FSA MORE BSE MAD COW CONTROL BREACHES JUNE 2013
Last updated on 6 June 2013 .
The FSA has published an update of BSE control breaches
The Food Standards Agency has investigated three incidents in which meat
from cattle over 72 months of age has entered the food chain without the animals
being tested for BSE. .
All of the incidents predate changes to the BSE testing rules that came in
on 1 March 2013. Before then it was mandatory for all cattle slaughtered for
human consumption and aged over 72 months to have a negative BSE test result
before they entered the food supply. Since 1 March this has no longer been a
requirement.
The health risk from eating the meat associated with any of these incidents
is very low as it is extremely unlikely that any of the cattle involved had BSE.
In addition, the parts of the animals most likely to contain BSE, the specified
risk material, had been removed and destroyed.
Under the BSE regulations, as a precaution, the animal slaughtered
immediately before the untested cattle and the two immediately after it are also
stopped from entering the food supply. ..
First incident
In the first incident, a cow aged 72 months and 3 days was slaughtered on
23 July 2012 at J A Jewitt (Meat) Ltd, a combined abattoir and cutting plant in
Co. Durham. The missed test was discovered in September during routine
cross-checks of slaughter and BSE testing data.
The carcass slaughtered immediately before the untested animal was rejected
for other reasons and was disposed of. The untested carcass and two associated
carcasses were dispatched as part of a consignment of 52 sides to a meat
processor. All the sides were then processed and mixed with other consignments
of beef and dispatched to eight different food businesses as both fresh and
frozen product. Much of the product was sold on and consumed. However, 21 cases
of frozen meat associated with the untested animal were traced, detained and
destroyed. ..
Second incident
In the second incident, a cow aged 77 months and 18 days was slaughtered
on 11 September 2012 at Simply Halal (Banham), a combined abattoir and cutting
plant in Norfolk. The missed test was discovered in November during routine
cross-checks of slaughter and BSE testing data.
Meat from the untested carcass and three associated carcasses was sold to
five separate food businesses. The local authorities for the food businesses
that received the meat confirmed that it had all had been sold, in chilled form,
and most likely consumed. ..
Third incident
In the third incident, the animal, aged 72 months and 193 days, was
slaughtered on 29 November 2012, at Anglo Dutch Meats (Charing), a combined
abattoir and cutting plant in Kent. A batch of 70 animals was processed that
day. Of these, 41 required testing. Forty animals were tested and all found to
be negative. The one remaining untested carcass went into the food supply.
The missed test was discovered in January following routine cross-checks of
slaughter and BSE testing data. The untested carcass, together with the three
associated carcasses, was sold to Alec Jarrett Ltd, a combined slaughterhouse
and cutting plant in Bristol as part of a consignment of 108 sides. The meat was
then cut at Alec Jarrett alongside a second consignment from Anglo Dutch Meats.
Some of the cut meat was sold as chilled product to a number of businesses. The
remaining frozen meat was voluntarily detained at the cold store and
subsequently sent for disposal by Alec Jarrett Ltd. The breach was not the
responsibility of Alec Jarrett Ltd. ..
Goats test positive for scrapie
Two goats that tested positive for scrapie entered the food supply
following an error at the testing laboratory.
Scrapie is a disease found in sheep and goats and is similar to BSE.
However, there is no known risk to humans from eating meat from scrapie infected
animals. In addition, the parts of the animal most likely to contain infectivity
were removed before entering the human food chain.
The two animals were slaughtered as part of a batch of 26 goats on 21
January 2013 at Melton Meat Ltd, a slaughterhouse in Leicestershire. This was
part of the Compulsory Scrapie Flocks Scheme, which allows undiagnosed animals
from flocks affected by scrapie to be monitored for the disease at
slaughter.
The slaughterhouse took the required samples from all the goats slaughtered
that day and received the test results from LGC Runcorn, an approved testing
laboratory, on 22 January. On 23 January, the results identified two positive
samples and those carcasses were destroyed. The remaining carcasses were
immediately released for sale. However, on 25 January LGC notified the FSA that
an error had occurred at the laboratory and the wrong carcasses were identified
as positive. The two positive carcasses were sold direct to two private
customers from Melton Meat Ltd’s on site shop. These were cash sales and it was
not possible to identify the customers and retrieve the meat.
