PERSON TO PERSON TRANSMISSION OF THE TSE PRION DISEASE, never say never. as the disease mutates, it becomes more virulent in some cases, and cwd is efficiently transmitted from cervid to cervid. there are now multiple strains of CWD in cervids, as with the TSE prion disease in bovine, sheep and goats, and we now have the atypical TSE in these species, that have mutated, and some strains _have_ become more virulent. we now have younger humans dying from the TSE prion disease, with shorter incubation period, and that are much younger. human to human casual transmission of the TSE prion disease...again, never say never. ...TSS
A Kiss of a Prion: New Implications for Oral Transmissibility
Bianca Da Costa Dias and Stefan F. T. Weiss + Author Affiliations
School of Molecular and Cell Biology University of the Witwatersrand, Johannesburg South Africa Reprints or correspondence: Prof Stefan F. T. Weiss School of Molecular and Cell Biology University of the Witwatersrand Private Bag 3 2050 Wits Johannesburg South Africa (email@example.com). There is no doubt about it: prions-infectious particles composed mainly if not entirely of misfolded protein (scrapie-type prion protein [PrPSc]), which are the causative agents of transmissible spongiform encephalopathies (TSE) such as scrapie, variant Creutzfeldt-Jakob Disease (vCJD), and bovine spongiform encephalopathy (BSE)-are transmissible [1–3]. These agents may be introduced via intracerebral, intravenous, intraperitoneal, or intraventricular infection, and recent research indicates that oral transmission may also occur. The last mode of transmission is of particular interest because it indicates that the consumption of meat and other products derived from animals experiencing prion disorders may pose a real risk to humans. Recent reports suggest that, in addition to meat, bodily fluids such as blood, saliva, feces, and milk may well be risk factors for possible transmission of TSEs to humans. Successful oral transmission among different animal species (interspecies) has been demonstrated. However, species specificity, the “ species barrier,” and the mode of transmission must be taken into account and may explain why cattle, sheep, goats, mink, and mice are successfully orally infected with bovine scrapie-type prion protein (bovPrPSc), whereas the ingestion of bovPrPSc by pigs, poultry, and cervids such as elk and deer fails to cause disease . Humans are also thought to be susceptible to oral infection by bovPrPSc by means of contaminated bovine products (eg, meat pies), and this is believed to be the manner in which the zoonotic disease vCJD originated .
But where do prions hide in the body? They replicate primarily in the central nervous system, particularly in the brain and the lymphoreticular system , as well as in other tissues such as muscle . Furthermore, the presence of these infectious agents in bodily excretions and secretions is a major cause for concern, because it enhances the risks of transmissibility. Prions have been identified in feces of asymptomatic deer  and in the blood, saliva, and urine of deer with chronic wasting disease [7, 8]. PrPSc has also been detected in the salivary glands of scrapie-affected sheep .
The report by Maddison et al  in this issue of theJournal describes for the first time, to our knowledge, the secretion of prions into the oral cavity of sheep. The authors used silicon dioxide (SiO2) to concentrate prions, in conjunction with serial protein misfolding cyclic amplification, or sPMCA, a method to amplify and detect the presence of very low concentrations of PrPSc. Serial protein misfolding cyclic amplification has numerous applications, such as the sensitive detection of pathological prions , later application for in vitro generation of prions , and detection of prions in body fluids such as blood from scrapie-infected hamsters ; the last example succeeded even in the presymptomatic phase . Maddison et al  used this technique to demonstrate that prions are present in buccal swab samples obtained from sheep with preclinical scrapie infections.
However, one must pose the following question: how do ingested infectious PrPSc prions reach the mucus and saliva? After oral ingestion, prions are thought to be taken up first by Peyer patches before they disseminate through gut-associated lymphoid tissues, the lymphoreticular system, the vagus nerve, and the enteric nervous system, after which they enter the central nervous system . Internalization of prions in the intestine is thought to be performed by M-(microfold) cells  and by enterocytes, which internalize bovPrPSc dependent on the prion receptor LRP/LR .
Maddison et al  suggest, according to their data, that prions are able to spread from the small intestine to the oral salivary glands and epithelia within a period of 9 months. This route explains the occurrence of prions in saliva and the shedding of prions into the oral cavity.
The transmissibility of scrapie among sheep (intraspecies) is well recognized. It must be emphasized that horizontal transfer (from one individual to another) of scrapie is the main route of infection, because vertical transmission of disease from mother to offspring via milk or placental tissue occurs infrequently. Thus, in view of the report by Maddison et al, the oral transmissibility of prions among sheep may serve as a major route for horizontal scrapie transfer. This occurrence is plausible because sheep often lick each other. Maddison et al  indicate that, because of the similarities in prion tissue distribution, their implications for the oral transmission of ovine scrapie might be true for other prion diseases, such as cervid chronic wasting disease and human vCJD. If this is true for humans, a kiss of a prion may sometimes have lethal consequences.
Next Section Acknowledgments We thank the Deutsche Forschungsgemeinschaft (DFG) grant WE 2664/2–1, Germany and the National Research Foundation (NRF), South Africa, for financial support. We thank Professor Juergen Richt, Kansas State University, United States, for a critical reading of this paper.
Previous SectionNext Section Footnotes Potential conflicts of interest: none reported.
Financial support: Deutsche Forschungsgemeinschaft, Germany (grant WE 2664/2–1) and the National Research Foundation, South Africa.
we are (in my opinion), exposed to the TSE prion in so many different ways in every day life, the potential for exposure and then becoming infected via taking care of a loved one with TSE prion disease, in my opinion risk factor there from is minimal, if proper precautions are taken, and even if they were not, the chance of becoming infected from a kiss, or casual contact is low, but I do not think it is zero, actually, far from it. I put this all together for a documentation of the known facts to date, of the potential casual human to human transmission. I did not put it together to scare anyone. with aerosol transmission of the TSE prion a reality now, infectivity in urine and feces and transmission there from being reality now with the TSE prion disease, I don’t see how anyone can rule _out_ the potential for transmission of the TSE prion via a kiss (a vehicle for transmission of the TSE prion via saliva), or even for a cut or open wound (all a cut is and transmission there from, is an crude inoculation of sorts, and inoculation has been proven to be an efficient mode of transmission for the TSE prion disease), even the eye, from either one of the body fluids now that how proven to be infections. I can’t see why we have such safety protocols for laboratory workers working with the TSE prion disease, but yet the same officials will say it’s o.k. for the public, friends, and or family members to do just the opposite with their loved ones when succumbing to the CJD TSE prion disease. don’t get me wrong, I did it too, and would probably do it again as far as kissing my mom. but science is science, and the transmission studies speak for themselves with the bodily fluids. simply put, which is all I was saying, we can’t say never, and or that none of these cases to date, have not been, and or will not be, a potential vehicle for transmission. I believe, and this is my opinion, that more concern for casual transmission with body fluids and materials there from, should be put forth to families with their loved ones, and I think that the safety protocols there from should be revised, to match that of the laboratory settings. again, this is my opinion. your opinion, and or others here, may read the same science and feel different out the findings. ...take care, kind regards, terry
SUBSTANCE DATA SHEET
HUMAN PRION AGENTS
FOR USE IN RESEARCH LABORATORIES
SECTION I - INFECTIOUS AGENT
Name: Creutzfeldt-Jakob agent, Kuru agent
Synonym or Cross Reference:: Subacute spongiform encephalopathy, Creutzfeldt-Jakob disease (CJD), Kuru, Transmissible Spongiform Encephalopathy (TSE).
Characteristics: Filterable, self-replicating agent, slow infectious pathogen, prion protein (PrP)
SECTION II - RECOMMENDED PRECAUTIONS
Containment Requirements: Biosafety level 3 facilities, practices and containment equipment for activities involving these agents; also listed under biosafety level 2 with special precautions; level of containment will depend on the nature of the manipulations and the amount of sera, bio/necropsy materials handled
Protective Clothing: Gown and gloves when handling potentially infectious materials; eye protection may also be indicated
Other Precautions: Extreme care must be taken to avoid accidental autoinoculation or other parenteral inoculations of infectious tissues and fluids
SECTION III - HANDLING INFORMATION
Spills: Allow any potential aerosols to settle; wearing protective clothing, gently cover spill with paper towel and apply 1N sodium hydroxide, starting at perimeter and working towards the center; allow sufficient contact time (1 hour) before clean up
Disposal: Decontaminate before disposal; steam sterilization (132·C for 1 hour), disinfection with 1N sodium hydroxide for 1 hour, incineration
Storage: In sealed containers that are appropriately labeled
The main precaution to be taken by laboratorians working with prion-infected or contaminated material is to avoid accidental puncture of the skin.3 Persons handling contaminated specimens should wear cut-resistant gloves if possible. If accidental contamination of unbroken skin occurs, the area should be washed with detergent and abundant quantities of warm water (avoid scrubbing); brief exposure (1 minute to 1N NaOH or a 1:10 dilution of bleach) can be considered for maximum safety.6 Additional guidance related to occupational injury are provided in the WHO infection control guidelines.6 Unfixed samples of brain, spinal cord, and other tissues containing human prions should be processed with extreme care in a BSL-2 facility utilizing BSL-3 practices.
