJD transmitted through foods contaminated with prion of bovine spongiform encephalopathy was almost eliminated but unfortunately mechanism of infection to young adults is unknown. Chronic wasting disease of deer spreading in north America, south Korea and recently in northern Europe appears an emerging threat to us. Recent studies on A‐beta, Tau, alpha‐synuclein and others linked to Alzheimer's disease, Parkinson's disease and so on demonstrated they also share characteristics with prion proteins, notably auto‐aggregation, self‐propagation and induction of lesions in animals. These findings suggest that research and development of treatment on Prion disease would contribute greatly to overcome such neurodegenerative diseases. International cooperation all over the world is crucial in overcoming Prion diseases.
Symposium 24: S24‐2
Neuropathology of prion diseases: principles and more
Gabor G. Kovacs
Institute of Neurology, Medical University of Vienna, Vienna, Austria
Prion diseases may be triggered through infection, germline mutations in PRNP, and most frequently by yet unidentified “sporadic” events that generate disease‐associated PrP. Classical light microscopic features of prion diseases include spongiform change, neuronal loss, and astro‐ and microgliosis. Amyloid plaques are seen only in a subset of prion diseases. Immunostaining for disease‐associated PrP reveals a wide range of morphologies from fine to coarse and plaque‐like deposits. The codon 129 polymorphism in combination with the Western blot pattern of PrPres serves as a basis for molecular subtyping of sporadic Creutzfeldt‐Jakob disease (CJD) and is important to distinguish the BSE‐related variant CJD characterized by florid plaques in neuropathology. Genetic prion diseases are associated either with parenchymal or vascular PrP amyloidosis, with CJD–like features, or with thalamic degeneration as in fatal familial insomnia, Furthermore, novel phenotypes, including the variably protease sensitive prionopathy or the PrP systemic amyloidosis, or yet unclassifiable forms such as the dementia with thalamic degeneration and peculiar cortical PrP immunoreactivity, have been also described. Studies on the intracellular processing and regional distribution patterns of disease‐associated PrP, or the description of concomitant proteinopathies in prion diseases contributed to the understanding of other neurodegenerative diseases. Interestingly, amyloid‐beta is mostly associated with iatrogenic CJD, tau pathology is more frequently seen in sporadic CJD and variant CJD, while genetic prion diseases show distinct combinations of additional proteinopathies including amyloid‐beta, tau, and alpha‐synuclein, but not TDP‐43. Thus, neuropathology still provides remarkable observations to unravel the secrets of prion diseases and those with prion‐like features.
SATURDAY, SEPTEMBER 26, 2020
A nationwide trend analysis in the incidence and mortality of Creutzfeldt–Jakob disease in Japan between 2005 and 2014 with increasing trends of incidence and mortality
snip...
Overall, the AAPCs of age-adjusted CJD-associated mortality rates rose significantly over the study period (3.2%; 95% confidence interval [CI] 1.4–5.1%). The AAPC of the age-adjusted incidence rates also increased (overall 6.4%; 95% CI 4.7–8.1%). The CJD-associated increases in the mortality and incidence rates were especially prominent among adults over the age of 70 years. Given this trend in aging of population, the disease burden of CJD will continue to increase in severity. Our findings thus recommend that policymakers be aware of the importance of CJD and focus on preparing to address the increasing prevalence of dementia.
snip...
Chapter 10 - Variably protease-sensitive prionopathy
Author links open overlay panel Silvio Notari1 Brian S.Appleby1234 Pierluigi Gambetti1
1 Department of Pathology, Case Western Reserve University, Cleveland, OH, United States
2 National Prion Disease Pathology Surveillance Center, Case Western Reserve University, Cleveland, OH, United States
3 Department of Neurology, Case Western Reserve University, Cleveland, OH, United States
4 Department of Psychiatry, Case Western Reserve University, Cleveland, OH, United States
Available online 7 June 2018.
Abstract
Variably protease-sensitive prionopathy (VPSPr), originally identified in 2008, was further characterized and renamed in 2010. Thirty-seven cases of VPSPr have been reported to date, consistent with estimated prevalence of 0.7–1.7% of all sporadic prion diseases. The lack of gene mutations establishes VPSPr as a sporadic form of human prion diseases, along with sporadic Creutzfeldt–Jakob disease (sCJD) and sporadic fatal insomnia. Like sCJD, VPSPr affects patients harboring any of the three genotypes, MM, MV, and VV at the prion protein (PrP) gene polymorphic codon 129, with VPSPr VV accounting for 65% of all VPSPr cases. Distinguishing clinical features include a median 2-year duration and presentation with psychiatric signs, speech/language impairment, or cognitive decline. Neuropathology comprises moderate spongiform degeneration, PrP amyloid miniplaques, and a target-like or plaque-like PrP deposition. The abnormal PrP associated with VPSPr typically forms an electrophoretic profile of five to seven bands (according to the antibody) presenting variable protease resistance depending on the 129 genotype. The familial prion disease associated with the V180I PrP gene mutation which harbors an abnormal PrP with similar electrophoretic profile might serve as a model for VPSPr. Transmission to animals has definitively established VPSPr as a prion disease. Because of its recent identification, rarity, and the elusiveness of its abnormal PrP, VPSPr remains largely understudied.
