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From: TSS ()
Subject: Re: cattletoday.com CENSORS TSS ON BSE AKA MAD COW
Date: March 21, 2006 at 10:33 am PST

In Reply to: Re: cattletoday.com CENSORS TSS ON BSE AKA MAD COW posted by TSS on March 21, 2006 at 10:31 am:


Original Message -----
> From: "Terry S. Singeltary Sr."
> To:
> Sent: Monday, March 06, 2006 5:59 PM
> Subject: Creutzfeldt Jakob disease statistics Monday 6 March 2006
Reference
> number: 2006/0088
>
>
> ##################### Bovine Spongiform Encephalopathy
> #####################
>
>
> Subject: Creutzfeldt Jakob disease statistics Monday 6 March 2006
Reference
> number: 2006/0088
> Date: March 6, 2006 at 3:22 pm PST
>
>
> Monthly Creutzfeldt Jakob disease statistics
> Published:
> Monday 6 March 2006
> Reference number:
> 2006/0088
>
>
> The Department of Health is today issuing the latest information about the
> numbers of known cases of Creutzfeldt Jakob disease. This includes cases
of
> variant Creutzfeldt Jakob disease (vCJD) - the form of the disease thought
> to be linked to BSE. The position is as follows:
>
> Definite and probable CJD cases in the UK:
>
> As at 3 March 2006
>
> Summary of vCJD cases
>
> Deaths
>
> Deaths from definite vCJD (confirmed): 110
>
> Deaths from probable vCJD (without neuropathological confirmation): 44
>
> Deaths from probable vCJD (neuropathological confirmation pending): 0
>
> Number of deaths from definite or probable vCJD (as above): 154
>
> Alive
>
> Number of probable vCJD cases still alive: 6
>
> Total number of definite or probable vCJD (dead and alive): 160
>
> The next table will be published on Monday 3rd April 2006
>
> Referrals: a simple count of all the cases which have been referred to the
> National CJD Surveillance Unit for further investigation in the year in
> question. CJD may be no more than suspected; about half the cases referred
> in the past have turned out not to be CJD. Cases are notified to the Unit
> from a variety of sources including neurologists, neuropathologists,
> neurophysiologists, general physicians, psychiatrists,
electroencephalogram
> (EEG) departments etc. As a safety net, death certificates coded under the
> specific rubrics 046.1 and 331.9 in the 9th ICD Revisions are obtained
from
> the Office for National Statistics in England and Wales, the General
> Register Office for Scotland and the General Register Office for Northern
> Ireland.
>
> Deaths: All columns show the number of deaths that have occurred in
definite
> and probable cases of all types of CJD and GSS in the year shown. The
> figures include both cases referred to the Unit for investigation while
the
> patient was still alive and those where CJD was only discovered post
mortem
> (including a few cases picked up by the Unit from death certificates).
There
> is therefore no read across from these columns to the referrals column.
The
> figures will be subject to retrospective adjustment as diagnoses are
> confirmed.
>
> Definite cases: this refers to the diagnostic status of cases. In definite
> cases the diagnosis will have been pathologically confirmed, in most cases
> by post mortem examination of brain tissue (rarely it may be possible to
> establish a definite diagnosis by brain biopsy while the patient is still
> alive).
>
> Probable vCJD cases: are those who fulfil the ‘probable’ criteria set out
in
> the Annex and are either still alive, or have died and await post mortem
> pathological confirmation. Those still alive will always be shown within
the
> current year's figures.
>
> Sporadic: Classic CJD cases with typical EEG and brain pathology. Sporadic
> cases appear to occur spontaneously with no identifiable cause and account
> for 85% of all cases.
>
> Probable sporadic: Cases with a history of rapidly progressive dementia,
> typical EEG and at least two of the following clinical features;
myoclonus,
> visual or cerebellar signs, pyramidal/extrapyramidalsigns or akinetic
> mutism.
>
> Iatrogenic: where infection with classic CJD has occurred accidentally as
> the result of a medical procedure. All UK cases have resulted from
treatment
> with human derived pituitary growth hormones or from grafts using dura
mater
> (a membrane lining the skull).
>
> Familial: cases occurring in families associated with mutations in the PrP
> gene (10 - 15% of cases).
>
> GSS: Gerstmann-Straussler-Scheinker syndrome - an exceedingly rare
inherited
> autosomal dominant disease, typified by chronic progressive ataxia and
> terminal dementia. The clinical duration is from 2 to 10 years, much
longer
> than for CJD.