Bovine Spongiform Encephalopathy Although the eventual total number of variant CJD cases resulting from BSE transmission to humans is unknown, a review of the epidemiological data from the United Kingdom indicates that BSE transmission to humans is not efficient.9 The most prudent approach is to study BSE prions at a minimum in a BSL-2 facility utilizing BSL-3 practices. When performing necropsies on large animals where there is an opportunity that the worker may be accidentally splashed or have contact with high-risk materials (e.g., spinal column, brain) personnel should wear full body coverage personal protective equipment (e.g., gloves, rear closing gown and face shield). Disposable plasticware, which can be discarded as a dry regulated medical waste, is highly recommended. Because the paraformaldehyde vaporization procedure does not diminish prion titers, BSCs must be decontaminated with 1N NaOH and rinsed with water. HEPA filters should be bagged out and incinerated. Although there is no evidence to suggest that aerosol transmission occurs in the natural disease, it is prudent to avoid the generation of aerosols or droplets during the manipulation of tissues or fluids and during the necropsy of experimental animals. It is further strongly recommended that impervious gloves be worn for activities that provide the opportunity for skin contact with infectious tissues and fluids.
The main precaution to be taken when working with prion-infected or contaminated material is to avoid puncture of the skin. If accidental contamination of skin occurs, the area is swabbed with In sodium hydroxide (NaOH) for 5 minutes and then washed with copious amounts of water. Unfixed samples of brain, spinal cord, and other tissues containing human prions should be processed with extreme care at BSL 3.
Prions are characterized by extreme resistance to conventional inactivation procedures including irradiation, boiling, dry heat, and chemicals (formalin, betapropiolactone, alcohols). Sterilization of rodent brain extracts with high titers of prions requires autoclaving at 132C for 4.5 hours. Denaturing organic solvents such as phenol or chaotropic reagents such as guanidine isothiocyanate or alkali such as NaOH can also be used for sterilization. Disposable plasticware, which can be discarded as a dry waste, is highly recommended.
Although there is no evidence to suggest that aerosol transmission occurs in the natural disease, it is prudent to avoid the generation of aerosols or droplets during the manipulation of tissues or fluids and during the necropsy of experimental animals. Formaldehyde-fixed and paraffin-embedded tissues, especially of the brain, remain infectious. Some investigators recommend that formalin-fixed tissues from suspected cases of prion disease be immersed for 30 min in 96% formic acid or phenol before histopathologic processing, but such treatment may severely distort the microscopic neuropathology.
another interesting aspect of the TSE prion disease is KURU ;
Figure 25. All cooking. including that of human flesh from diseased kinsmen. was done in pits with steam made by pouring water over the hot stones, or cooked in bamboo cylinders in the hot ashes. Children participated in both the butchery and the handling of cooked meat, rubbing their soiled hands in their armpits or hair, and elsewhere on their bodies. They rarely or never washed. Infection with the kuru virus was most probably through the cuts and abrasions of the skin. or from nose-picking, rye (eye...tss) rubbing, or mucosal injury.
These detailed descriptions will be published elsewhere but have reaffirmed the oral histories of endocannibalism in the Fore recorded previously12,22–24 and that this practice ceased abruptly at the time of Australian administrative control over the kuru areas. Although isolated events might have occurred for a few years after this prohibition, we are confident that new exposures of individuals to kuru at mortuary feasts would not have occurred after 1960. Not only have no cases of kuru been recorded in people born after 1959 (and only nine were recorded in those born after 1956); but also all the 11 last recorded cases of kuru that we report here were born before 1950. If any source of infection remained, whether from surreptitious cannibalism, possible ground contam-ination with human prions at sites where food was prepared, or other lateral routes, we would expect individuals born after this period to have kuru—especially since children are thought to have had shorter incubation periods than adults. However, no such cases have been observed. Additionally, although a fraction of hamster-adapted scrapie prions have been shown to survive in soil for at least 3 years,25 the mortuary feast practices (during which the entire body would be consumed) were undertaken so that any substantial contamination of soil would not have occurred, and traditional bamboo knives and leaf plates were burned after the feast. Furthermore, no clusters of kuru cases, as seen earlier in the epidemic,26 have been recorded for many years....
Kuru: The Science and the Sorcery
Special Jury Prize Winner, Pacific International Documentary Film Festival 2011.
This is the true story of one of the most incredible and challenging medical detective stories of the 20th Century; a history of human tragedy, adventure and discovery. It is the story of the Fore, a Papuan community immersed in cannibalistic mortuary practices and sorcery in one of the most remote regions on the planet, and the tragic disease that threatened to wipe out their entire population.
In 1961, a young Australian medical researcher, Michael Alpers, puts up his hand to work on a new and strange disease in the Eastern Highlands of Papua New Guinea. There, he teams up with an American outer, Dr Carleton Gajdusek, who has been in the local Fore region since 1957. For Michael it is the beginning of a lifelong obsession.
Together, they are amidst a major epidemic. It is killing over 200 people a year with devastating effects. It mainly targets women and children. The local people, the Fore, call the disease kuru, their word for shivering. They believe it is caused by sorcery.
Michael and Carleton are baffled by the disease. There are no scientific disciplines to guide them as they attempt to unravel its mysteries. By pure chance, a link is made to a strange transmissible animal disease in sheep, Scrapie. The two kuru researchers embark on a 10-year experiment to see if the fatal degenerative brain disease in humans could be transmissible like Scrapie.
The decision is made to perform an autopsy on a kuru victim and inoculate the kuru material into a chimpanzee. Kigea, ayoung girl in the village is identified as being in the early stages of kuru. Kigea’s family, gives Michael permission to perform an autopsy upon her death.
A brain sample taken from Kigea after her death is flown to the USA and injected into a chimpanzee called Daisy. While Michael follows the progress of the transmission experiment, he starts to collate all the recorded data on kuru and begins to suspect cannibalism as the cause of the spreadof the disease.
Within two years, he diagnoses Daisy with kuru. This is a defining moment. It confirms kuru is transmissible and can cross the species barrier. The revelation, together with epidemiological data collated with anthropologist Shirley Lindenbaum, links the Fore’s mortuary feasts (consumption of dead relatives) to the transmission of kuru. Cannibalism is the cause, and its origin is linked to a rare disease called Creutzfeldt Jakob Disease(CJD), but the story of kuru is far from over.
The infecting agent is the first new pathogen – prions – to be discovered in over 100 years. Research results in two Nobel prizes: it’s discoveries turning scientific understanding upside down, causing rifts in the beliefs ofthe science community.
Then Mad Cow Disease (Bovine Spongiform Encephalopathy or BSE) reared its head in the mid 1980s, and 10 years later the human variant CJD. All eyes turned to kuru, the only model of a prion epidemic in human populations. Many unknowns still surround prion diseases: there is no cure for kuru, or any of the prion diseases. The effects are devastating and unprecedented incubation periods can extend beyond 50 years.
Michael is the key and heart to this story, providing unique access to the Fore people, and the world’s other leading authorities on the matter; including Americans Prof. DC Gajdusek (Nobel Prize 1976), Prof. Stan Prusiner (Nobel Prize 1997), Prof Shirley Lindenbaum (Anthropologist) and British Prof. John Collinge (Director, MRC Prion Unit, UK).
Kuru: The Science and the Sorcery combines history, science and anthropology to tell a unique and ongoing ‘history of science’ documentary spanning five decades. It intertwines the thinking of great minds, locally and internationally, to reveal how this rare disease in the remote highlands of PNG exploded to international attention and how Prion research has now revealed we are all descendants of a remote past of cannibal practices.
Kuru: The Science and the Sorcery Australian scientist Michael Alpers dedicated over 50 years to researching Kuru, an obscure and incurable brain disease unique to the Fore people of New Guinea. Kuru was once thought to be a psychosomatic illness, an infection, a genetic disorder, even a sorcerer's curse, but Alpers' findings pointed to cannibalism as the culprit. Yet a recent discovery has proven to be even more disturbing: the malady is linked to mad cow disease and its human equivalent, variant CJD. With a decades-long incubation period, could a larger outbreak be on its way?
human flesh taste very sweet
KURU EPIDEMIOLOGICAL PATROLS
People of the Kuru region part 1
boy playing with animal bladder, blowing it up like a balloon. ...
People of the Kuru region part 2
Monday, November 19, 2012
Prion in Saliva of Bovine Spongiform Encephalopathy–Infected Cattle
Prion transmission is usually not considered to be airborne like influenza or chicken pox. But we and others recently have found that prions can also be efficiently transmitted to mice through aerosols , . Although aerosol-transmitted prions have never been found under natural conditions, this finding highlights the necessity of revising the current prion-related biosafety guidelines and health standards in diagnostic and scientific laboratories being potentially confronted with prion-infected materials.
Thursday, December 29, 2011
Aerosols An underestimated vehicle for transmission of prion diseases?
please see more on Aerosols and TSE prion disease here ;
Monday, November 26, 2012
Aerosol Transmission of Chronic Wasting Disease in White-tailed Deer
Simultaneous Onset of Alzheimer's Disease in a Husband and Wife in Their Mid Fifties: What do We Really Know?