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Keywords
sensitive transmissible sporadic anchorless internal fragment psychiatric abnormalities speech impairment cognitive declinenormal-pressure hydrocephalus atypical dementia
*** Conclusions. Preliminary results from transmission studies in bank voles strongly support the notion that VPSPr is a transmissible prion disease. Interestingly, VPSPr undergoes divergent evolution in the two genetic lines of voles, with sCJD-like features in BvM109 and GSS-like properties in BvI109. The discovery of previously unrecognized prion diseases in both humans and animals (i.e., Nor98 in small ruminants) demonstrates that the range of prion diseases might be wider than expected and raises crucial questions about the epidemiology and strain properties of these new forms. We are investigating this latter issue by molecular and biological comparison of VPSPr, GSS and Nor98.
Romolo Nonno,1 Michele Di Bari,1 Laura Pirisinu,1 Claudia D’Agostino,1 Stefano Marcon,1 Geraldina Riccardi,1 Gabriele Vaccari,1 Piero Parchi,2 Wenquan Zou,3 Pierluigi Gambetti,3 Umberto Agrimi1 1 Istituto Superiore di Sanità; Rome, Italy; 2 Dipartimento di Scienze Neurologiche, Università di Bologna; Bologna, Italy; 3 Case Western Reserve University; Cleveland, OH USA
Background. Variably protease-sensitive prionopathy (VPSPr) is a recently described “sporadic”neurodegenerative disease involving prion protein aggregation, which has clinical similarities with non-Alzheimer dementias, such as fronto-temporal dementia. Currently, 30 cases of VPSPr have been reported in Europe and USA, of which 19 cases were homozygous for valine at codon 129 of the prion protein (VV), 8 were MV and 3 were MM. A distinctive feature of VPSPr is the electrophoretic pattern of PrPSc after digestion with proteinase K (PK). After PK-treatment, PrP from VPSPr forms a ladder-like electrophoretic pattern similar to that described in GSS cases. The clinical and pathological features of VPSPr raised the question of the correct classification of VPSPr among prion diseases or other forms of neurodegenerative disorders. Here we report preliminary data on the transmissibility and pathological features of VPSPr cases in bank voles.
Materials and Methods. Seven VPSPr cases were inoculated in two genetic lines of bank voles, carrying either methionine or isoleucine at codon 109 of the prion protein (named BvM109 and BvI109, respectively). Among the VPSPr cases selected, 2 were VV at PrP codon 129, 3 were MV and 2 were MM. Clinical diagnosis in voles was confirmed by brain pathological assessment and western blot for PK-resistant PrPSc (PrPres) with mAbs SAF32, SAF84, 12B2 and 9A2.
Results. To date, 2 VPSPr cases (1 MV and 1 MM) gave positive transmission in BvM109. Overall, 3 voles were positive with survival time between 290 and 588 d post inoculation (d.p.i.). All positive voles accumulated PrPres in the form of the typical PrP27–30, which was indistinguishable to that previously observed in BvM109 inoculated with sCJDMM1 cases. In BvI109, 3 VPSPr cases (2 VV and 1 MM) showed positive transmission until now. Overall, 5 voles were positive with survival time between 281 and 596 d.p.i.. In contrast to what observed in BvM109, all BvI109 showed a GSS-like PrPSc electrophoretic pattern, characterized by low molecular weight PrPres. These PrPres fragments were positive with mAb 9A2 and 12B2, while being negative with SAF32 and SAF84, suggesting that they are cleaved at both the C-terminus and the N-terminus. Second passages are in progress from these first successful transmissions.
Conclusions. Preliminary results from transmission studies in bank voles strongly support the notion that VPSPr is a transmissible prion disease. Interestingly, VPSPr undergoes divergent evolution in the two genetic lines of voles, with sCJD-like features in BvM109 and GSS-like properties in BvI109. The discovery of previously unrecognized prion diseases in both humans and animals (i.e., Nor98 in small ruminants) demonstrates that the range of prion diseases might be wider than expected and raises crucial questions about the epidemiology and strain properties of these new forms. We are investigating this latter issue by molecular and biological comparison of VPSPr, GSS and Nor98.
