Wednesday, January 4, 2012

A Bovine Prion Acquires an Epidemic Bovine Spongiform Encephalopathy Strain-Like Phenotype on Interspecies Transmission

Neurobiology of Disease

A Bovine Prion Acquires an Epidemic Bovine Spongiform Encephalopathy Strain-Like Phenotype on Interspecies Transmission

Vincent Béringue1, Olivier Andréoletti2,*, Annick Le Dur1,*, Rachid Essalmani3, Jean-Luc Vilotte3, Caroline Lacroux2, Fabienne Reine1, Laëtitia Herzog1, Anne-Gaëlle Biacabé4, Thierry Baron4, Maria Caramelli5, Cristina Casalone5, and Hubert Laude1

+ Author Affiliations

1Institut National de la Recherche Agronomique (INRA), Unité de Recherche 892, Virologie Immunologie Moléculaires, F-78350 Jouy-en-Josas, France, 2INRA, Unité Mixte de Recherche 1225, Interactions Hôtes-Agents Pathogènes, Ecole Nationale Vétérinaire, F-31000 Toulouse, France, 3INRA, Unité de Recherche 339, Génétique Biochimique et Cytogénétique, F-78350 Jouy-en-Josas, France, 4Agence Française de Sécurité Sanitaire des Aliments, Unité Agents Transmissibles Non Conventionnels, F-69000 Lyon, France, and 5Instituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle, d'Aosta, Torino, Italy Correspondence should be addressed to either Hubert Laude or Vincent Béringue, Institut National de la Recherche Agronomique, Unité de Recherche 892, Virologie Immunologie Moléculaires, F-78350 Jouy-en-Josas, or ↵*O.A. and A.L. contributed equally to this work.


Implementation in Europe of large-scale testing to detect bovine spongiform encephalopathy (BSE)-infected cattle and prevent the transmission of this prion disease to humans has recently led to the discovery of novel types of bovine prions. We characterized atypical isolates called BSE L-type by analyzing their molecular and neuropathological properties during transmission to several mouse lines transgenic for the prion protein (PrP). Unexpectedly, such isolates acquired strain features closely similar to those of BSE-type agents when propagated in mice expressing ovine PrP, although they retained phenotypic traits distinct from BSE in other lines, including bovine PrP mice. These findings further underline the relationship between the crossing of species barrier and prion strain diversification, and, although the origin of the epidemic BSE agent has only been speculative until now, they provide new insight into the nature of the events that could have led to the appearance of this agent.

bovine prion BSE atypical BSE strain evolution degeneration transgenic


Discussion We examined the strain behavior of a class of cattle prion isolates newly identified by their atypical PrPres signature compared with the classical BSE agent (Casalone et al., 2004; Buschmann et al., 2006), designated BSE-L in the present study. During transmission to transgenic mice, the different isolates analyzed shared identical molecular and biological features, supporting the view that a unique infectious agent is actually involved in the cases named L-type BSE and BASE, depending on the authors (see Introduction). The main finding emerging from this study is that the BSE-L agent, although displaying phenotypic traits distinct from those of BSE and BSE-related agents on the other transgenic mouse lines studied, acquired a BSE-like strain phenotype during transmission to mice expressing ovine PrP.

When serially transmitted to mice expressing the same PrP sequence as the natural host (tgBov), BSE-L (four cases) and BSE (three cases) maintained separate, stable phenotypes. Thus, BSE-L isolates showed (1) faster disease transmission than cattle BSE and related agents, as was reported recently for a German case (Buschmann et al., 2006), (2) a distinctive PrPres signature, as in cattle, and (3) distinguishable PrP deposition and vacuolation patterns in the brain. Primary transmission to mouse or human PrP transgenic mice also revealed striking differences between the two agents. Thus, unlike that seen with various sources of BSE or the vCJD agent, BSE-L provoked no overt disease or detectable PrPres accumulation in tga20 mice. Inversely, it induced an early PrPres accumulation in the brain of tgHu mice relative to cattle BSE, with either agent retaining its distinctive PrPres profile. A worrying implication of this latter result is that the BSE-L agent might be transmissible to and possibly more virulent in humans than classical BSE, an issue that deserves to be investigated further.