Jonathan Heath1, Lindsay Goicochea2, Mark Smith3, Rudy Castellani4. 1Department of Pathology, University of Maryland; 2University; 3Case Western Reserve University; 4University of Maryland, Baltimore, Maryland
Whereas the genetic factors influencing the development and expression of Alzheimer's disease are well characterized, environmental factors are currently thought to play a marginal role. Such factors as prior closed head injury, post-menopausal estrogen deficiency, aluminum exposure, smoking, diabetes, atherosclerotic cardiovascular disease, and diet, among others, confer only a modest increased risk if any, and are only tangentially considered in the major pathogenic cascades that are presently hypothesized. We present the simultaneous onset of Alzheimer's disease in a husband and wife, with both subjects experiencing cognitive dysfunction within the same month. Both subjects were in their mid-fifties at the time of presentation, both subjects showed progressively neurological decline with prominent memory loss, both subjects experienced myoclonus late in their disease course prompting referral to the National Prion Disease Pathology Surveillance Center, and both subjects expired 12 years after onset, within two months of each other. Review of the family pedigree revealed no family history of dementia or other neurologic illnesses in multiple first degree relatives. The only historical finding of note was that both subjects had moved out of their home briefly while it was being remodeled, and both became symptomatic shortly after moving back in. At autopsy, the subjects had classic advanced Alzheimer's disease, with Braak stage VI pathology that was otherwise identiical in quantity and distribution of amyloid-beta, cerebral amyloid angiopathy, and neurofibrillary degeneration. While no specific toxin or other environmental cause was discerned, these two cases raise the issue of epigenetic factors in Alzheimer's disease that may be more robust than current literature indicates.
NEUROLOGY 1998;50:684-688 © 1998 American Academy of Neurology
Creutzfeldt-Jakob disease in a husband and wife
P. Brown, MD, L. Cervenáková, MD, L. McShane, PhD, L. G. Goldfarb, MD, K. Bishop, BS, F. Bastian, MD, J. Kirkpatrick, MD, P. Piccardo, MD, B. Ghetti, MD and D. C. Gajdusek, MD From the Laboratory of CNS Studies (Drs. Brown, Cervenáková, Goldfarb, and Gajdusek), NINDS, and Biometric Research Branch (Dr. McShane), NCI, National Institutes of Health, Bethesda, MD; the Department of Obstetrics (K. Bishop), Gynecology and Reproductive Sciences, University of Texas Houston Health Science Center, Houston, TX; the Department of Pathology (Dr. Bastian), University of South Alabama Medical Center, Mobile, AL; the Department of Pathology (Dr. Kirkpatrick), The Methodist Hospital, Houston, TX; and the Department of Pathology (Drs. Piccardo and Ghetti), Indiana University School of Medicine, Indianapolis, IN.
Address correspondence and reprint requests to Dr. Paul Brown, Building 36, Room 5B21, National Institutes of Health, Bethesda, MD 20892.
A 53-year-old man died of sporadic Creutzfeldt-Jakob disease (CJD) after a 1.5-year clinical course. Four and a half years later, his then 55-year-old widow died from CJD after a 1-month illness. Both patients had typical clinical and neuropathologic features of the disease, and pathognomonic proteinase-resistant amyloid protein ("prion" protein, or PrP) was present in both brains. Neither patient had a family history of neurologic disease, and molecular genetic analysis of their PrP genes was normal. No medical, surgical, or dietary antecedent of CJD was identified; therefore, we are left with the unanswerable alternatives of human-to-human transmission or the chance occurrence of sporadic CJD in a husband and wife.
Received May 5, 1997. Accepted in final form September 10, 1997.
SEE CJD IN MAN AND HIS CAT ;
[Image] Research letters Volume 352, Number 9134 [Image] 3 October 1998 [Previous] [Next]
Simultaneous occurrence of spongiform encephalopathy in a man and his cat in Italy
Gianluigi Zanusso, Ettore Nardelli, Anna Rosati, GianMaria Fabrizi, Sergio Ferrari, Antonella Carteri, Franco De Simone, Nicola Rizzuto, Salvatore Monaco
Transmissible spongiform encephalopathies (TSE) encompass inherited, acquired, and sporadic mammalian neurological disorders, and are characterised by the conversion of the cellular prion protein (PrP) in an insoluble and protease-resistant isoform (PrPres). In human TSE, four types of PrPres have been identified according to size and glycoform ratios, which may represent different prion strains. Type-1 and type-2 PrPres are associated with sporadic Creutzfeldt-Jakob disease (CJD), type 3 with iatrogenic CJD, and type 4 with variant CJD.1,2 There is evidence that variant CJD is caused by the bovine spongiform encephalopathy (BSE)-prion strain.2-4 The BSE strain has been identified in three cats with feline spongiform encephalopathy (FSE), a prion disease which appeared in 1990 in the UK.5 We report the simultaneous occurrence of sporadic CJD in a man and a new variety of FSE in his cat.
A 60-year-old man, with no unusual dietary habits, was admitted in November, 1993, because of dysarthria, cerebellar ataxic gait, visual agnosia, and myoclonus. An electroencephalogram (EEG) showed diffuse theta-delta activity. A brain magnetic resonance imaging scan was unremarkable. 10 days later, he was speechless and able to follow only simple commands. Repeat EEGs showed periodic triphasic complexes. 2 weeks after admission, he was mute, akinetic, and unable to swallow. He died in early January, 1994.
His 7-year-old, neutered, female shorthaired cat presented in November, 1993, with episodes of frenzy, twitching of its body, and hyperaesthesia. The cat was usually fed on canned food and slept on its owner's bed. No bites from the cat were recalled. In the next few days, the cat became ataxic, with hindquarter locomotor dysfunction; the ataxia got worse and there was diffuse myoclonus. The cat was killed in mid-January, 1994.
No pathogenic mutations in the patient's PrP gene were found. The patient and the cat were methionine homozygous at codon 129. Histology of the patient's brain showed neocortical and cerebellar neuronal loss, astrocytosis, and spongiosis (figure A). PrP immunoreactivity showed a punctate pattern and paralleled spongiform changes (figure B). The cat's brain showed mild and focal spongiosis in deeper cortical layers of all four lobes (figure C), vacuolated cortical neurons (figure D), and mild astrogliosis. The cerebellar cortex and the dentate nucleus were gliosed. Immunoreactive PrP showed a punctate pattern in neocortex, allocortex, and caudate nucleus (figure E). Western blot analysis of control and affected human and cat brain homogenates showed 3 PrP bands of 27-35 kDa. After digestion with proteinase K and deglycosylation, only samples from the affected patient and cat showed type-1 PrPres, with PrP glycoform ratios comparable to those observed in sporadic CJD1 (details available from author).
Microscopic sections of patient and cat brains
A: Occipital cortex of the patient showing moderate spongiform degeneration and neuronal loss (haematoxylin and eosin) and B: punctate perineuronal pattern of PrP immunoreactivity; peroxidase immunohistochemistry with monoclonal antibody 3F4. C: cat parietal cortex showing mild spongiform degeneration (haematoxylin and eosin).D: vacuolated neurons (arrow, haematoxylin and eosin), E: peroxidase immunohistochemistry with antibody 3F4 shows punctate perineuronal deposition of PrP in temporal cortex.
This study shows a spatio-temporal association between human and feline prion diseases. The clinical features of the cat were different from previously reported cases of FSE which were characterised by gradual onset of behavioural changes preceding locomotor dysfunction and ataxia.5 Neuropathological changes were also at variance with the diffuse spongiosis and vacuolation of brainstem neurons, seen in FSE.5 The synaptic pattern of PrP deposition, similar in the cat and in the patient, was atypical for a BSE-related condition. Evidence of a new type of FSE was further provided by the detection of a type-1 PrPres, other than the BSE-associated type 4.2 Taken together, our data suggest that the same agent strain of sporadic CJD was involved in the patient and in his cat.
It is unknown whether these TSE occurred as the result of horizontal transmission in either direction, infection from an unknown common source, or the chance occurrence of two sporadic forms.
1 Parchi P, Castellani R, Capellari S, et al. Molecular basis of phenotypic variablity in sporadic Creutzfeldt-Jakob disease. Ann Neurol 1996; 39: 767-78 [PubMed].
2 Collinge J, Sidle KCL, Meads J, Ironside J, Hill AF. Molecular analysis of prion strain variation and the aetiology of 'new variant' CJD. Nature 1996; 383: 685-90 [PubMed].
3 Bruce ME, Will RG, Ironside JW, et al. Transmissions to mice indicate that 'new variant' CJD is caused by the BSE agent. Nature 1997; 389: 498-501 [PubMed].
4 Hill AF, Desbruslais M, Joiner S, et al. The same prion strain causes vCJD and BSE. Nature 1997; 389: 448-50 [PubMed].
5 Pearson GR, Wyatt JM, Henderson JP, Gruffydd-Jones TJ. Feline spongiform encephalopathy: a review. Vet Annual 1993; 33: 1-10.
Sezione di Neurologie Clinica, Dipartimento di Scienze Neurologiche e della Visione, Università di Verona, Policlinico Borgo Roma, 37134 Verona, Italy (S Monaco; e mail rizzuto@Gorgorna.univr.it); and Istituto Zooprofilattico Sperimentale della Lombardia e dell' Emilia, Brescia
Terry S. Singeltary Sr. wrote:
######## Bovine Spongiform Encephalopathy #########
Greetings list members,
ODD that some FELINE in Italy seem to have this same or maybe very similar phenotype of TSE;
In October 1998 the simultaneous occurrence of spongiform encephalopathy in a man and his pet cat was reported. The report from Italy noted that the cat did not display the same clinical features as FSE cases previously seen. Indeed, the presence of a new type of FSE was suggested. The man was diagnosed as having sporadic CJD, and neither case (man nor cat) appeared to be affected by a BSE-related condition.
Case‐to‐case transmission in humans: case reports and series in which spread through everyday human contact is suggested There are six reports in which this possible mode of transmission is considered. The most recent is that of a couple from the USA who had been married for 30 years.47 The husband died at age 53. He had no relevant family history, but had had a rotator cuff repair one year before disease onset. His wife developed symptoms four and half years after her husband's death. She was morbidly obese and had had a previous hysterectomy, hernia repair and cholecystectomy. Both occasionally ate brains in the form of ‘kizka’, a type of sausage.