Tables of Cases Examined
National Prion Disease Pathology Surveillance Center Cases Examined¹
Updated quarterly.
Last updated on: December 8th, 2020
8The sporadic cases include 4054 cases of sporadic Creutzfeldt-Jakob disease (sCJD), 73 cases of Variably Protease-Sensitive Prionopathy (VPSPr) and 35 cases of sporadic Fatal Insomnia (sFI).
Subject: CWD GSS TSE PRION SPINAL CORD, Confucius Ponders, What if?
Saturday, February 2, 2019
CWD GSS TSE PRION SPINAL CORD, Confucius Ponders, What if?
snip...
***> In particular the US data do not clearly exclude the possibility of human (sporadic or familial) TSE development due to consumption of venison. The Working Group thus recognizes a potential risk to consumers if a TSE would be present in European cervids.'' Scientific opinion on chronic wasting disease (II) <***
REVIEW
***> In conclusion, sensory symptoms and loss of reflexes in Gerstmann-Sträussler-Scheinker syndrome can be explained by neuropathological changes in the spinal cord. We conclude that the sensory symptoms and loss of lower limb reflexes in Gerstmann-Sträussler-Scheinker syndrome is due to pathology in the caudal spinal cord. <***
***> The clinical and pathological presentation in macaques was mostly atypical, with a strong emphasis on spinal cord pathology.<***
***> The notion that CWD can be transmitted orally into both new-world and old-world non-human primates asks for a careful reevaluation of the zoonotic risk of CWD. <***
***> 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.<***
***> In particular the US data do not clearly exclude the possibility of human (sporadic or familial) TSE development due to consumption of venison. The Working Group thus recognizes a potential risk to consumers if a TSE would be present in European cervids.'' Scientific opinion on chronic wasting disease (II) <***
Thursday, March 8, 2018
Familial human prion diseases associated with prion protein mutations Y226X and G131V are transmissible to transgenic mice expressing human prion protein
Saturday, February 2, 2019
CWD GSS TSE PRION SPINAL CORD, Confucius Ponders, What if?
FRIDAY, JANUARY 10, 2014
vpspr, sgss, sffi, TSE, an iatrogenic by-product of gss, ffi, familial type prion disease, what if ???
Greetings Friends, Neighbors, and Colleagues,
vpspr, sgss, sffi, TSE, an iatrogenic by-product of gss, ffi, familial type prion disease, what if ???
Confucius is confused again.
I was just sitting and thinking about why there is no genetic link to some of these TSE prion sGSS, sFFi, and it’s really been working on my brain, and then it hit me today.
what if, vpspr, sgss, sffi, TSE prion disease, was a by-product from iatrogenic gss, ffi, familial type prion disease ???
it could explain the cases of no genetic link to the gss, ffi, familial type prion disease, to the family.
sporadic and familial is a red herring, in my opinion, and underestimation is spot on, due to the crude prehistoric diagnostic procedures and criteria and definition of a prion disease.
I say again, what if, iatrogenic, what if, with all these neurological disorders, with a common denominator that is increasingly showing up in the picture, called the prion.
I urge all scientist to come together here, with this as the utmost of importance about all these neurological disease that are increasingly showing up as a prion mechanism, to put on the front burners, the IATROGENIC aspect and the potential of transmission there from, with diseases/disease??? in question.
by definition, could they be a Transmissible Spongiform Encephalopathy TSE prion type disease, and if so, what are the iatrogenic chances of transmission?
this is very important, and should be at the forefront of research, and if proven, could be a monumental breakthrough in science and battle against the spreading of these disease/diseases.
the US National Library of Medicine National Institutes of Health pub-med site, a quick search of the word SPORADIC will give you a hit of 40,747. of those, there are a plethora of disease listed under sporadic. sporadic simply means (UNKNOWN).
the US National Library of Medicine National Institutes of Health pub-med site, a quick search of the word FAMILIAL will give you a hit of 921,815. of those, there are a plethora of disease listed under familial.
again, sporadic and familial is a red herring, in my opinion.
also, in my opinion, when you start have disease such as sporadic Fatal Familial Insomnia, (and or sporadic GSS, or the VPSPr type prion disease), and there is NO familial genetic linkage to the family of the diseased, I have serious questions there as to a familial type disease, and thus, being defined as such.
*UPDATE* NOVEMBER 16, 2014 vpspr, sgss, sffi, TSE, an iatrogenic by-product of gss, ffi, familial type prion disease, what if ???
Friday, January 10, 2014
Monday, August 9, 2010
Variably protease-sensitive prionopathy: A new sporadic disease of the prion protein or just more Prionbaloney ?