>
> vCJD: Variant CJD, the hitherto unrecognised variant of CJD discovered by
> the National CJD Surveillance Unit and reported in The Lancet on 6 April
> 1996. This is characterised clinically by a progressive neuropsychiatric
> disorder leading to ataxia, dementia and myoclonus (or chorea) without the
> typical EEG appearance of CJD. Neuropathology shows marked spongiform
change
> and extensive florid plaques throughout the brain.
>
> Definite vCJD cases still alive: These will be cases where the diagnosis
has
> been pathologically confirmed (by brain biopsy).
>
> Related links
> Download CJD statistics March 2006 (PDF, 12K)
> Notes to editor
> ANNEX
>
> DIAGNOSTIC CRITERIA FOR VARIANT CJD
>
> I A) PROGRESSIVE NEUROPSYCHIATRIC DISORDER
>
> B) DURATION OF ILLNESS > 6 MONTHS
>
> C) ROUTINE INVESTIGATIONS DO NOT SUGGEST AN ALTERNATIVE DIAGNOSIS
>
> D) NO HISTORY OF POTENTIAL IATROGENIC EXPOSURE
>
> II A) EARLY PSYCHIATRIC SYMPTOMS *
>
> B) PERSISTENT PAINFUL SENSORY SYMPTOMS **
>
> C) ATAXIA
>
> D) MYOCLONUS OR CHOREA OR DYSTONIA
>
> E) DEMENTIA
>
> III A) EEG DOES NOT SHOW THE TYPICAL APPEARANCE OF SPORADIC CJD *** (OR NO
> EEG PERFORMED)
>
> B) BILATERAL PULVINAR HIGH SIGNAL ON MRI SCAN
>
> IV A) POSITIVE TONSIL BIOPSY
>
> DEFINITE: IA (PROGRESSIVE NEUROPSYCHIATRIC DISORDER) and NEUROPATHOLOGICAL
> CONFIRMATION OF vCJD ****
>
> PROBABLE: I and 4/5 OF II and III A and III B or I and IV A
>
> * depression, anxiety, apathy, withdrawal, delusions.
>
> ** this includes both frank pain and/ or unpleasant dysaesthesia
>
> *** generalised triphasic periodic complexes at approximately one per
second
>
> ****spongiform change and extensive PrP deposition with florid plaques,
> throughout the cerebrum and cerebellum.
>
>
> Reference number:
> 2006/0088
>
>
>
http://www.dh.gov.uk/PublicationsAndStatistics/PressReleases/PressReleasesNo
> tices/fs/en?CONTENT_ID=4131172&chk=EejSdT
>
>
> ALL CJD * As at 3rd March 2006 (see increase in sCJD)
>
>
>
> http://www.dh.gov.uk/assetRoot/04/13/11/73/04131173.pdf
>
>
>
>
> USA
>
>
> notice steady increase, but also notice in 2005, # 7 the 38 pendings cases
> through Oct. and #8 includes 53 type pending, 1 type unknown.
>
> if you look at 2003 there were 3 type unknown.
>
> wonder if they were the same or different than the unknown in 2005?
>
> considering the soup that has been brewing over here in the USA for years
> via the rendering of BSE and atypical TSE in cattle, CWD, Scrapie, a few
TME
> cases (not too much due to scent gland, but there were a few rendered, but
> all this, and you have one hell of a recipe for a new strains of TSE in
> humans. then who knows what 'friendly fire' cases would look like from
this
> soup via secondary transmission via medical/surgical/dental arena. ...TSS
>
>
> National Prion Disease Pathology Surveillance Center case exams...
>
>
>
> http://www.cjdsurveillance.com/resources-casereport.html
>
>
>
>
>
> HUMAN and ANIMAL TSE Classifications i.e. mad cow
> disease and the UKBSEnvCJD only theory
>
> TSEs have been rampant in the USA for decades in many
> species, and they all have been rendered and fed back
> to animals for human/animal consumption. 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 2005.
> With all the science to date refuting it, to continue
> to validate this myth, will only spread this TSE agent
> through a multitude of potential routes and sources
> i.e. consumption, surgical, blood, medical, cosmetics
> etc. I propose as with Aguzzi, Asante, Collinge,
> Caughey, Deslys, Dormont, Gibbs, Ironside, Manuelidis,
> Marsh, et al and many more, that the world of TSE
> Tranmissible 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. This would further have to be broken down to
> strain of species and then the route of transmission
> would further have to be broken down. Accumulation and
> Transmission are key to the threshold from subclinical
> to clinical disease, and of that, I even believe that
> physical and or blunt trauma may play a role of onset
> of clinical symptoms in some cases, but key to all
> this, is to stop the amplification and transmission of
> this agent, the spreading of, no matter what strain.