In contrast, the BSE-L agent appeared to undergo a strain phenotype shift during transmission to tgOv mice, despite an incubation period during primary inoculation ( 400 d) much shorter than with cattle BSE ( 700 d) or BSE-H ( 600 d) (Beringue et al., 2006), suggesting a lower transmission barrier from cattle to tgOv for BSE-L. Surprisingly, this novel strain phenotype appeared very similar to that of cattle BSE and related agents propagated onto the same mice, according to various criteria. First, the survival times observed after stabilization on tgOv differed by 5% at most between BSE-L and BSE-type agents, which is unlikely to be significant. Second, the spatial distribution of PrPres in the brain showed only a few, minor differences, although being clearly distinct from the patterns observed with several classes of transmissible spongiform encephalopathy (TSE) agents characterized on these mice, including the BSE-H agent (Le Dur et al., 2005; Beringue et al., 2006) (our unpublished data). Third, the vacuolation profiles observed from the second passage on, once the spongiform changes became substantial, essentially overlapped. Fourth, the PrPres molecular profiles of BSE-L and BSE agents on tgOv mice were indistinguishable.

The available typing methods, relying on the comparison of neuropathological features or a PrPres signature (Fraser and Dickinson, 1968; Hecker et al., 1992), arguably have inherent limitations and may be considered of higher value in differentiating two strains than in looking for a potential strain identity. Another issue is the number and the diversity of isolates propagated on the recipient host. In this regard, it is worth emphasizing that 136 prion infectious sources from various species, including 100 natural sheep or goat scrapie isolates, have been transmitted successfully to tgOv mice to date (supplemental Table S1, available at as supplemental material). Remarkably, a PrPres profile with unglycosylated species of intermediate molecular size ( 20 kDa) and prominent diglycoforms has been uniquely and consistently observed with cattle BSE or BSE-related agents, until BSE-L isolates were analyzed. All other sources generated unglycosylated species with either higher or lower (e.g., CH1641 scrapie isolate) mobility (Vilotte et al., 2001; Le Dur et al., 2005; Beringue et al., 2006). Therefore, the observed phenotypic convergence between BSE-L and BSE during transmission on tgOv mice appears as an uncommon event, so far involving only these two strains, both of bovine origin.

Our findings may represent a novel, striking example of the evolutionary potential of prion agents during transmission to a foreign host, which can promote strain shift and emergence of unprecedented properties in a yet unpredictable manner (Kimberlin et al., 1987; Scott et al., 1997; Bartz et al., 2000; Wadsworth et al., 2004). It is unclear in the present state of our investigations which type of mechanism, selection or de novo emergence, may account for the apparent conversion of BSE-L toward the classical BSE strain. Preferential selection in these mice of a classical-type BSE agent that would preexist as a minor component in the brain tissue of BSE-L-infected cattle is one possibility. Indeed, recent observations have questioned the strain homogeneity of the agent present in cattle BSE infectious sources. Thus, transmission of BSE isolates to C57BL and SJL mice expressing the same mouse PrP allele was reported to result in a divergent strain phenotype among the two lines (Asante et al., 2002; Lloyd et al., 2004). Also, biochemical analyses revealed a dual PrPres signature in BSE (and vCJD) brain homogenates (Yull et al., 2006), which may suggest, albeit not exclusively, the presence of a secondary, minor strain component. However, favored propagation of a BSE-like component preexisting in BSE-L-infected brain tissues is unlikely to explain our observation because, as mentioned above, the BSE agent produces much prolonged incubation periods compare with BSE-L in tgOv mice. A still missing piece of information is whether the observed convergence truly reflects a permanent strain shift of the BSE-L agent, because both reversible and irreversible changes have been reported to occur during heterologous transmission of a biologically cloned prion strain (Kimberlin et al., 1987; Scott et al., 1997). Experiments are underway to determine whether the “ovinized” BSE-L agent would retain BSE phenotypic traits during reinoculation to tgBov mice, as we found it to be the case for the ovinized BSE agent. It would also be of interest to learn whether BSE-L would behave similarly on mice expressing an ovine PrP allotype other than Val136Arg154Gln171 as in the present study, because even single amino acid differences in the PrP sequence might be crucial in promoting a strain phenotype shift (Bruce, 2003; Wadsworth et al., 2004).