LGC has carried out their its internal investigation regarding the reasons
for the error at its laboratory. Melton Meat Ltd was not responsible for the
positive animals entering the food chain.
EURO QUALITY RECALLS ITS LAMBS' BRAINS
Euro Quality Lambs Ltd is recalling its lambs’ brains, which have entered
the food chain without being inspected properly. The Food Standards Agency is
asking all local authority enforcement officers to ensure that the product is
withdrawn from sale and destroyed. The Agency has issued a Food Alert for
Action.
Tuesday, March 5, 2013
FSA notified of BSE control breaches again and again 5 March 2013
Thursday, January 17, 2013
FSA notified of two breaches of BSE testing regulations 14 January 2013
BREACHES OF BSE CONTROLS IN CONSIGNMENTS OF BEEF
Due to an oversight, four breaches of BSE controls in British beef
identified last year were not publicised immediately on the Agency’s website in
the normal manner.
COW AGED OVER 72 MONTHS ENTERS FOOD SUPPLY WITHOUT BEING TESTED FOR BSE
The Agency has been notified that meat has entered the food supply from a
cow aged over 72 months that had not been tested for BSE. A negative BSE test
result is mandatory for cattle slaughtered for human consumption at over 72
months of age.
UNTESTED COW ENTERS THE FOOD SUPPLY
The Agency has been notified that meat from a cow that did not have the
required BSE test has entered the food supply. The 62 month old cow had been
slaughtered on farm for welfare reasons.
Friday, November 30, 2012
PROPOSED DECISION TO STOP BSE TESTING OF HEALTHY CATTLE SLAUGHTERED FOR
HUMAN CONSUMPTION FSA 12/12/04 Open Board – 11 December 2012
Thursday, September 6, 2012
UK Breaches of BSE controls in consignments of beef 2011 communications
missing four reports
Wednesday, December 21, 2011
Potential mad cows that entered food supply without being tested for BSE
2011: UK END OF YEAR REVIEW
Monday, November 14, 2011
Bullock aged over 72 months enters food supply without being tested for
BSE
Monday, June 3, 2013
Unsuccessful oral transmission of scrapie from British sheep to
cattle
Sunday, June 2, 2013
Characterisation of an Unusual TSE in a Goat by Transmission in Knock-in
Transgenic Mice
Thursday, May 30, 2013
World Organization for Animal Health (OIE) has upgraded the United States'
risk classification for mad cow disease to "negligible" from "controlled", and
risk further exposing the globe to the TSE prion mad cow type disease U.S. gets
top mad-cow rating from international group and risk further exposing the globe
to the TSE prion mad cow type disease
Tuesday, May 21, 2013
Canada, USA, Bad feed, mad cows: Why we know three BSE cases had a common
origin and why the SSS policy is in full force $$$
Friday, May 10, 2013
Evidence of effective scrapie transmission via colostrum and milk in
sheep
Tuesday, April 30, 2013
Transmission of classical scrapie via goat milk
Veterinary Record2013;172:455 doi:10.1136/vr.f2613
Monday, May 6, 2013
Warning of mad cow disease threat to blood transfusions
Thursday, April 4, 2013
Variably protease-sensitive prionopathy in the UK: a retrospective review
1991–2008
Brain (2013) 136 (4): 1102-1115. doi: 10.1093/brain/aws366
*** The discovery of previously unrecognized prion diseases in both humans
and animals (i.e., Nor98 in small ruminants) demonstrates that the range of
prion diseases might be wider than expected and raises crucial questions about
the epidemiology and strain properties of these new forms. We are investigating
this latter issue by molecular and biological comparison of VPSPr, GSS and
Nor98.