Immunocytochemistry confirmed pathogenic prion protein deposition in brain tissue from both husband and wife. Full sequencing of the open reading frame of the PRNP failed to demonstrate any pathogenic mutations. Another suspected conjugal case has recently been shown not to be CJD. The histopathological specimens did not stain for prion protein despite the microscopic appearance of spongiform change.48
Sporadic CJD has been described in two co‐workers who shared a school wing for 9 months.49 The first was a 48‐year‐old Californian‐born man of Hispanic American descent who had had a traumatic leg amputation at age 23, but was otherwise well. The second was a 48‐year‐old Chilean‐born male who had a blood transfusion 6 months before onset of symptoms, and was known to eat lambs' brains. The first patient developed symptoms 5 months after the last contact with his colleague and was confirmed to have spCJD 2 months after this. The second patient developed symptoms months later and died 9 months after the last contact with his colleague.
An English woman, who died of CJD, histologically confirmed at post mortem, was known to have contact with several affected members of a family with familial CJD and was related to them by marriage.39 She had known one of the family, who later died of CJD and had afternoon tea with her at family gatherings, twice a year, for 20 years, as well as visiting in her final illness. The woman herself died 12 years later. There is another similar case of probable CJD, reported in a Chilean woman who died 13 years after contact with a family with familial CJD. No details of contact are given. A third case of death from CJD in someone related in marriage to a family with familial CJD has been reported in France, in a Tunisian family. No details are given with regards to family history or contact.21 What is notable about these last three incidents of supposed infection by social contact is that all have occurred in association with familial CJD. Although these patients were not known to have been genetically related to their spouses, the possibility that they came from the same gene pool cannot be dismissed.
Coincident Scrapie Infection and Nephritis Lead to Urinary Prion Excretion
Seeger, Harald; Heikenwalder, Mathias; Zeller, Nicolas; Kranich, Jan; Schwarz, Petra; Gaspert, Ariana; Seifert, Burkhardt; Miele, Gino; Aguzzi, Adriano
Date of publication 2005 Language English Notes Includes references Medium text Pagination p. 324-326. Journal Title Science ISSN 0036-8075 Volume/Issue 2005 Oct. 14, v. 310, no. 5746 Abstract Prion infectivity is typically restricted to the central nervous and lymphatic systems of infected hosts, but chronic inflammation can expand the distribution of prions. We tested whether chronic inflammatory kidney disorders would trigger excretion of prion infectivity into urine. Urinary proteins from scrapie-infected mice with lymphocytic nephritis induced scrapie upon inoculation into noninfected indicator mice. Prionuria was found in presymptomatic scrapie-infected and in sick mice, whereas neither prionuria nor urinary PrP[superscript Sc] was detectable in prion-infected wild-type or PrP[superscript C]-overexpressing mice, or in nephritic mice inoculated with noninfectious brain. Thus, urine may provide a vector for horizontal prion transmission, and inflammation of excretory organs may influence prion spread.
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AGRIS 2013 - FAO of the United Nations
Detection of Prion Protein in Urine-Derived Injectable Fertility Products by a Targeted Proteomic Approach
Alain Van Dorsselaer mail, * E-mail: email@example.com (NRC); firstname.lastname@example.org (AVD)
Affiliation: Laboratoire de Spectrométrie de Masse Bio-Organique, Université de Strasbourg, IPHC, CNRS, UMR7178, Strasbourg, France
X Christine Carapito, Affiliation: Laboratoire de Spectrométrie de Masse Bio-Organique, Université de Strasbourg, IPHC, CNRS, UMR7178, Strasbourg, France
X François Delalande, Affiliation: Laboratoire de Spectrométrie de Masse Bio-Organique, Université de Strasbourg, IPHC, CNRS, UMR7178, Strasbourg, France
X Christine Schaeffer-Reiss, Affiliation: Laboratoire de Spectrométrie de Masse Bio-Organique, Université de Strasbourg, IPHC, CNRS, UMR7178, Strasbourg, France
X Daniele Thierse, Affiliation: Laboratoire de Spectrométrie de Masse Bio-Organique, Université de Strasbourg, IPHC, CNRS, UMR7178, Strasbourg, France
X Hélène Diemer, Affiliation: Laboratoire de Spectrométrie de Masse Bio-Organique, Université de Strasbourg, IPHC, CNRS, UMR7178, Strasbourg, France
X Douglas S. McNair, Affiliation: Cerner Corporation, Kansas City, Missouri, United States of America
X Daniel Krewski, Affiliation: McLaughlin Centre for Population Health Risk Assessment, University of Ottawa, Ontario, Canada
X Neil R. Cashman mail
Conclusions/Significance The presence of protease-sensitive prion protein in urinary-derived injectable fertility products containing hCG, hMG, and hMG-HP suggests that prions may co-purify in these products. Intramuscular injection is a relatively efficient route of transmission of human prion disease, and young women exposed to prions can be expected to survive an incubation period associated with a minimal inoculum. The risks of urine-derived fertility products could now outweigh their benefits, particularly considering the availability of recombinant products.
Citation: Van Dorsselaer A, Carapito C, Delalande F, Schaeffer-Reiss C, Thierse D, et al. (2011) Detection of Prion Protein in Urine-Derived Injectable Fertility Products by a Targeted Proteomic Approach. PLoS ONE 6(3): e17815. doi:10.1371/journal.pone.0017815
Editor: Jean-Luc Darlix, Institut National de la Santé et de la Recherche Médicale, France
Received: November 12, 2010; Accepted: February 10, 2011; Published: March 23, 2011
Discussion Using classical proteomic analyses, prion protein was detected for the first time in two u-hCG preparations, and was among 33 different non-gonadotropin proteins identified as contaminants of these pharmaceutical products. In contrast, r-hCG preparations were negative for prion proteins.
In one of the two u-hCG products tested, human prion protein was among the ten major contaminants. The fact that prion protein sequences were identified in several spots on our 2D electrophoresis gels is likely due to the presence of heterogeneous glycosylation and degraded prion protein forms. It is also worth noting that in the u-hCG preparation of manufacturer A, plasminogen was identified among the urinary impurities; plasminogen has been identified as a binding protein for disease-associated prion protein .
Both hMG and hMG-HP were tested using 2D gel electrophoresis. The results confirmed that the two hMGs tested were less pure than hMG-HP and contained a large number of total proteins (mainly represented by urinary impurities). Non-gonadotropin proteins present in hMG-HP products were identified by MS, resulting in 34 co-purified contaminants. Only gonadotropin proteins were seen in all the recombinant preparations analyzed by 2D gel electrophoresis. Using this 2D-gel/LC-MS/MS proteomic workflow, prion proteins were identified only in u-hCG and not in hMG-HP preparations. In parallel, a targeted proteomic approach (LC-SRM) was developed to detect human prion proteins which are sensitive to proteases. The method was optimized to provide quantitative data in each container of product. This is the most sensitive MS-based quantification technique currently available with a limit of detection in the low femtomolar range. This approach for prion protein detection, identification and quantification was used on all gonadotropin pharmaceutical preparations included in our study, including both urinary (hCG, hMG, hMG-HP) and recombinant products.
All urine-derived preparations tested, produced by different manufacturers, showed the presence of human prion proteins in varying amounts. These findings demonstrate that the purification processes for different urine-derived preparations are unable to remove prion proteins from the source material and that the process controls employed do not permit the identification of this contaminant.
Do the prion protein peptides detected in this study originate from infectious prions? Preparation of tryptic peptides is preceded by solubilization in 8M urea, which is adequate to disaggregate and denature the disease-associated isoform of the prion protein rendering it susceptible to trypsin digestion. It is also clear that native and diseased isoforms of the prion protein share affinity for chromatography substrates utilized to purify peptide hormones . Finally, infectious prions can range down in size to oligomers of a few dozen prion protein molecules , which would be undetectable by existing biochemical methodologies including MS methods employed in this study.
Although no cases of human prion disease due to the use of urinary gonadotropins have been recognized to date, the epidemiological signal for transmission may be difficult to detect. Each year, more than 300,000 young women in the US and Canada are prescribed urine-derived gonadotropins for infertility. Although the Food and Drug Administration and Health Canada once considered these products to be in the lowest category of risk for prion disease transmission, the discovery of full infectivity in the urine of nephritic scrapie-infected mice in 2005 led to new requirements for product labeling and a review of donor procedures and manufacturing processes. Additional recent findings suggest that urinary prion excretion can occur without renal pathology , . These results warrant a reassessment as to whether the risks of urine-derived fertility products could now outweigh their benefits, particularly considering the availability of recombinant products that do not require human urine as a substrate.
Although urinary gonadotropins have been previously characterized as safe , , this opinion may be overly optimistic in view of the present findings, supported by results from other recently published studies. Notably, blood products were once also considered ‘safe’, based on the lack of detectable prions in vCJD using an inadequately sensitive mouse bioassay . In line with recent published studies, the 2010 updated World Health Organization tables on ‘Tissue infectivity distribution in transmissible spongiform encephalopathy’ moved urine from the category of ‘Tissues with no detectable infectivity’ to the category of ‘Lower-infectivity tissue’ (the latter category includes blood) .