In conclusion, the findings reported in the present study provide new insight into the nature of the events that could have contributed to the emergence of the BSE epidemic. The various theories currently proposed regarding the origin of the BSE agent invoke two kinds of mechanisms (Colchester and Colchester, 2005; Baron and Biacabe, 2006): an intrinsic cause, i.e., a spontaneously diseased cattle attributable for instance to somatic or germ-line mutation of PrP, or an extrinsic cause, i.e., the infection of cattle by a prion from another species, involving a strain change or not. Our observation is consistent with the view that the epidemic BSE agent could have originated from an endogenous, cattle prion. It also points to the theoretical possibility of a multiple causative event, in which a prion sporadically present in cattle may have “mutated” through passage on an intermediary host such as a sheep.

During the review process of this paper, a study performed on conventional mice has been published that reports converging features of BASE-subpassaged mice toward BSE-inoculated mice (Capobianco et al., 2007), thus strengthening the notion that the BSE-L agent tends to acquire epidemic BSE-like properties during transmission to a heterologous host.

full text ;

Saturday, January 29, 2011

Atypical L-Type Bovine Spongiform Encephalopathy (L-BSE) Transmission to Cynomolgus Macaques, a Non-Human Primate

Jpn. J. Infect. Dis., 64 (1), 81-84, 2011

Friday, December 23, 2011

Oral Transmission of L-type Bovine Spongiform Encephalopathy in Primate Model

Volume 18, Number 1—January 2012 Dispatch

Saturday, June 25, 2011

Transmissibility of BSE-L and Cattle-Adapted TME Prion Strain to Cynomolgus Macaque


Sunday, June 26, 2011

Risk Analysis of Low-Dose Prion Exposures in Cynomolgus Macaque

2. The discovery might indicate the existence of a different strain of BSE from that present in the general epidemic or an unusual response by an individual host.

3. If further atypical lesion distribution cases are revealed in this herd then implications of misdiagnosis of 'negative' cases in other herds may not be insignificant.


This minute is re-issued with a wider distribution. The information contained herein should NOT be disseminated further except on the basis of ''NEED TO KNOW''.

R Bradley





Over the next 8-10 weeks, approximately 40% of all the adult mink on the farm died from TME.


The rancher was a ''dead stock'' feeder using mostly (>95%) downer or dead dairy cattle...

Saturday, December 01, 2007
Phenotypic Similarity of Transmissible Mink Encephalopathy in Cattle and L-type Bovine Spongiform Encephalopathy in a Mouse Model
Volume 13, Number 12–December 2007


When L-type BSE was inoculated into ovine transgenic mice and Syrian hamster the resulting molecular fingerprint had changed, either in the first or a subsequent passage, from L-type into C-type BSE. In addition, non-human primates are specifically susceptible for atypical BSE as demonstrated by an approximately 50% shortened incubation time for L-type BSE as compared to C-type. Considering the current scientific information available, it cannot be assumed that these different BSE types pose the same human health risks as C-type BSE or that these risks are mitigated by the same protective measures. This study will contribute to a correct definition of specified risk material (SRM) in atypical BSE. The incumbent of this position will develop new and transfer existing, ultra-sensitive methods for the detection of atypical BSE in tissue of experimentally infected cattle.

Wednesday, July 28, 2010

Atypical prion proteins and IBNC in cattle DEFRA project code SE1796 FOIA Final report

Tuesday, November 02, 2010

BSE - ATYPICAL LESION DISTRIBUTION (RBSE 92-21367) statutory (obex only) diagnostic criteria CVL 1992

Tuesday, July 14, 2009 U.S.