VARIABLY PROTEASE-SENSITVE PRIONOPATHY IS TRANSMISSIBLE ...price of prion
poker goes up again $
OR-10: Variably protease-sensitive prionopathy is transmissible in bank
voles
Romolo Nonno,1 Michele Di Bari,1 Laura Pirisinu,1 Claudia D’Agostino,1
Stefano Marcon,1 Geraldina Riccardi,1 Gabriele Vaccari,1 Piero Parchi,2 Wenquan
Zou,3 Pierluigi Gambetti,3 Umberto Agrimi1 1Istituto Superiore di Sanità; Rome,
Italy; 2Dipartimento di Scienze Neurologiche, Università di Bologna; Bologna,
Italy; 3Case Western Reserve University; Cleveland, OH USA
Background. Variably protease-sensitive prionopathy (VPSPr) is a recently
described “sporadic”neurodegenerative disease involving prion protein
aggregation, which has clinical similarities with non-Alzheimer dementias, such
as fronto-temporal dementia. Currently, 30 cases of VPSPr have been reported in
Europe and USA, of which 19 cases were homozygous for valine at codon 129 of the
prion protein (VV), 8 were MV and 3 were MM. A distinctive feature of VPSPr is
the electrophoretic pattern of PrPSc after digestion with proteinase K (PK).
After PK-treatment, PrP from VPSPr forms a ladder-like electrophoretic pattern
similar to that described in GSS cases. The clinical and pathological features
of VPSPr raised the question of the correct classification of VPSPr among prion
diseases or other forms of neurodegenerative disorders. Here we report
preliminary data on the transmissibility and pathological features of VPSPr
cases in bank voles.
Materials and Methods. Seven VPSPr cases were inoculated in two genetic
lines of bank voles, carrying either methionine or isoleucine at codon 109 of
the prion protein (named BvM109 and BvI109, respectively). Among the VPSPr cases
selected, 2 were VV at PrP codon 129, 3 were MV and 2 were MM. Clinical
diagnosis in voles was confirmed by brain pathological assessment and western
blot for PK-resistant PrPSc (PrPres) with mAbs SAF32, SAF84, 12B2 and 9A2.
Results. To date, 2 VPSPr cases (1 MV and 1 MM) gave positive transmission
in BvM109. Overall, 3 voles were positive with survival time between 290 and 588
d post inoculation (d.p.i.). All positive voles accumulated PrPres in the form
of the typical PrP27–30, which was indistinguishable to that previously observed
in BvM109 inoculated with sCJDMM1 cases.
In BvI109, 3 VPSPr cases (2 VV and 1 MM) showed positive transmission until
now. Overall, 5 voles were positive with survival time between 281 and 596
d.p.i.. In contrast to what observed in BvM109, all BvI109 showed a GSS-like
PrPSc electrophoretic pattern, characterized by low molecular weight PrPres.
These PrPres fragments were positive with mAb 9A2 and 12B2, while being negative
with SAF32 and SAF84, suggesting that they are cleaved at both the C-terminus
and the N-terminus. Second passages are in progress from these first successful
transmissions.
Conclusions. Preliminary results from transmission studies in bank voles
strongly support the notion that VPSPr is a transmissible prion disease.
Interestingly, VPSPr undergoes divergent evolution in the two genetic lines of
voles, with sCJD-like features in BvM109 and GSS-like properties in BvI109.
The discovery of previously unrecognized prion diseases in both humans and
animals (i.e., Nor98 in small ruminants) demonstrates that the range of prion
diseases might be wider than expected and raises crucial questions about the
epidemiology and strain properties of these new forms. We are investigating this
latter issue by molecular and biological comparison of VPSPr, GSS and Nor98.
Wednesday, March 28, 2012
VARIABLY PROTEASE-SENSITVE PRIONOPATHY IS TRANSMISSIBLE, price of prion
poker goes up again $
Sunday, March 31, 2013
Creutzfeldt Jakob Disease CJD worlds youngest documented victim, 11 years
old, shall we pray
Volume 33, Issue 3, Article first published online: 20 JAN 2013
Special Lecture
Human prion diseases: Molecular, cellular and population biology
Mark W. Head
National CJD Research & Surveillance Unit, Centre for Clinical Brain
Sciences, School of Clinical Sciences,
The University of Edinburgh, Edinburgh, UK
snip...