Current urine collection systems pool the urine of thousands of donors and, unlike the blood collection system, do not allow for donor tracing. There is also no mechanism of ensuring that the designated donor is actually the one who provides the urine, as donation is normally done at home. However, even if donor management and tracing were flawless, the fact that prionuria may exist well before the onset of clinically overt prion disease, without being detectable by current methods, remains a cause for concern. Furthermore, the now indisputable detection of prions in urine of experimental animals, the lack of a species barrier for human-to-human transmission, the relative efficiency of the intramuscular injection route for prion transmission, and the young age of fertility drug recipients all support application of the ‘precautionary principle’ for urinary derived pharmaceuticals. As risk management paradigms shift towards more proactive approaches intended to ‘anticipate and prevent’ emerging risks –, a careful examination of the risk of transmission of human prion disease through the use of urine-derived hormones and peptides would appear to be warranted.
Friday, March 25, 2011
Detection of Prion Protein in Urine-Derived Injectable Fertility Products by a Targeted Proteomic Approach
HD.13: CWD infection in the spleen of humanized transgenic mice
Liuting Qing and Qingzhong Kong Case Western Reserve University; Cleveland, OH USA
Chronic wasting disease (CWD) is a widespread prion disease in free-ranging and captive cervid species in North America, and there is evidence suggesting the existence of multiple CWD strains. The susceptibility of human CNS and peripheral organs to the various CWD prion strains remains largely unclear. Current literature suggests that the classical CWD strain is unlikely to infect human brain, but the potential for peripheral infection by CWD in humans is unknown. We detected protease-resistant PrpSc in the spleens of a few humanized transgenic mice that were intracerebrally inoculated with natural CWD isolates, but PrpSc was not detected in the brains of any of the CWD-inoculated mice. Our ongoing bioassays in humanized Tg mice indicate that intracerebral challenge with such PrpSc-positive humanized mouse spleen already led to prion disease in most animals. ***These results indicate that the CWD prion may have the potential to infect human peripheral lymphoid tissues.
HD.12: Comparative study of the distribution of the prion protein in the squirrel monkey (Saimiri sciureus) following experimental challenge with variant and sporadic CJD
Diane L. Ritchie,1 Paul Brown,2 Susan Gibson,3 Thomas R. Kreil,4 Christian Abee3 and James W. Ironside1 1National CJD Surveillance Unit; Edinburgh, UK; 2Bethesda; Bethesda, MD USA; 3Deparment of Comparative Medicine; University of South Alabama; Mobile, AL USA; 4Baxter Bioscience; Vienna, Austria
Introduction, Reports suggest that the number of tissues and organs showing the presence of the abnormal prion protein (PrPTSE) in variant CJD (vCJD) patients may be greater than previously thought. A limited peripheral involvement in some cases of sporadic CJD (sCJD) has also been reported. This accumulation of PrPTSE outside the brain has raised concerns about the possible iatrogenic transmission risk of vCJD. The squirrel monkey (Saimiri sciureus) has been shown to be highly susceptible to experimental challenge with human prion disease. Neuropathological and biochemical analyses of CNS tissue have shown that sCJD and vCJD can be distinguished in the squirrel monkey and that many of the strain characteristics that define these agents are conserved after transmission. Following on from these initial studies, immunohistochemistry and western blot analysis were performed on a wide range of peripheral tissues including, lymphoreticular tissues and peripheral neural tissue to establish the full-body distribution of PrPTSE in this primate animal model. Materials and Methods. Brain homogenates from sCJD or vCJD patients were inoculated into the frontal cortex of squirrel monkeys. Animals were kept under constant clinical surveillance. At post-mortem, formalin fixed CNS tissue and a wide range of peripheral tissues were taken for immunohistochemical analysis together with frozen tissues taken for the biochemical detection of PrPTSE. Results. Immunohistochemical analysis showed no evidence of PrPTSE deposition in peripheral tissues in either variant or sporadic CJD-infected animals. However, western blot assays detected PrPTSE in the spleen of a proportion of the vCJD- infected animals. The PrPTSE isotype resembled that detected in CNS tissue from the vCJD- infected animals and from human vCJD cases. ***In addition, western blot analysis detected PrPTSE in the spleen of a single animal following challenge with sporadic CJD. The PrPTSE type in this animal resembled that found in CNS tissue from the same animal, with a PrPTSE type similar to that found in human sCJD type 1 cases. Conclusion. This study confirms the accumulation of PrPTSE in the CNS and spleen of a proportion of squirrel monkeys infected intra-cerebrally with human vCJD. Furthermore, this study extends the evidence that there may be a peripheral involvement in some cases of sCJD. PrPTSE typing confirms the conservation of PrPTSE type on transmission to the squirrel monkey and suggests that there are no tissue-specific adaptations in the biochemical phenotype of the agent strain following primate-to-primate transmission.
Oral.15: Molecular barriers to zoonotic prion transmission: Comparison of the ability of sheep, cattle and deer prion disease isolates to convert normal human prion protein to its pathological isoform in a cell-free system
Marcelo A.Barria,1 Aru Balachandran,2 Masanori Morita,3 Tetsuyuki Kitamoto,4 Rona Barron,5 Jean Manson,5 Richard Kniqht,1 James W. lronside1 and Mark W. Head1 1National CJD Research and Surveillance Unit; Centre for Clinical Brain Sciences; School of Clinical Sciences; The University of Edinburgh; Edinburgh, UK; 2National and OIE Reference Laboratory for Scrapie and CWD; Canadian Food Inspection Agency; Ottawa Laboratory; Fallowfield. ON Canada; 3Infectious Pathogen Research Section; Central Research Laboratory; Japan Blood Products Organization; Kobe, Japan; 4Department of Neurological Science; Tohoku University Graduate School of Medicine; Sendai. Japan; 5Neurobiology Division; The Roslin Institute and R(D)SVS; University of Edinburgh; Easter Bush; Midlothian; Edinburgh, UK
Background. Bovine spongiform encephalopathy (BSE) is a known zoonotic prion disease, resulting in variant Creurzfeldt- Jakob disease (vCJD) in humans. In contrast, classical scrapie in sheep is thought to offer little or no danger to human health. However, a widening range of prion diseases have been recognized in cattle, sheep and deer. The risks posed by individual animal prion diseases to human health cannot be determined a priori and are difficult to assess empirically. The fundamemal event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein (PrPC) to its pathological isoform (PrPSc). Here we report the use of a rapid molecular conversion assay to test whether brain specimens from different animal prion diseases are capable of seeding the conversion of human PrPC ro PrPSc. Material and Methods. Classical BSE (C-type BSE), H-type BSE, L-type BSE, classical scrapie, atypical scrapie, chronic wasting disease and vCJD brain homogenates were tested for their ability to seed conversion of human PrPC to PrPSc in protein misfolding cyclic amplification (PMCA) reactions. Newly formed human PrPSc was detected by protease digestion and western blotting using the antibody 3F4. Results. C-type BSE and vCJD were found to efficiently convert PrPC to PrPSc. Scrapie failed to convert human PrPC to PrPSc. Of the other animal prion diseases tested only chronic wasting disease appeared to have the capability ro convert human PrPC to PrPSc. The results were consistent whether the human PrPC came from human brain, humanised transgenic mouse brain or from cultured human cells and the effect was more pronounced for PrPC with methionine at codon 129 compared with that with valine. Conclusion. Our results show that none of the tested animal prion disease isolates are as efficient as C-type BSE and vCJD in converting human prion protein in this in vitro assay. ***However, they also show that there is no absolute barrier ro conversion of human prion protein in the case of chronic wasting disease.
Invited.16: Studies of chronic wasting disease transmission in cervid and non-cervid species
Edward A, Hoover,1 Candace K. Mathiason,1 Davin M. Henderson,1 Nicholas J. Haley,1 Davis M. Seelig,1 Nathaniel D. Denkers,1 Amy V. Nalls,1 Mark D. Zabe,1 Glenn C. Telling,1 Fernando Goni2 and Thomas Wisniewski,2 1Prion Research Center; Colorado State University; Fort Collins, CO USA; 2New York University School of Medicine; New York, NY USA
How and why some misfolded proteins become horizontally transmitted agents and occasionally cross species barriers are issues fundamental to understanding prion disease. Chronic wasting disease (CWD) of cervids is perhaps a prototype of horizontal prion transmission, encompassing efficient mucosal uptake, lymphoid amplification, neuroinvasion, peripheralization, and dissemination via mucosal excretion. Efficient mucosal transmission of CWD in deer has been demonstrated by oral, nasal, aerosol, and indirect contact exposure. In addition, other studies (Mathiason CK, et al.) reported at the symposium support a significant role for pre- and/or postnatal transmission of CWD from doe to offspring. Accumulating, yet still incomplete, evidence also suggests that the period of relatively covert CWD infection may be longer than originally thought. Given the above, minimally invasive sensitive assays based on body fluids from live animals would aid substantially in understanding the biology of CWD. We have been applying seeded realtirne quaking-induced amplification of recombinant PrP substrates (i.e., RT-QuIC methodology) to: (1) investigate antemortem CWD detection, and (2) model PrP-based species barriers and trans-species adaptation-topics we previously explored using sPMCA and in vivo bioassays. At this symposium, we report sensitive and specific detection CWD prions in saliva, urine, blood (Mathiason lab), and rectal and pharyngeal lymph node samples (Haley NJ, et al.) from pre-symptomatic and symptomatic experimentally and naturally exposed deer. Other ongoing studies are employing RT-QuIC methodology to model amplification barriers among CWD, FSE, BSE, and CJD prions using cervine, feline, bovine, human, and promiscuous rPrP substrates and the above species prion seeds, cellular co-factors, and transgenic mice. Finally, in collaboration with the Wisniewski laboratory, we are conducting of experimental CWD vaccination studies in deer employing oral administration of an attenuated Salmonella vector expressing cervid PrP epitopes.