Emergency Bovine Spongiform Encephalopathy Response Plan Summary and BSE Red Book Date: February 14, 2000 at 8:56 am PST WHERE did we go wrong $$$



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.


Thursday, June 23, 2011

Experimental H-type bovine spongiform encephalopathy characterized by plaques and glial- and stellate-type prion protein deposits

LET'S take a closer look at this new prionpathy or prionopathy, and then let's look at the g-h-BSEalabama mad cow. This new prionopathy in humans? the genetic makeup is IDENTICAL to the g-h-BSEalabama mad cow, the only _documented_ mad cow in the world to date like this, ......wait, it get's better. this new prionpathy is killing young and old humans, with LONG DURATION from onset of symptoms to death, and the symptoms are very similar to nvCJD victims, OH, and the plaques are very similar in some cases too, bbbut, it's not related to the g-h-BSEalabama cow, WAIT NOW, it gets even better, the new human prionpathy that they claim is a genetic TSE, has no relation to any gene mutation in that family. daaa, ya think it could be related to that mad cow with the same genetic make-up ??? there were literally tons and tons of banned mad cow protein in Alabama in commerce, and none of it transmitted to cows, and the cows to humans there from ??? r i g h t $$$ ALABAMA MAD COW g-h-BSEalabama In this study, we identified a novel mutation in the bovine prion protein gene (Prnp), called E211K, of a confirmed BSE positive cow from Alabama, United States of America. This mutation is identical to the E200K pathogenic mutation found in humans with a genetic form of CJD. This finding represents the first report of a confirmed case of BSE with a potential pathogenic mutation within the bovine Prnp gene. We hypothesize that the bovine Prnp E211K mutation most likely has caused BSE in "the approximately 10-year-old cow" carrying the E221K mutation.

Saturday, August 14, 2010

BSE Case Associated with Prion Protein Gene Mutation (g-h-BSEalabama) and VPSPr PRIONPATHY (see mad cow feed in COMMERCE IN ALABAMA...TSS)

her healthy calf also carried the mutation (J. A. Richt and S. M. Hall PLoS Pathog. 4, e1000156; 2008).

This raises the possibility that the disease could occasionally be genetic in origin. Indeed, the report of the UK BSE Inquiry in 2000 suggested that the UK epidemic had most likely originated from such a mutation and argued against the scrapierelated assumption. Such rare potential pathogenic PRNP mutations could occur in countries at present considered to be free of BSE, such as Australia and New Zealand. So it is important to maintain strict surveillance for BSE in cattle, with rigorous enforcement of the ruminant feed ban (many countries still feed ruminant proteins to pigs). Removal of specified risk material, such as brain and spinal cord, from cattle at slaughter prevents infected material from entering the human food chain. Routine genetic screening of cattle for PRNP mutations, which is now available, could provide additional data on the risk to the public. Because the point mutation identified in the Alabama animals is identical to that responsible for the commonest type of familial (genetic) CJD in humans, it is possible that the resulting infective prion protein might cross the bovine-human species barrier more easily. Patients with vCJD continue to be identified. The fact that this is happening less often should not lead to relaxation of the controls necessary to prevent future outbreaks. Malcolm A. Ferguson-Smith Cambridge University Department of Veterinary Medicine, Madingley Road, Cambridge CB3 0ES, UK e-mail: Jürgen A. Richt College of Veterinary Medicine, Kansas State University, K224B Mosier Hall, Manhattan, Kansas 66506-5601, USA NATURE|Vol 457|26 February 2009

P.9.21 Molecular characterization of BSE in Canada

Jianmin Yang1, Sandor Dudas2, Catherine Graham2, Markus Czub3, Tim McAllister1, Stefanie Czub1 1Agriculture and Agri-Food Canada Research Centre, Canada; 2National and OIE BSE Reference Laboratory, Canada; 3University of Calgary, Canada

Background: Three BSE types (classical and two atypical) have been identified on the basis of molecular characteristics of the misfolded protein associated with the disease. To date, each of these three types have been detected in Canadian cattle.

Objectives: This study was conducted to further characterize the 16 Canadian BSE cases based on the biochemical properties of there associated PrPres.