Potential future zoonoses
Scrapie is endemic in many countries around the world, yet there is no
evidence to suggest that it is pathogenic for humans. The intense investigations
of ruminant TSEs that followed the BSE epidemic have resulted in the
identification of several distinct animal prion diseases, atypical or Nor98
scrapie in sheep and H-type and L-type BSE in cattle.32 Moreover, BSE is
experimentally transmissible to sheep and there are concerns that if BSE were to
have infected the national flock in the UK its presence might be masked by
endemic scrapie, but it might retain its pathogenicity for humans.33,34 Another
concern, particularly for the North American countries, is the spread of chronic
wasting disease in farmed and free-ranging deer and elk.35 There is no known
epidemiological link between any of these animal prion diseases and human
disease, but there are active efforts to try to quantify strain-related species
barriers between the diseases known to be a risk (BSE/ vCJD), those thought not
to represent a risk (scrapie) and those for which data is lacking (atypical
scrapie, H- and L-type BSE and BSE in sheep).36 In assessing whether or not
human prion diseases might have an animal origin, it is important to have a
proper understanding of the clinicopathological heterogeneity of the sporadic
human prion diseases, because it is against this backdrop that any new acquired
forms of the disease will be seen and from which it will need to be
distinguished.
Sporadic CJD and variably protease-sensitive prionopathy
Sporadic CJD is the most commonly occurring human prion disease; it occurs
world-wide and it has long been known to be clinically and pathologically
heterogeneous. The molecular basis for this heterogeneity is currently thought
to reside in a combination of the PRNP codon 129 polymorphic status of the
patient (MM, MV, or VV) and the type (type 1 or type 2) of the
protease-resistant component of PrPSc determined by protease K digestion and
Western blotting (termed PrPres).37,38 The original sCJD sub-classification
system of Parchi et al. that recognized six sCJD subtypes (MM1/MV1, MM2c, MM2t,
MV2,VV2 and VV1) has had to be modified to accommodate the growing number of
cases recognized to contain both type 1 and type 2 PrPres in different or
sometimes the same regions of the brain.39,40 Moreover, intensive surveillance
and investigation of forms of human prion disease that lack PRNP mutation and
known risk factors has identified another sporadic human prion disease, termed
protease-sensitive prionopathy (VPSPr).41While intensively investigated, the
etiology and diversity of the sporadic human prion diseases remain poorly
understood.
snip...
There is also a potentially important practical corollary to the idea of
prion-like spread, which may affect future stem cell therapies for
neurodegenerative diseases. Presumably therapeutic stem cell-derived neurons
would be equally susceptible to “infection” (with misfolded protein aggregates)
as the patient’s own cells, unless steps were taken to prevent this,55 the most
obvious of which would be to prevent expression of the gene product that can be
converted to a pathological prion-like isoform.The suggestion that a prion-like
mechanism of spread of molecular pathology underlies diseases as diverse as
Alzheimer’s disease and Parkinson’s disease has led some researchers to explore
whether the molecular pathology of these diseases is transmissible in an
experimental setting56–58 and to suggest that perhaps some cases of these more
common neurodegenerative illnesses might, like CJD, be acquired.58,59
snip...
MOLECULAR BASIS OF HUMAN PRION DISEASES Molecular strain typing Molecular
strain typing in the form of classifying the mobility and glycoform ratio of
protease-resistant prion protein byWestern blotting is a remarkably useful
adjunct to neuropathological assessment during the post-mortem diagnosis of
human prion diseases (Fig. 1). The glycoform ratio difference between vCJD and
all forms of sCJD is a remarkably robust phenomenon, although the mechanism
underlying it remains obscure. All cases of vCJD examined show type 2B PrPres,
irrespective of brain region assayed and the PrPres type is also found in
lymphoreticular tissues, albeit with presumably tissue-specific minor
modification of mobility and an accentuation of the glycoform ratio. Similarly
sCJD cases are characterized by a narrow range of glycoform ratios, distinct
from vCJD, and the presence of either type 1 or type 2 PrPres (type 1A and type
2A).The PrPres types found in the brain in iCJD and kuru resemble those found in
sCJD (type 1A and type 2A), from which they were presumably derived. Individual
cases of gCJD, GSS and FFI usually have type 1 or type 2 PrPres, but with a
glycoform ratio in which the non-glycosylated component is under-represented
(which we have termed A/B). However, this is not always true and a broad
spectrum of glycoform ratios can be found in genetic prion diseases. Moreover,
some cases of GSS are characterized by an approximately 8 kDa (N- and
C-terminally truncated) PrPres fragment, and some cases of FFI have little
detectable PrPres at all. Despite the diagnostic utility, a simple one-to-one
correspondence between PrPres type and disease phenotype (and by implication to
agent strain) seems unlikely in principle and is complicated by the facts.