> BUT, to continue with this myth that the U.K. strain of
> BSE one strain in cows, and the nv/v CJD, one strain in
> humans, and that all the rest of human TSE is one
> single strain i.e. sporadic CJD (when to date there are
> 6 different phenotypes of sCJD), and that no other
> animal TSE transmits to humans, to continue with this
> masquerade will only continue to spread, expose, and
> kill, who knows how many more in the years and decades
> to come. ONE was enough for me, My Mom, hvCJD, DOD
> 12/14/97 confirmed, which is nothing more than another
> mans name added to CJD, like CJD itself, Jakob and
> Creutzfeldt, or Gerstmann-Straussler-Scheinker
> syndrome, just another CJD or human TSE, named after
> another human. WE are only kidding ourselves with the
> current diagnostic criteria for human and animal TSE,
> especially differentiating between the nvCJD vs the
> sporadic CJD strains and then the GSS strains and also
> the FFI fatal familial insomnia strains or the ones
> that mimics one or the other of those TSE? Tissue
> infectivity and strain typing of the many variants of
> the human and animal TSEs are paramount in all variants
> of all TSE. There must be a proper classification that
> will differentiate between all these human TSE in order
> to do this. With the CDI and other more sensitive
> testing coming about, I only hope that my proposal will
> some day be taken seriously.
>
>
> My name is Terry S. Singeltary Sr. and I am no
> scientist, no doctor and have no PhDs, but have been
> independently researching human and animal TSEs since
> the death of my Mother to the Heidenhain Variant of
> Creutzfeldt Jakob Disease on December 14, 1997
> 'confirmed'. ...TSS
>
>
>
>
> Terry S. Singeltary Sr.
> P.O. Box 42
> Bacliff, Texas USA 77518
>
>
>
> SOURCES
>
>
> Full Text
> Diagnosis and Reporting of Creutzfeldt-Jakob Disease
> Singeltary, Sr et al.
> JAMA.2001; 285: 733-734
>
>
>
>
>
http://jama.ama-assn.org/cgi/content/full/285/6/733?maxtoshow=&HITS=10&hits=
>
10&RESULTFORMAT=&fulltext=dignosing+and+reporting+creutzfeldt+jakob+disease&
> searchid=1048865596978_1528&stored_search=&FIRSTINDEX=0&journalcode=jama
>
>
>
>
> Coexistence of multiple PrPSc types in individuals with
>
> Creutzfeldt-Jakob disease
>
>
> Magdalini Polymenidou, Katharina Stoeck, Markus
> Glatzel, Martin Vey, Anne Bellon, and Adriano Aguzzi
>
>
> Summary
>
>
> Background The molecular typing of sporadic
> Creutzfeldt-Jakob disease (CJD) is based on the size
> and glycoform
>
> ratio of protease-resistant prion protein (PrPSc), and
> on PRNP haplotype. On digestion with proteinase K, type
> 1 and
>
> type 2 PrPSc display unglycosylated core fragments of
> 21 kDa and 19 kDa, resulting from cleavage around amino
>
> acids 82 and 97, respectively.
>
> Methods We generated anti-PrP monoclonal antibodies to
> epitopes immediately preceding the differential proteinase
>
> K cleavage sites. These antibodies, which were
> designated POM2 and POM12, recognise type 1, but not
> type 2, PrPSc.
>
> Findings We studied 114 brain samples from 70 patients
> with sporadic CJD and three patients with variant CJD.
>
> Every patient classified as CJD type 2, and all variant
> CJD patients, showed POM2/POM12 reactivity in the
>
> cerebellum and other PrPSc-rich brain areas, with a
> typical PrPSc type 1 migration pattern.
>
> Interpretation The regular coexistence of multiple
> PrPSc types in patients with CJD casts doubts on the
> validity of
>
> electrophoretic PrPSc mobilities as surrogates for
> prion strains, and questions the rational basis of
> current CJD
>
> classifications.
>
>
> snip...
>
>
> The above results set the existing CJD classifications
>
> into debate and introduce interesting questions about
>
> human CJD types. For example, do human prion types
>
> exist in a dynamic equilibrium in the brains of affected
>
> individuals? Do they coexist in most or even all CJD
>
> cases? Is the biochemically identified PrPSc type simply
>
> the dominant type, and not the only PrPSc species?
>
>
> Published online October 31, 2005
>
>
>
>
> http://neurology.thelancet.com
>
>
>
>
>
> Detection of Type 1 Prion Protein in Variant
>
> Creutzfeldt-Jakob Disease
>
> Helen M. Yull,* Diane L. Ritchie,*
>
> Jan P.M. Langeveld,? Fred G. van Zijderveld,?