AD.06: Detecting prions in the brain and blood of TSE-infected deer and hamsters
Alan Elder,1 Davin Henderson,1 Anca Selariu,1 Amy Nalls,1 Byron Caughey,2 Richard Bessen,1 Jason Bartz3 and Candace Mathiason1 1Colorado State University; Fort Collins, CO USA; 2NIH Rocky Mountain Laboratories; Hamilton, MT USA; 3Creighton University; Omaha, NE USA
While large quantities of protease resistant prion protein (PrPres) can be demonstrated by western blot or IHC in lymphoid biopsies or post-mortem brain tissues harvested from prion-infected animals, these conventional assays are less reliable as means to detect the small quantities of prions thought to be present in bodily fluids or associated with early and asymptomatic phases of TSE disease. The Real Time-Quaking Induced Conversion (RT-QuIC) assay is capable of detecting prions at concentrations below the level of sensitivity of conventional assays and provides a real-time fluorescent readout negating the use of proteases. We have made modifications to the RT-QuIC assay to utilize it for the detection of PrPres in brain and blood harvested from various species infected with prions. In this study, we analyzed CWD-infected deer and CWD/TME-infected hamster whole blood to determine the effect of: (1) various anticoagulants, (2) freezing and (3) NaPTA precipitation. Brain tissue and blood collected from naive deer and hamsters served as negative controls. We were able to demonstrate amplifiable prions in (1) brain and blood samples harvested from CWD/TME-infected animals, (2) heparinized blood, (3) frozen vs. fresh blood and (4) NaPTA treated samples. The RT-QuIC assay is able to detect PrPres in various species of animals and shows promise as an antemortem diagnostic tool for blood-borne TSEs.
Oral.08: Mother to offspring transmission of chronic wasting disease in Reeve's Muntjac deer
Amy Nalls,1 Erin McNulty,1 Jenny Powers,2 Davis Seelig,1 Clare Hoover,1 Nicholas Haley,1 Jeanette Hayes-Klug,1 Kelly Anderson,1 Paula Stewart,3 Wilfred Goldmann,3 Edward A. Hoover1 and Candace K. Mathiason1 1Colorado State University; Fort Collins, CO USA; 2National Park Service; Fort Collins, CO USA; 3The Roslin Institute and Royal School of Veterinary Studies; Edinburgh, UK
To investigate the role mother to offspring transmission plays in chronic wasting disease (CWD), we have developed a cervid model employing the Reeve's muntjac deer (Muntiacus reevesi). Eight muntjac doe were orally inoculated with CWD and tested PrPCWD lymphoid positive by 4 mo post infection. Fourteen fawns were born to these eight CWD-infected doe-3 were born viable, 6 were born non-viable and 5 were harvested as fetuses from early or end-stage CWD-infected doe. All three viable fawns have demonstrated CWD IHC lymphoid biopsy positivity between 43 d post birth and 11 mo post birth. Two of these three CWD positive viable offspring have developed clinical signs consistent with TSE disease (28-33 mo post birth). Moreover, CWD prions have been detected by sPMCA in 11 of 16 tissues harvested from 6 full-term non-viable fawns and in 7 of 11 fetal tissues harvested in utero from the second and third trimester fetuses. Additional tissues and pregnancy related fluids from doe and offspring are being analyzed for CWD prions. In summary, using the muntjac deer model we have demonstrated CWD clinical disease in offspring born to CWD-infected doe, and in utero transmission of CWD from mother to offspring. These studies provide basis to further investigate the mechanisms of maternal transfer of prions.
AD.63: Susceptibility of domestic cats to chronic wasting disease
Amy V.Nalls,1 Candace Mathiason,1 Davis Seelig,2 Susan Kraft,1 Kevin Carnes,1 Kelly Anderson,1 Jeanette Hayes-Klug1 and Edward A. Hoover1 1Colorado State University; Fort Collins, CO USA; 2University of Minnesota; Saint Paul, MN USA
Domestic and nondomestic cats have been shown to be susceptible to feline spongiform encephalopathy (FSE), almost certainly caused by consumption of bovine spongiform encephalopathy (BSE)-contaminated meat. Because domestic and free-ranging nondomestic felids scavenge cervid carcasses, including those in areas affected by chronic wasting disease (CWD), we evaluated the susceptibility of the domestic cat (Felis catus) to CWD infection experimentally. Cohorts of 5 cats each were inoculated either intracerebrally (IC) or orally (PO) with CWD-infected deer brain. At 40 and 42 mo post-inoculation, two IC-inoculated cats developed signs consistent with prion disease, including a stilted gait, weight loss, anorexia, polydipsia, patterned motor behaviors, head and tail tremors, and ataxia, and progressed to terminal disease within 5 mo. Brains from these two cats were pooled and inoculated into cohorts of cats by IC, PO, and intraperitoneal and subcutaneous (IP/SC) routes. Upon subpassage, feline-adapted CWD (FelCWD) was transmitted to all IC-inoculated cats with a decreased incubation period of 23 to 27 mo. FelCWD was detected in the brains of all the symptomatic cats by western blotting and immunohistochemistry and abnormalities were seen in magnetic resonance imaging, including multifocal T2 fluid attenuated inversion recovery (FLAIR) signal hyper-intensities, ventricular size increases, prominent sulci, and white matter tract cavitation. Currently, 3 of 4 IP/SQ and 2 of 4 PO inoculared cats have developed abnormal behavior patterns consistent with the early stage of feline CWD. These results demonstrate that CWD can be transmitted and adapted to the domestic cat, thus raising the issue of potential cervid-to- feline transmission in nature.
Monday, June 17, 2013
Early detection of chronic wasting disease prions in urine of pre-symptomatic deer by real-time quaking-induced conversion assay
Thursday, April 12, 2012
Health professions and risk of sporadic Creutzfeldt–Jakob disease, 1965 to 2010
Eurosurveillance, Volume 17, Issue 15, 12 April 2012
Tuesday, May 28, 2013
Late-in-life surgery associated with Creutzfeldt-Jakob disease: a methodological outline for evidence-based guidance
Sunday, June 9, 2013
TSEAC March 14, 2013: Transmissible Spongiform Encephalopathies Advisory Committee Meeting Webcast
Tuesday, May 21, 2013
CJD, TSE, PRION, BLOOD Abstracts of the 23rd Regional Congress of the International Society of Blood Transfusion, Amsterdam, The Netherlands, June 2-5, 2013
Tuesday, March 5, 2013
Use of Materials Derived From Cattle in Human Food and Cosmetics; Reopening of the Comment Period FDA-2004-N-0188-0051 (TSS SUBMISSION)
FDA believes current regulation protects the public from BSE but reopens comment period due to new studies
Thursday, October 25, 2012
Current limitations about the cleaning of luminal endoscopes and TSE prion risk factors there from
Article in Press
Saturday, January 16, 2010
Evidence For CJD TSE Transmission Via Endoscopes 1-24-3 re-Singeltary to Bramble et al
Evidence For CJD/TSE Transmission Via Endoscopes
From Terry S. Singletary, Sr email@example.com 1-24-3
Tuesday, July 31, 2012
11 patients may have been exposed to fatal disease Creutzfeldt-Jakob Disease CJD Greenville Memorial Hospital
Thursday, August 02, 2012
CJD case in Saint John prompts letter to patients Canada CJD case in Saint John prompts letter to patients
Saturday, February 12, 2011
Another Pathologists dies from CJD, another potential occupational death ?
another happenstance of bad luck, a spontaneous event from nothing, or friendly fire ???
Thursday, July 08, 2010
GLOBAL CLUSTERS OF CREUTZFELDT JAKOB DISEASE - A REVIEW 2010
Sunday, May 10, 2009
Meeting of the Transmissible Spongiform Encephalopathies Committee On June 12, 2009 (Singeltary submission)
Thursday, January 29, 2009
Medical Procedures and Risk for Sporadic Creutzfeldt-Jakob Disease, Japan, 1999-2008 (WARNING TO Neurosurgeons and Ophthalmologists) Volume 15, Number 2-February 2009 Research
Wednesday, August 20, 2008
Tonometer disinfection practice in the United Kingdom: A national survey
Tuesday, August 12, 2008
Biosafety in Microbiological and Biomedical Laboratories Fifth Edition 2007 (occupational exposure to prion diseases)
Monday, December 31, 2007
Risk Assessment of Transmission of Sporadic Creutzfeldt-Jakob Disease in Endodontic Practice in Absence of Adequate Prion Inactivation
Subject: CJD: update for dental staff
Date: November 12, 2006 at 3:25 pm PST
1: Dent Update. 2006 Oct;33(8):454-6, 458-60.
CJD: update for dental staff.
Friday, July 19, 2013
Beaumont Hospital in Dublin assessing patients for CJD
Saturday, September 21, 2013
CJD CONFIRMED in patient at New Hampshire Department of Health and Human Services (DHHS), Catholic Medical Center (CMC), and the Manchester Health Department (MHD)
Thursday, September 26, 2013
Minimise transmission risk of CJD and vCJD in healthcare settings Guidance
Wednesday, June 19, 2013
Spreading of tau pathology in Alzheimer's disease by cell-to-cell transmission
MAD COW TESTING ONLY CATCHES SOME MAD COWS
SPREADING IT ALL AROUND
Saturday, October 19, 2013
***A comparative study of modified confirmatory techniques and additional immuno-based methods for non-conclusive autolytic Bovine spongiform encephalopathy cases
Wednesday, September 25, 2013
Inspections, Compliance, Enforcement, and Criminal Investigations BSE TSE PRION 2013
Wednesday, October 09, 2013
WHY THE UKBSEnvCJD ONLY THEORY IS SO POPULAR IN IT'S FALLACY, £41,078,281 in compensation REVISED
Thursday, October 10, 2013
CJD REPORT 1994 increased risk for consumption of veal and venison and lamb
Monday, October 14, 2013
Researchers estimate one in 2,000 people in the UK carry variant CJD proteins
Friday, August 16, 2013
*** Creutzfeldt-Jakob disease (CJD) biannual update August 2013 U.K. and Contaminated blood products induce a highly atypical prion disease devoid of PrPres in primates
WHAT about the sporadic CJD TSE proteins ?