Methods: Immuno-reactivity, molecular weight, glycoform profiles and relative proteinase K sensitivity of the PrPres from each of the 16 confirmed Canadian BSE cases was determined using modified Western blot analysis. Results: Fourteen of the 16 Canadian BSE cases were C type, 1 was H type and 1 was L type. The Canadian H and L-type BSE cases exhibited size shifts and changes in glycosylation similar to other atypical BSE cases. PK digestion under mild and stringent conditions revealed a reduced protease resistance of the atypical cases compared to the C-type cases. N terminal- specific antibodies bound to PrPres from H type but not from C or L type. The C-terminal-specific antibodies resulted in a shift in the glycoform profile and detected a fourth band in the Canadian H-type BSE.

Discussion: The C, L and H type BSE cases in Canada exhibit molecular characteristics similar to those described for classical and atypical BSE cases from Europe and Japan. This supports the theory that the importation of BSE contaminated feedstuff is the source of C-type BSE in Canada. *** It also suggests a similar cause or source for atypical BSE in these countries.

Saturday, July 23, 2011


Saturday, November 6, 2010

TAFS1 Position Paper on Position Paper on Relaxation of the Feed Ban in the EU


Archive Number 20101206.4364 Published Date 06-DEC-2010 Subject PRO/AH/EDR>

Prion disease update 2010 (11) PRION DISEASE UPDATE 2010 (11)

October 2009 O.11.3 Infectivity in skeletal muscle of BASE-infected cattle

Silvia Suardi1, Chiara Vimercati1, Fabio Moda1, Ruggerone Margherita1, Ilaria Campagnani1, Guerino Lombardi2, Daniela Gelmetti2, Martin H. Groschup3, Anne Buschmann3, Cristina Casalone4, Maria Caramelli4, Salvatore Monaco5, Gianluigi Zanusso5, Fabrizio Tagliavini1 1Carlo Besta" Neurological Institute,Italy; 2IZS Brescia, Italy; 33FLI Insel Riems, D, Germany; 4CEA-IZS Torino, Italy; 5University of Verona, Italy

Background: BASE is an atypical form of bovine spongiform encephalopathy caused by a prion strain distinct from that of BSE. Upon experimental transmission to cattle, BASE induces a previously unrecognized disease phenotype marked by mental dullness and progressive atrophy of hind limb musculature. Whether affected muscles contain infectivity is unknown. This is a critical issue since the BASE strain is readily transmissible to a variety of hosts including primates, suggesting that humans may be susceptible.

Objectives: To investigate the distribution of infectivity in peripheral tissues of cattle experimentally infected with BASE. Methods: Groups of Tg mice expressing bovine PrP (Tgbov XV, n= 7-15/group) were inoculated both i.c. and i.p. with 10% homogenates of a variety of tissues including brain, spleen, cervical lymph node, kidney and skeletal muscle (m. longissimus dorsi) from cattle intracerebrally infected with BASE. No PrPres was detectable in the peripheral tissues used for inoculation either by immunohistochemistry or Western blot.

Results: Mice inoculated with BASE-brain homogenates showed clinical signs of disease with incubation and survival times of 175±15 and 207±12 days. Five out of seven mice challenged with skeletal muscle developed a similar neurological disorder, with incubation and survival times of 380±11 and 410±12 days. At present (700 days after inoculation) mice challenged with the other peripheral tissues are still healthy. The neuropathological phenotype and PrPres type of the affected mice inoculated either with brain or muscle were indistinguishable and matched those of Tgbov XV mice infected with natural BASE.

Discussion: Our data indicate that the skeletal muscle of cattle experimentally infected with BASE contains significant amount of infectivity, at variance with BSE-affected cattle, raising the issue of intraspecies transmission and the potential risk for humans. Experiments are in progress to assess the presence of infectivity in skeletal muscles of natural BASE.