First, the choice of analyzing only that fraction of PrPSc which survives a
particular concentration of protease may seem arbitrary. Second, the
interpretation of a molecular population variable, such as glycosylation site
occupancy, as conforming to two or three discrete types, could be seen as
simplistic. Lastly, protease digestion may be considered to be a somewhat blunt
instrument to distinguish secondary and higherorder conformational differences
in PrPSc. Even when genotype (mutations and polymorphisms) is taken into
account, three major types (1, 2, 8 kDa) and three wild-type genotypes (MM,MV
and VV) provide insufficient molecular variation to account for all the
phenotypic variations observed. For example, two forms of sCJD share methione
homozygosity and type 2A PrPres but one form closely resembles FFI (without the
causative mutation) and the other is CJD-like.8 Two more substantial problems,
which may point toward a more subtle and perhaps informative approach to PrPSc
analysis, are discussed below. The co-occurrence of PrPres types 1 and 2 Once
controversial, the idea that PrPSc in individual cases might be composed of
mixtures (or different types co-occurring) is now well recognized and
accepted.40,70 There are probably two phenomena at play here. One is the finding
of different predominant types in individual samples from different parts of the
brain or more rarely approximately equal amounts of type 1A and type 2A in the
same sCJD brain samples.The other is the observation made using antibodies that
specifically recognize type 1 or type 2 PrPres, that a minority type always
accompanies a majority type in sCJD and vCJD, albeit at sub-detectable levels
when conventional antibodies are used.71–75 The former issue is more tractable
and a consensus is beginning to emerge that when multiple brain sampling and
sensitive co-detection is performed on cohorts of sCJD cases, a plateau is
reached at between 30–40% of cases showing co-occurrence. Our own data examining
four regions (temporal cortex, parietal cortex, occipital cortex and thalamus)
instead of frontal cortex only, shows a rise in detected co-occurrence from 3%
to 24% of cases.76 Interestingly, only very rarely did this re-analysis involve
a change in the predominant type found in the brain overall. Parchi et al. have
offered a revised version of their 1999 sporadic CJD classification system that
adds mixed type to the original “pure” types and have shown that the most common
of these 12 sCJD subtypes can be recognized on histological grounds, without
reference to biochemical analysis.39,40,77 It will be interesting to see in the
fullness of time whether this additional complexity reflects a more refined
series of discrete clinicopathological phenotypes or whether it is indicative of
a spectrum of phenotypes depending on the spacio-temporal accumulation of PrPSc
types set against the patient genotype.78
Variably protease-sensitive prionopathy The phenotypic complexity of the
sporadic forms of human prion disease has increased with the report of a new
sporadic human prion disease, termed variably proteasesensitive prionopathy
(VPSPr) that is distinct from previously recognized sub-types of sCJD.41,79
There are no mutations in the open reading frame of PRNP. The patients have no
known risk factors for the disease, but the disease is most common in theVV
genotype, as opposed to sCJD, which is most common in the MM genotype. The
neuropathology involves medium-sized vacuolation and characteristic
microplaques. Durations of illness can be very long and this coupled with
symptoms that do not conform well to CJD have prompted speculation that the
condition may be under-ascertained. The most interesting aspect of the disease
from a biochemical perspective is that although PrPSc is abundantly present in
the brain, PrPres is difficult to detect because of its sensitivity to
proteolysis and because what remains after proteinase K (PK) digestion is both
C- and N-terminally cleaved by PK digestion and seen as a faint 8 kDa band on
Western blots (Fig. 2). The degree of protease resistance is reported to reflect
the codon 129 genotype, withVV being least resistant andMM being most resistant,
despite having the same 8 kDa PrPres fragment predominating.79We have identified
two cases of VPSPr prospectively in the UK80,81 and recently completed a
retrospective review for such cases confirming many of the original observations
by Gambetti and colleagues.41,79 Our work has shown that some areas of the VPSPr
brain contain PrPres similar in appearance to that found in sCJD and conversely
that some cases of sCJD have a very minor PrPres band similar to the 8 kDa
PrPres band that typifies VPSPr.82
snip...