WE now know that some cases of sporadic CJD are linked to atypical BSE and atypical Scrapie, so why are not MORE concerned about the sporadic CJD, and all it’s sub-types $$$
Sunday, August 11, 2013
Creutzfeldt-Jakob Disease CJD cases rising North America updated report August 2013
Creutzfeldt-Jakob Disease CJD cases rising North America with Canada seeing an extreme increase of 48% between 2008 and 2010
Welsh Government and Food Standards Agency Wales Joint Public Consultation on the Proposed Transmissible Spongiform Encephalopathies (Wales) Regulations 2013 Singeltary Submission WG18417
Sunday, October 13, 2013
CJD TSE Prion Disease Cases in Texas by Year, 2003-2012
Tuesday, September 24, 2013
NORDION (US), INC., AND BIOAXONE BIOSCIENCES, INC., Settles $90M Mad Cow TSE prion Contamination Suit Cethrin(R)
Case 0:12-cv-60739-RNS Document 1 Entered on FLSD Docket 04/26/2012 Page 1 of 15
Monday, October 21, 2013
WTO Mad cow disease (No 193)
Saturday, July 6, 2013
Small Ruminant Nor98 Prions Share Biochemical Features with Human Gerstmann-Sträussler-Scheinker Disease and Variably Protease-Sensitive Prionopathy
Thursday, March 29, 2012
atypical Nor-98 Scrapie has spread from coast to coast in the USA 2012
NIAA Annual Conference April 11-14, 2011San Antonio, Texas
Monday, April 25, 2011
Experimental Oral Transmission of Atypical Scrapie to Sheep
Volume 17, Number 5-May 2011 However, work with transgenic mice has demonstrated the potential susceptibility of pigs, with the disturbing finding that the biochemical properties of the resulting PrPSc have changed on transmission (40).
Monday, December 14, 2009
Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease Are Encoded by Distinct Prion Types
(hmmm, this is getting interesting now...TSS)
Sporadic CJD type 1 and atypical/ Nor98 scrapie are characterized by fine (reticular) deposits,
see also ;
All of the Heidenhain variants were of the methionine/ methionine type 1 molecular subtype.
see full text ;
Monday, December 14, 2009
Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease Are Encoded by Distinct Prion Types
Friday, March 09, 2012
Experimental H-type and L-type bovine spongiform encephalopathy in cattle: observation of two clinical syndromes and diagnostic challenges
Thursday, June 23, 2011
Experimental H-type bovine spongiform encephalopathy characterized by plaques and glial- and stellate-type prion protein deposits
Tuesday, August 22, 2006
BSE ATYPICAL TEXAS AND ALABAMA UPDATE JANUARY 20, 2007
2009 UPDATE ON ALABAMA MAD COW FOUND IN 2006
http://bse-atypical.blogspot.com/2006/08/bse-atypical-texas-and-alabama-update.html I ask Professor Kong ;
Thursday, December 04, 2008 3:37 PM
Subject: RE: re--Chronic Wating Disease (CWD) and Bovine Spongiform Encephalopathies (BSE): Public Health Risk Assessment
''IS the h-BSE more virulent than typical BSE as well, or the same as cBSE, or less virulent than cBSE? just curious.....''
Professor Kong reply ;
''As to the H-BSE, we do not have sufficient data to say one way or another, but we have found that H-BSE can infect humans. I hope we could publish these data once the study is complete. Thanks for your interest.''
Qingzhong Kong, PhD Associate Professor Department of Pathology Case Western Reserve University Cleveland, OH 44106 USA
Thursday, December 04, 2008 2:37 PM
"we have found that H-BSE can infect humans."
personal communication with Professor Kong. ...TSS
BSE-H is also transmissible in our humanized Tg mice.
The possibility of more than two atypical BSE strains will be discussed.
Supported by NINDS NS052319, NIA AG14359, and NIH AI 77774.
please see below from PRION2013 ;
*** This study imply the possibility that the novel BSE prions with high virulence in cattle will be emerged during intraspecies transmission.
AD.56: The emergence of novel BSE prions by serial passages of H-type BSE in bovinized mice
Kentaro Masujin, Naoko Tabeta, Ritsuko Miwa, Kohtaro Miyazawa, Hiroyuki Okada, Shirou Mohri and Takashi Yokoyama
National Institute of Animal Health; Tsukuba, Japan
H-type bovine spongiform encephalopathy (BSE) is an atypical form of BSE, and has been detected in several European countries, and North America. Transmission studies of H-type BSE led to the emergence of the classical BSE (C-BSE) phenotypes during passages in inbred wild type and bovinized PrP-overexpressing transgenic mice. In this study, we conducted serial passages of Canadian H-type BSE isolate in bovinized PrP-overexpressing transgenic mice (TgBoPrP). H-type BSE isolate was transmitted to TgBoPrP with incubation periods of 320 ± 12.2 d at primary passage. The incubation period of 2nd and 3rd passage were constant (~= 220 d), no clear differences were observed in their biological and biochemical properties. However, at the forth passage, 2 different BSE phenotypes were confirmed; one is shorter survival times (109 ± 4 d) and the other is longer survival times. TgBoPrP mice with longer incubation period showed the H-type phenotype of PrPsc profile and pathology. However, those of shorter incubation period were different phenotypes from previously existed BSE prions (C-BSE, L-type BSE, and H-type BSE). *** This study imply the possibility that the novel BSE prions with high virulence in cattle will be emerged during intraspecies transmission.
please see ;
Thursday, August 15, 2013
The emergence of novel BSE prions by serial passages of H-type BSE in bovinized mice
Wednesday, September 25, 2013
Presence of subclinical infection in gene-targeted human prion protein transgenic mice exposed to atypical BSE
*** TESTING MAD COWS ONLY CONFIRMS _SOME_ MAD COWS ***
HOW MANY WERE MISSED, AND CONSUMBED ???
Saturday, October 19, 2013
A comparative study of modified confirmatory techniques and additional immuno-based methods for non-conclusive autolytic Bovine spongiform encephalopathy cases
Friday, October 25, 2013
*** UK FSA TSE BSE Board meeting agenda: 5 November 2013 ***
Aspects of the Cerebellar Neuropathology in Nor98
Gavier-Widén, D1; Benestad, SL2; Ottander, L1; Westergren, E1 1National Veterinary Insitute, Sweden; 2National Veterinary Institute,
Norway Nor98 is a prion disease of old sheep and goats. This atypical form of scrapie was first described in Norway in 1998. Several features of Nor98 were shown to be different from classical scrapie including the distribution of disease associated prion protein (PrPd) accumulation in the brain. The cerebellum is generally the most affected brain area in Nor98. The study here presented aimed at adding information on the neuropathology in the cerebellum of Nor98 naturally affected sheep of various genotypes in Sweden and Norway. A panel of histochemical and immunohistochemical (IHC) stainings such as IHC for PrPd, synaptophysin, glial fibrillary acidic protein, amyloid, and cell markers for phagocytic cells were conducted. The type of histological lesions and tissue reactions were evaluated. The types of PrPd deposition were characterized. The cerebellar cortex was regularly affected, even though there was a variation in the severity of the lesions from case to case. Neuropil vacuolation was more marked in the molecular layer, but affected also the granular cell layer. There was a loss of granule cells. Punctate deposition of PrPd was characteristic. It was morphologically and in distribution identical with that of synaptophysin, suggesting that PrPd accumulates in the synaptic structures. PrPd was also observed in the granule cell layer and in the white matter. The pathology features of Nor98 in the cerebellum of the affected sheep showed similarities with those of sporadic Creutzfeldt-Jakob disease in humans.
***The pathology features of Nor98 in the cerebellum of the affected sheep showed similarities with those of sporadic Creutzfeldt-Jakob disease in humans.