>
> Moira E. Bruce,? James W. Ironside,* and
>
> Mark W. Head*
>
> From the National CJD Surveillance Unit,* School of
> Molecular
>
> and Clinical Medicine, University of Edinburgh, Edinburgh,
>
> United Kingdom; Central Institute for Animal Disease
> Control
>
> (CIDC)-Lelystad, ? Lelystad, The Netherlands; Institute
> for Animal
>
> Health, Neuropathogenesis Unit, ? Edinburgh, United Kingdom
>
> Molecular typing of the abnormal form of the prion
>
> protein (PrPSc) has come to be regarded as a powerful
>
> tool in the investigation of the prion diseases. All
> evidence
>
> thus far presented indicates a single PrPSc molecular
>
> type in variant Creutzfeldt-Jakob disease (termed
>
> type 2B), presumably resulting from infection with a
>
> single strain of the agent (bovine spongiform
> encephalopathy).
>
> Here we show for the first time that the PrPSc
>
> that accumulates in the brain in variant Creutzfeldt-
>
> Jakob disease also contains a minority type 1 component.
>
> This minority type 1 PrPSc was found in all 21
>
> cases of variant Creutzfeldt-Jakob disease tested,
> irrespective
>
> of brain region examined, and was also
>
> present in the variant Creutzfeldt-Jakob disease tonsil.
>
> The quantitative balance between PrPSc types was maintained
>
> when variant Creutzfeldt-Jakob disease was
>
> transmitted to wild-type mice and was also found in
>
> bovine spongiform encephalopathy cattle brain, indicating
>
> that the agent rather than the host specifies their
>
> relative representation. These results indicate that PrPSc
>
> molecular typing is based on quantitative rather than
>
> qualitative phenomena and point to a complex relationship
>
> between prion protein biochemistry, disease phenotype
>
> and agent strain. (Am J Pathol 2006, 168:151-157;
>
> DOI: 10.2353/ajpath.2006.050766)
>
>
> snip...
>
>
> Discussion
>
> In the apparent absence of a foreign nucleic acid genome
>
> associated with the agents responsible for transmissible
>
> spongiform encephalopathies or prion diseases,
>
> efforts to provide a molecular definition of agent strain
>
> have focused on biochemical differences in the abnormal,
>
> disease-associated form of the prion protein, termed
>
> PrPSc. Differences in PrPSc conformation and glycosylation
>
> have been proposed to underlie disease phenotype
>
> and form the biochemical basis of agent strain. This
>
> proposal has found support in the observation that the
>
> major phenotypic subtypes of sCJD appear to correlate
>
> with the presence of either type 1 or type 2 PrPSc in
>
> combination with the presence of either methionine or
>
> valine at codon 129 of the prion protein gene.2 Similarly,
>
> the PrPSc type associated with vCJD correlates with the
>
> presence of type 2 PrPSc and is distinct from that found in
>
> sCJD because of a characteristically high occupancy of
>
> both N-linked glycosylation sites (type 2B).6,11 The
>
> means by which such conformational difference is detected
>
> is somewhat indirect; relying on the action of proteases,
>
> primarily proteinase K, to degrade the normal
>
> Figure 6. Type 1 PrPSc is a stable minority component
> of PrPSc from the vCJD
>
> brain. Western blot analysis of PrP in a sample of
> cerebral cortex from a
> case
>
> of vCJD during digestion with proteinase K is shown.
> Time points assayed
>
> are indicated in minutes (T0, 5, 10, 30, 60, 120, 180).
> Duplicate blots were
>
> probed with 3F4, which detects both type 1 and type 2
> PrPSc, and with 12B2,
>
> which detects type 1. The insert shows a shorter
> exposure of the same time
>
> course study from a separate experiment also probed
> with 3F4. Both blots
>
> included samples of cerebral cortex from a case of
> sporadic CJD MM1 (Type
>
> 1) and molecular weight markers (Markers) indicate
> weights in kd.
>
> Figure 7. A minority type 1-like PrPSc is found in vCJD
> tonsil, vCJD
> transmitted
>
> to mice and in BSE. Western blot analysis of PrPSc in a
> concentrated
>
> sample of tonsil from a case of vCJD (Tonsil), in a
> concentrated brain
> sample
>
> of a wild-type mouse (C57BL) infected with vCJD and in
> a sample of cattle
>
> BSE brain (BSE) is shown. Tissue extracts were digested
> with proteinase K.