18.173 page 189

Experimental Challenge of Cattle with H-type and L-type Atypical BSE

A. Buschmann1, U. Ziegler1, M. Keller1, R. Rogers2, B. Hills3, M.H. Groschup1. 1Friedrich-Loeffler-Institut, Greifswald-Insel Riems, Germany, 2Health Canada, Bureau of Microbial Hazards, Health Products & Food Branch, Ottawa, Canada, 3Health Canada, Transmissible Spongiform Encephalopathy Secretariat, Ottawa, Canada

Background: After the detection of two novel BSE forms designated H-type and L-type atypical BSE the question of the pathogenesis and the agent distribution of these two types in cattle was fully open. From initial studies of the brain pathology, it was already known that the anatomical distribution of L-type BSE differs from that of the classical type where the obex region in the brainstem always displays the highest PrPSc concentrations. In contrast in L-type BSE cases, the thalamus and frontal cortex regions showed the highest levels of the pathological prion protein, while the obex region was only weakly involved.

Methods:We performed intracranial inoculations of cattle (five and six per group) using 10%brainstemhomogenates of the two German H- and L-type atypical BSE isolates. The animals were inoculated under narcosis and then kept in a free-ranging stable under appropriate biosafety conditions.At least one animal per group was killed and sectioned in the preclinical stage and the remaining animals were kept until they developed clinical symptoms. The animals were examined for behavioural changes every four weeks throughout the experiment following a protocol that had been established during earlier BSE pathogenesis studies with classical BSE. Results and

Discussion: All animals of both groups developed clinical symptoms and had to be euthanized within 16 months. The clinical picture differed from that of classical BSE, as the earliest signs of illness were loss of body weight and depression. However, the animals later developed hind limb ataxia and hyperesthesia predominantly and the head. Analysis of brain samples from these animals confirmed the BSE infection and the atypical Western blot profile was maintained in all animals. Samples from these animals are now being examined in order to be able to describe the pathogenesis and agent distribution for these novel BSE types.

Conclusions: A pilot study using a commercially avaialble BSE rapid test ELISA revealed an essential restriction of PrPSc to the central nervous system for both atypical BSE forms. A much more detailed analysis for PrPSc and infectivity is still ongoing.

Saturday, November 19, 2011

Novel Prion Protein in BSE-affected Cattle, Switzerland

Wednesday, February 16, 2011




Sunday, April 18, 2010


Monday, April 25, 2011

Experimental Oral Transmission of Atypical Scrapie to Sheep

Volume 17, Number 5-May 2011

Thursday, June 2, 2011

USDA scrapie report for April 2011 NEW ATYPICAL NOR-98 SCRAPIE CASES Pennsylvania AND California

Monday, June 20, 2011 2011

Annual Conference of the National Institute for Animal Agriculture ATYPICAL NOR-98 LIKE SCRAPIE UPDATE USA

Thursday, July 14, 2011

Histopathological Studies of "CH1641-Like" Scrapie Sources Versus Classical Scrapie and BSE Transmitted to Ovine Transgenic Mice (TgOvPrP4)

Wednesday, October 12, 2011

White-tailed deer are susceptible to the agent of sheep scrapie by intracerebral inoculation


Saturday, December 3, 2011

Isolation of Prion with BSE Properties from Farmed Goat Volume 17, Number 12—December 2011

14th ICID International Scientific Exchange Brochure -

Final Abstract Number: ISE.114

Session: International Scientific Exchange

Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009

T. Singeltary

Bacliff, TX, USA


An update on atypical BSE and other TSE in North America. Please remember, the typical U.K. c-BSE, the atypical l-BSE (BASE), and h-BSE have all been documented in North America, along with the typical scrapie's, and atypical Nor-98 Scrapie, and to date, 2 different strains of CWD, and also TME. All these TSE in different species have been rendered and fed to food producing animals for humans and animals in North America (TSE in cats and dogs ?), and that the trading of these TSEs via animals and products via the USA and Canada has been immense over the years, decades.