NOR98 SHOWS MOLECULAR FEATURES REMINISCENT OF GSS
R. Nonno1, E. Esposito1, G. Vaccari1, E. Bandino2, M. Conte1, B. Chiappini1, S. Marcon1, M. Di Bari1, S.L. Benestad3, U. Agrimi1 1 Istituto Superiore di Sanità, Department of Food Safety and Veterinary Public Health, Rome, Italy (firstname.lastname@example.org); 2 Istituto Zooprofilattico della Sardegna, Sassari, Italy; 3 National Veterinary Institute, Department of Pathology, Oslo, Norway
Molecular variants of PrPSc are being increasingly investigated in sheep scrapie and are generally referred to as "atypical" scrapie, as opposed to "classical scrapie". Among the atypical group, Nor98 seems to be the best identified. We studied the molecular properties of Italian and Norwegian Nor98 samples by WB analysis of brain homogenates, either untreated, digested with different concentrations of proteinase K, or subjected to enzymatic deglycosylation. The identity of PrP fragments was inferred by means of antibodies spanning the full PrP sequence. We found that undigested brain homogenates contain a Nor98-specific PrP fragment migrating at 11 kDa (PrP11), truncated at both the C-terminus and the N-terminus, and not N-glycosylated. After mild PK digestion, Nor98 displayed full-length PrP (FL-PrP) and N-glycosylated C-terminal fragments (CTF), along with increased levels of PrP11. Proteinase K digestion curves (0,006-6,4 mg/ml) showed that FL-PrP and CTF are mainly digested above 0,01 mg/ml, while PrP11 is not entirely digested even at the highest concentrations, similarly to PrP27-30 associated with classical scrapie. Above 0,2 mg/ml PK, most Nor98 samples showed only PrP11 and a fragment of 17 kDa with the same properties of PrP11, that was tentatively identified as a dimer of PrP11. Detergent solubility studies showed that PrP11 is insoluble in 2% sodium laurylsorcosine and is mainly produced from detergentsoluble, full-length PrPSc. Furthermore, among Italian scrapie isolates, we found that a sample with molecular and pathological properties consistent with Nor98 showed plaque-like deposits of PrPSc in the thalamus when the brain was analysed by PrPSc immunohistochemistry. Taken together, our results show that the distinctive pathological feature of Nor98 is a PrP fragment spanning amino acids ~ 90-155. This fragment is produced by successive N-terminal and C-terminal cleavages from a full-length and largely detergent-soluble PrPSc, is produced in vivo and is extremely resistant to PK digestion.
*** Intriguingly, these conclusions suggest that some pathological features of Nor98 are reminiscent of Gerstmann-Sträussler-Scheinker disease.
A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes
Annick Le Dur*,?, Vincent Béringue*,?, Olivier Andréoletti?, Fabienne Reine*, Thanh Lan Laï*, Thierry Baron§, Bjørn Bratberg¶, Jean-Luc Vilotte?, Pierre Sarradin**, Sylvie L. Benestad¶, and Hubert Laude*,?? +Author Affiliations
*Virologie Immunologie Moléculaires and ?Génétique Biochimique et Cytogénétique, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; ?Unité Mixte de Recherche, Institut National de la Recherche Agronomique-Ecole Nationale Vétérinaire de Toulouse, Interactions Hôte Agent Pathogène, 31066 Toulouse, France; §Agence Française de Sécurité Sanitaire des Aliments, Unité Agents Transmissibles Non Conventionnels, 69364 Lyon, France; **Pathologie Infectieuse et Immunologie, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; and ¶Department of Pathology, National Veterinary Institute, 0033 Oslo, Norway
***Edited by Stanley B. Prusiner, University of California, San Francisco, CA (received for review March 21, 2005)
Abstract Scrapie in small ruminants belongs to transmissible spongiform encephalopathies (TSEs), or prion diseases, a family of fatal neurodegenerative disorders that affect humans and animals and can transmit within and between species by ingestion or inoculation. Conversion of the host-encoded prion protein (PrP), normal cellular PrP (PrPc), into a misfolded form, abnormal PrP (PrPSc), plays a key role in TSE transmission and pathogenesis. The intensified surveillance of scrapie in the European Union, together with the improvement of PrPSc detection techniques, has led to the discovery of a growing number of so-called atypical scrapie cases. These include clinical Nor98 cases first identified in Norwegian sheep on the basis of unusual pathological and PrPSc molecular features and "cases" that produced discordant responses in the rapid tests currently applied to the large-scale random screening of slaughtered or fallen animals. Worryingly, a substantial proportion of such cases involved sheep with PrP genotypes known until now to confer natural resistance to conventional scrapie. Here we report that both Nor98 and discordant cases, including three sheep homozygous for the resistant PrPARR allele (A136R154R171), efficiently transmitted the disease to transgenic mice expressing ovine PrP, and that they shared unique biological and biochemical features upon propagation in mice. *** These observations support the view that a truly infectious TSE agent, unrecognized until recently, infects sheep and goat flocks and may have important implications in terms of scrapie control and public health.
Monday, December 1, 2008
When Atypical Scrapie cross species barriers
Andreoletti O., Herva M. H., Cassard H., Espinosa J. C., Lacroux C., Simon S., Padilla D., Benestad S. L., Lantier F., Schelcher F., Grassi J., Torres, J. M., UMR INRA ENVT 1225, Ecole Nationale Veterinaire de Toulouse.France; ICISA-INlA, Madrid, Spain; CEA, IBiTec-5, DSV, CEA/Saclay, Gif sur Yvette cedex, France; National Veterinary Institute, Postboks 750 Sentrum, 0106 Oslo, Norway, INRA IASP, Centre INRA de Tours, 3738O Nouzilly, France.
Atypical scrapie is a TSE occurring in small ruminants and harbouring peculiar clinical, epidemiological and biochemical properties. Currently this form of disease is identified in a large number of countries. In this study we report the transmission of an atypical scrapie isolate through different species barriers as modeled by transgenic mice (Tg) expressing different species PRP sequence.
The donor isolate was collected in 1995 in a French commercial sheep flock. inoculation into AHQ/AHQ sheep induced a disease which had all neuro-pathological and biochemical characteristics of atypical scrapie. Transmitted into Transgenic mice expressing either ovine or PrPc, the isolate retained all the described characteristics of atypical scrapie.
Surprisingly the TSE agent characteristics were dramatically different v/hen passaged into Tg bovine mice. The recovered TSE agent had biological and biochemical characteristics similar to those of atypical BSE L in the same mouse model. Moreover, whereas no other TSE agent than BSE were shown to transmit into Tg porcine mice, atypical scrapie was able to develop into this model, albeit with low attack rate on first passage.
Furthermore, after adaptation in the porcine mouse model this prion showed similar biological and biochemical characteristics than BSE adapted to this porcine mouse model. Altogether these data indicate.
(i) the unsuspected potential abilities of atypical scrapie to cross species barriers
(ii) the possible capacity of this agent to acquire new characteristics when crossing species barrier
These findings raise some interrogation on the concept of TSE strain and on the origin of the diversity of the TSE agents and could have consequences on field TSE control measures.
Friday, February 11, 2011
Atypical/Nor98 Scrapie Infectivity in Sheep Peripheral Tissues
Emerging Infectious Diseases • www.cdc.gov/eid • Vol. 17, No. 5, May 2011
Experimental Oral Transmission of Atypical Scrapie to Sheep
Marion M. Simmons, S. Jo Moore,1 Timm Konold, Lisa Thurston, Linda A. Terry, Leigh Thorne, Richard Lockey, Chris Vickery, Stephen A.C. Hawkins, Melanie J. Chaplin, and John Spiropoulos
To investigate the possibility of oral transmission of atypical scrapie in sheep and determine the distribution of infectivity in the animals’ peripheral tissues, we challenged neonatal lambs orally with atypical scrapie; they were then killed at 12 or 24 months. Screening test results were negative for disease-specifi c prion protein in all but 2 recipients; they had positive results for examination of brain, but negative for peripheral tissues. Infectivity of brain, distal ileum, and spleen from all animals was assessed in mouse bioassays; positive results were obtained from tissues that had negative results on screening. These fi ndings demonstrate that atypical scrapie can be transmitted orally and indicate that it has the potential for natural transmission and iatrogenic spread through animal feed. Detection of infectivity in tissues negative by current surveillance methods indicates that diagnostic sensitivity is suboptimal for atypical scrapie, and potentially infectious material may be able to pass into the human food chain.
Although we do not have epidemiologic evidence that supports the effi cient spread of disease in the fi eld, these data imply that disease is potentially transmissible under fi eld situations and that spread through animal feed may be possible if the current feed restrictions were to be relaxed. Additionally, almost no data are available on the potential for atypical scrapie to transmit to other food animal species, certainly by the oral route. However, work with transgenic mice has demonstrated the potential susceptibility of pigs, with the disturbing fi nding that the biochemical properties of the resulting PrPSc have changed on transmission (40). The implications of this observation for subsequent transmission and host target range are currently unknown.
How reassuring is this absence of detectable PrPSc from a public health perspective? The bioassays performed in this study are not titrations, so the infectious load of the positive gut tissues cannot be quantifi ed, although infectivity has been shown unequivocally. No experimental data are currently available on the zoonotic potential of atypical scrapie, either through experimental challenge of humanized mice or any meaningful epidemiologic correlation with human forms of TSE. However, the detection of infectivity in the distal ileum of animals as young as 12 months, in which all the tissues tested were negative for PrPSc by the currently available screening and confi rmatory diagnostic tests, indicates that the diagnostic sensitivity of current surveillance methods is suboptimal for detecting atypical scrapie and that potentially infectious material may be able to pass into the human food chain undetected.
Emerging Infectious Diseases • www.cdc.gov/eid • Vol. 17, No. 5, May 2011
Saturday, October 19, 2013
ACA Council Meets to Endorse Several Proposed USAHA Resolutions (CWD TSE PRION DISEASE)
*** The potential impact of prion diseases on human health was greatly magnified by the recognition that interspecies transfer of BSE to humans by beef ingestion resulted in vCJD. While changes in animal feed constituents and slaughter practices appear to have curtailed vCJD, there is concern that CWD of free-ranging deer and elk in the U.S. might also cross the species barrier. Thus, consuming venison could be a source of human prion disease. Whether BSE and CWD represent interspecies scrapie transfer or are newly arisen prion diseases is unknown. Therefore, the possibility of transmission of prion disease through other food animals cannot be ruled out. There is evidence that vCJD can be transmitted through blood transfusion. There is likely a pool of unknown size of asymptomatic individuals infected with vCJD, and there may be asymptomatic individuals infected with the CWD equivalent. These circumstances represent a potential threat to blood, blood products, and plasma supplies.