The biochemical basis of the strain phenomenon The results of transmission
of individual samples from single examples of the six different Parchi et al.39
sCJD subtypes (MM1/MV1, VV1, MM2c, MV2, VV2) into humanized transgenic mice
suggest the existence of four distinct sCJD agents, termed M1, M2, V1 and V2,
and a fifth strain corresponding to MM2t or sporadic fatal insomnia.99,100
Interestingly, when we performed formally analogous experiments in the cell-free
PMCA reaction, similar results were obtained: The PrPres type of the seed was
conserved in the PMCA product and the efficiency of conversion appeared to be
determined by compatibility at codon 129 of PRNP.101 The behavior of the seeds
from heterozygous patients were particularly interesting, in that MV1 sCJD seeds
selectively amplified in MM substrate producing type 1 PrPres and MV2 sCJD seeds
selectively amplified in VV substrate producing type 2 PrPres (Fig. 6). These
results reinforce the association between methionine at codon 129 and the
production of type 1 PrPres and valine at codon 129 and the production of type 2
PrPres.
EMERGING RISKS Zoonotic disease BSE is the only animal prion strain with
demonstrated pathogenicity for humans.While it is tempting to suggest that
scrapie might represent the animal reservoir that results in some cases of sCJD,
there is no epidemiological evidence to support this hypothesis. The
pathogenicity of new or newly described animal prion diseases for humans is
unclear and this is particularly true for H- and L-type BSE, atypical scrapie
and for chronic wasting disease (CWD), all of which are probably consumed. Human
susceptibility has been modeled by attempted transmission to (humanized)
transgenic mice with sometimes conflicting results, depending on the transgenic
model used and depending upon whether central or peripheral tissues are
examined.102–106 We have attempted to establish whether PMCA can model the
molecular component of these hypothetical cross-species transmission events.107
The existing data correspond well with the established facts. First, PrPSc in
vCJD brain samples amplifies most efficiently in humanized mouse MM substrate,
less efficiently in MV substrate and not at all in VV. Cattle BSE PrPres is less
efficient than vCJD, but shows the same substrate genotypic preference. Sheep
scrapie fails to amplify detectably in any of the three substrates; however,
sheep BSE PrPres does amplify, again with a codon 129 preference for methionine
(Fig. 7). We are currently extending this approach to encompass atypical
scrapie, H- and L-type BSE and CWD using human rather than humanized PMCA
substrates.
Secondary infection
In the same way that animal reservoirs cannot be completely excluded as
causes of individual sCJD cases, neither can other environmental sources, such
as medical procedures. The known routes of iatrogenic CJD acquisition are
historically growth hormone therapy, dura mater grafting, corneal grafting and
certain highly specialized neurosurgical procedures. The secondary transmission
of vCJD by blood transfusion and experimental evidence showing the efficiency of
the transfusion of viable blood cells between scrapie and BSE-infected and naive
sheep have prompted a reappraisal of transfusion-transmitted CJD, including
consideration being given to the possibility of prion blood testing or
filtration.25,26,108,109
Blood transfusion is the original and most extensively used cellular
therapy, but we may be on the threshold of a new era of cellular therapies based
on embryonic stem cell and induced pluripotent stem cell technologies. Although
the potential for stem cell therapy-mediated prion transmission might be judged
remote, this was also considered to be the case for transfusion transmission of
CJD before 2004.
snip...
SUMMARY AND PERSPECTIVE
While the prospect of a major epidemic of vCJD in the UK and elsewhere
seems to be receding, there remain a series of uncertainties surrounding the
eventual numbers of individuals that will suffer from this devastating
condition.The issues include the effects of genotype on susceptibility and the
possible existence of substantial numbers of asymptomatic infected individuals
that may pose risks of onward transmission. sCJD remains the most frequently
occurring human prion disease and arguably the least well understood. Other
idiopathic forms of human prion disease (such as VPSPr), characterized by
protease-sensitive forms of the prion protein, also exist and their true
prevalence may be hard to ascertain. The possible risks from newly described
animal prion diseases and from emerging cellular therapies are currently poorly
quantified. On a more theoretic level the prion hypothesis has provided a
unifying conceptual framework for TSE research and provided a paradigm to
interrogate the similarities and differences between the diverse
neurodegenerative conditions involving prion-like mechanisms of molecular
pathology.