Wednesday, March 28, 2012
VARIABLY PROTEASE-SENSITVE PRIONOPATHY IS TRANSMISSIBLE ...price of prion poker goes up again $
OR-10 15:25 - 15:40 VARIABLY PROTEASE-SENSITIVE PRIONOPATHY IS TRANSMISSIBLE IN BANK VOLES Nonno
Re-Evidence for human transmission of amyloid-β pathology and cerebral amyloid angiopathy
>>> 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
IN CONFIDENCE
5 NOVEMBER 1992
TRANSMISSION OF ALZHEIMER TYPE PLAQUES TO PRIMATES
[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.]
Volume 26, Number 8—August 2020
Sporadic Creutzfeldt-Jakob Disease among Physicians, Germany, 1993–2018 high proportion of physicians with sCJD were surgeons
THURSDAY, JULY 02, 2020
Variant Creutzfeldt–Jakob Disease Diagnosed 7.5 Years after Occupational Exposure
Wednesday, December 23, 2020
Creutzfeldt–Jakob Disease with a Five-Year Clinical Course, Multicentric Cerebellar Prion Plaques and Prior History of Biopsy-Proven Primary Angiitis of the Central Nervous System: A Case for Iatrogenic Exposure?
*** 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.
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
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=8006664&dopt=Abstract
8. Even though human TSE‐exposure risk through consumption of game from European cervids can be assumed to be minor, if at all existing, no final conclusion can be drawn due to the overall lack of scientific data. In particular the US data do not clearly exclude the possibility of human (sporadic or familial) TSE development due to consumption of venison. The Working Group thus recognizes a potential risk to consumers if a TSE would be present in European cervids. It might be prudent considering appropriate measures to reduce such a risk, e.g. excluding tissues such as CNS and lymphoid tissues from the human food chain, which would greatly reduce any potential risk for consumers. However, it is stressed that currently, no data regarding a risk of TSE infections from cervid products are available.
MONDAY, NOVEMBER 30, 2020
***> REPORT OF THE MEETING OF THE OIE SCIENTIFIC COMMISSION FOR ANIMAL DISEASES Paris, 9–13 September 2019 BSE, TSE, PRION
see updated concerns with atypical BSE from feed and zoonosis...terry
THURSDAY, DECEMBER 17, 2020
THE MAD COW BSE TSE PRION THAT STOLE CHRISTMAS DECEMBER 2003, WHAT REALLY HAPPENED, A REVIEW 2020
WEDNESDAY, DECEMBER 23, 2020
BSE research project final report 2005 to 2008 SE1796 SID5
WEDNESDAY, DECEMBER 23, 2020
Idiopathic Brainstem Neuronal Chromatolysis IBNC BSE TSE Prion a Review 2020
Monday, November 30, 2020
Tunisia has become the second country after Algeria to detect a case of Camel Prion Disease CPD within a year
TUESDAY, NOVEMBER 17, 2020
The European Union summary report on surveillance for the presence of transmissible spongiform encephalopathies (TSE) in 2019 First published 17 November 2020
WEDNESDAY, OCTOBER 28, 2020
EFSA Annual report of the Scientific Network on BSE-TSE 2020 Singeltary Submission
WEDNESDAY, DECEMBER 2, 2020
EFSA Evaluation of public and animal health risks in case of a delayed post-mortem inspection in ungulates EFSA Panel on Biological Hazards (BIOHAZ) ADOPTED: 21 October 2020
i wonder if a 7 month delay on a suspect BSE case in Texas is too long, on a 48 hour turnaround, asking for a friend???
WEDNESDAY, JULY 31, 2019
The agent of transmissible mink encephalopathy passaged in sheep is similar to BSE-L
THURSDAY, SEPTEMBER 24, 2020
The emergence of classical BSE from atypical/ Nor98 scrapie
WEDNESDAY, APRIL 24, 2019
USDA Announces Atypical Bovine Spongiform Encephalopathy Detection Aug 29, 2018 A Review of Science 2019
MONDAY, DECEMBER 21, 2020
BSE TSE Prion in zoo animals, exotic ruminants, domestic cats, and CPD Camel Prion Disease, a review 2020
WEDNESDAY, MAY 29, 2019
Incomplete inactivation of atypical scrapie following recommended autoclave decontamination procedures USDA HERE'S YOUR SIGN!
THURSDAY, AUGUST 20, 2020
Why is USDA "only" BSE TSE Prion testing 25,000 samples a year?
TUESDAY, DECEMBER 01, 2020
Sporadic Creutzfeldt Jakob Disease sCJD and Human TSE Prion Annual Report December 14, 2020
Wednesday, December 16, 2020
Expanding spectrum of prion diseases Prusiner et al
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.
Terry S. Singeltary Sr.