12 years independent research of available data


I propose that the current diagnostic criteria for human TSEs only enhances and helps the spreading of human TSE from the continued belief of the UKBSEnvCJD only theory in 2009. With all the science to date refuting it, to continue to validate this old myth, will only spread this TSE agent through a multitude of potential routes and sources i.e. consumption, medical i.e., surgical, blood, dental, endoscopy, optical, nutritional supplements, cosmetics etc.


I would like to submit a review of past CJD surveillance in the USA, and the urgent need to make all human TSE in the USA a reportable disease, in every state, of every age group, and to make this mandatory immediately without further delay. The ramifications of not doing so will only allow this agent to spread further in the medical, dental, surgical arena's. Restricting the reporting of CJD and or any human TSE is NOT scientific. Iatrogenic CJD knows NO age group, TSE knows no boundaries. I propose as with Aguzzi, Asante, Collinge, Caughey, Deslys, Dormont, Gibbs, Gajdusek, Ironside, Manuelidis, Marsh, et al and many more, that the world of TSE Transmissible Spongiform Encephalopathy is far from an exact science, but there is enough proven science to date that this myth should be put to rest once and for all, and that we move forward with a new classification for human and animal TSE that would properly identify the infected species, the source species, and then the route.

Wednesday, August 24, 2011

There Is No Safe Dose of Prions

Wednesday, August 24, 2011

All Clinically-Relevant Blood Components Transmit Prion Disease following a Single Blood Transfusion: A Sheep Model of vCJD

EFSA Journal 2011 The European Response to BSE: A Success Story

EFSA and the European Centre for Disease Prevention and Control (ECDC) recently delivered a scientific opinion on any possible epidemiological or molecular association between TSEs in animals and humans (EFSA Panel on Biological Hazards (BIOHAZ) and ECDC, 2011). This opinion confirmed Classical BSE prions as the only TSE agents demonstrated to be zoonotic so far but the possibility that a small proportion of human cases so far classified as "sporadic" CJD are of zoonotic origin could not be excluded. Moreover, transmission experiments to non-human primates suggest that some TSE agents in addition to Classical BSE prions in cattle (namely L-type Atypical BSE, Classical BSE in sheep, transmissible mink encephalopathy (TME) and chronic wasting disease (CWD) agents) might have zoonotic potential.


see follow-up here about North America BSE Mad Cow TSE prion risk factors, and the ever emerging strains of Transmissible Spongiform Encephalopathy in many species here in the USA, including humans ;

Thursday, November 17, 2011

International cattle ID and traceability: Competitive implications for the US

Food Policy Volume 37, Issue 1, February 2012, Pages 31-40

Friday, November 18, 2011

country-of-origin labeling law (COOL) violates U.S. obligations under WTO rules WT/DS384/R WT/DS386/R

Monday, January 2, 2012

EFSA Minutes of the 6th Meeting of the EFSA Scientific Network on BSE-TSE Brussels, 29-30 November 2011

Thursday, August 12, 2010

Seven main threats for the future linked to prions

First threat

The TSE road map defining the evolution of European policy for protection against prion diseases is based on a certain numbers of hypotheses some of which may turn out to be erroneous. In particular, a form of BSE (called atypical Bovine Spongiform Encephalopathy), recently identified by systematic testing in aged cattle without clinical signs, may be the origin of classical BSE and thus potentially constitute a reservoir, which may be impossible to eradicate if a sporadic origin is confirmed.

***Also, a link is suspected between atypical BSE and some apparently sporadic cases of Creutzfeldt-Jakob disease in humans. These atypical BSE cases constitute an unforeseen first threat that could sharply modify the European approach to prion diseases.

Second threat


2011 Monday, September 26, 2011

L-BSE BASE prion and atypical sporadic CJD


Saturday, March 5, 2011


Tuesday, November 08, 2011

Can Mortality Data Provide Reliable Indicators for Creutzfeldt-Jakob Disease Surveillance? A Study in France from 2000 to 2008 Vol. 37, No. 3-4, 2011

Original Paper

Conclusions:These findings raise doubt about the possibility of a reliable CJD surveillance only based on mortality data.

Terry S. Singeltary Sr. on the Creutzfeldt-Jakob Disease Public Health Crisis

full text with source references ;


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