SNIP...see more here ;
Tuesday, June 4, 2013
INTERPRETING RESULTS OF FSIS VERIFICATION SAMPLING OF DOMESTIC BEEF PRODUCT
DERIVED FROM ADVANCED MEAT RECOVERY SYSTEMS (AMR01/FAMR01) FSIS Notice
38-12
Thursday, February 21, 2013
National Prion Disease Pathology Surveillance Center Cases Examined January
16, 2013
16 YEAR OLD SPORADIC FFI ?
Monday, January 14, 2013
Gambetti et al USA Prion Unit change another highly suspect USA mad cow
victim to another fake name i.e. sporadic FFI at age 16 CJD Foundation goes
along with this BSe
Monday, December 31, 2012
Creutzfeldt Jakob Disease and Human TSE Prion Disease in Washington State,
2006–2011-2012
Tuesday, December 25, 2012
CREUTZFELDT JAKOB TSE PRION DISEASE HUMANS END OF YEAR REVIEW DECEMBER 25,
2012
Tuesday, June 26, 2012
Creutzfeldt Jakob Disease Human TSE report update North America, Canada,
Mexico, and USDA PRION UNIT as of May 18, 2012
type determination pending Creutzfeldt Jakob Disease (tdpCJD), is on the
rise in Canada and the USA
Wednesday, June 13, 2012
MEXICO IS UNDER or MIS DIAGNOSING CREUTZFELDT JAKOB DISEASE AND OTHER PRION
DISEASE SOME WITH POSSIBLE nvCJD
Monday, October 10, 2011
EFSA Journal 2011 The European Response to BSE: A Success Story
snip...
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.
snip...
Tuesday, May 28, 2013
Late-in-life surgery associated with Creutzfeldt-Jakob disease: a
methodological outline for evidence-based guidance
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
snip...
Rural and Regional Affairs and Transport References Committee
The possible impacts and consequences for public health, trade and
agriculture of the Government's decision to relax import restrictions on beef
Final report June 2010
2.65 At its hearing on 14 May 2010, the committee heard evidence from Dr
Alan Fahey who has recently submitted a thesis on the clinical neuropsychiatric,
epidemiological and diagnostic features of Creutzfeldt-Jakob disease.48 Dr Fahey
told the committee of his concerns regarding the lengthy incubation period for
transmissible spongiform encephalopathies, the inadequacy of current tests and
the limited nature of our current understanding of this group of
diseases.49
2.66 Dr Fahey also told the committee that in the last two years a link has
been established between forms of atypical CJD and atypical BSE. Dr Fahey said
that: They now believe that those atypical BSEs overseas are in fact causing
sporadic Creutzfeldt-Jakob disease. They were not sure if it was due to mad
sheep disease or a different form. If you look in the textbooks it looks like
this is just arising by itself. But in my research I have a summary of a
document which states that there has never been any proof that sporadic
Creutzfeldt-Jakob disease has arisen de novo-has arisen of itself. There is no
proof of that. The recent research is that in fact it is due to atypical forms
of mad cow disease which have been found across Europe, have been found in
America and have been found in Asia. These atypical forms of mad cow disease
typically have even longer incubation periods than the classical mad cow
disease.50
Wednesday, March 31, 2010
Atypical BSE in Cattle
To date the OIE/WAHO assumes that the human and animal health standards set
out in the BSE chapter for classical BSE (C-Type) applies to all forms of BSE
which include the H-type and L-type atypical forms. This assumption is
scientifically not completely justified and accumulating evidence suggests that
this may in fact not be the case. Molecular characterization and the spatial
distribution pattern of histopathologic lesions and immunohistochemistry (IHC)
signals are used to identify and characterize atypical BSE. Both the L-type and
H-type atypical cases display significant differences in the conformation and
spatial accumulation of the disease associated prion protein (PrPSc) in brains
of afflicted cattle. Transmission studies in bovine transgenic and wild type
mouse models support that the atypical BSE types might be unique strains because
they have different incubation times and lesion profiles when compared to C-type
BSE.
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.
*** 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.
The chances of a person or domestic animal contracting CWD are “extremely
remote,” Richards said. The possibility can’t be ruled out, however. “One could
look at it like a game of chance,” he explained. “The odds (of infection)
increase over time because of repeated exposure. That’s one of the downsides of
having CWD in free-ranging herds: We’ve got this infectious agent out there that
we can never say never to in terms of (infecting) people and domestic
livestock.”
TSS