>
> Duplicate blots were probed with either 3F4 or 6H4,
> both of which detect
>
> type 1 and type 2 PrPSc, and with 12B2, which detects
> type 1. The blots
>
> included samples of cerebral cortex from a case of
> sporadic CJD MM1 (Type
>
> 1) and molecular weight markers (Markers) indicate
> weights in kd.
>
> Type 1 PrPSc in Variant Creutzfeldt-Jakob Disease 155
>
> AJP January 2006, Vol. 168, No. 1
>
> cellular form of PrP and produce a protease-resistant
>
> core fragment of PrPSc that differs in the extent of its
>
> N-terminal truncation according to the original
>
> conformation.
>
> A complication has recently arisen with the finding that
>
> both type 1 and type 2 can co-exist in the brains of
>
> patients with sCJD.2,5-8 More recently this same phenomenon
>
> has been demonstrated in patients with iatrogenically
>
> acquired and familial forms of human prion disease.
>
> 9,10 The existence of this phenomenon is now
>
> beyond doubt but its prevalence and its biological
> significance
>
> remain a matter of debate.
>
> Conventional Western blot analysis using antibodies
>
> that detect type 1 and type 2 PrPSc has severe quantitative
>
> limitations for the co-detection of type 1 and type 2
>
> PrPSc in individual samples, suggesting that the prevalence
>
> of co-occurrence of the two types might be underestimated.
>
> We have sought to circumvent this problem by
>
> using an antibody that is type 1-specific and applied this
>
> to the sole remaining human prion disease where the
>
> phenomenon of mixed PrPSc types has not yet been
>
> shown, namely vCJD.
>
> These results show that even in vCJD where susceptible
>
> individuals have been infected supposedly by a
>
> single strain of agent, both PrPSc types co-exist: a
> situation
>
> reminiscent of that seen when similarly discriminant
>
> antibodies were used to analyze experimental BSE in
>
> sheep.14,17 In sporadic and familial CJD, individual
>
> brains can show a wide range of relative amounts of the
>
> two types in samples from different regions, but where
>
> brains have been thoroughly investigated a predominant
>
> type is usually evident.2,6,10 This differs from this
> report
>
> on vCJD, where type 1 is present in all samples
> investigated
>
> but always as a minor component that never
>
> reaches a level at which it is detectable without a type
>
> 1-specific antibody. It would appear that the relative
> balance
>
> between type 1 and type 2 is controlled within
>
> certain limits in the vCJD brain. A minority type-1-like
>
> band is also detected by 12B2 in vCJD tonsil, in BSE
>
> brain and in the brains of mice experimentally infected
>
> with vCJD, suggesting that this balance of types is agent,
>
> rather than host or tissue, specific. Interestingly the
> "glycoform
>
> signature" of the type 2 PrPSc found in vCJD (type
>
> 2B) is also seen in the type 1 PrPSc components, suggesting
>
> that it could legitimately be termed type 1B.
>
> PrPSc isotype analysis has proven to be extremely
>
> useful in the differential diagnosis of CJD and is
> likely to
>
> continue to have a major role in the investigation of human
>
> prion diseases. However, it is clear, on the basis of
>
> these findings, that molecular typing has quantitative
> limitations
>
> and that any mechanistic explanation of prion
>
> replication and the molecular basis of agent strain
> variation
>
> must accommodate the co-existence of multiple
>
> prion protein conformers. Whether or not the different
>
> conformers we describe here correlate in a simple and
>
> direct way with agent strain remains to be determined. In
>
> principle two interpretations present themselves: either
>
> the two conformers can be produced by a single strain of
>
> agent or vCJD (and, therefore, presumably BSE) results
>
> from a mixture of strains, one of which generally
> predominates.
>
> Evidence for the isolation in mice of more than one
>
> strain from individual isolates of BSE has been presented
>
> previously.18,19
>
> One practical consequence of our findings is that the
>
> correct interpretation of transmission studies will depend
>
> on a full examination of the balance of molecular types
>
> present in the inoculum used to transmit disease, in
> addition
>
> to a thorough analysis of the molecular types that
>
> arise in the recipients. Another consequence relates to
>
> the diagnostic certainty of relying on PrPSc molecular
>
> type alone when considering the possibility of BSE
> infection
>
> or secondary transmission in humans who have a
>
> genotype other than methionine at codon 129 of the
>
> PRNP gene. In this context it is interesting to note
> that this
>
> minority type 1B component resembles the type 5 PrPSc
>
> described previously to characterize vCJD transmission
>
> into certain humanized PRNP129VV transgenic mouse
>
> models.12,20 This apparently abrupt change in molecular
>
> phenotype might represent a selection process imposed
>
> by this particular transgenic mouse model. Irrespective of
>
> whether this proves to be the case, the results shown
>
> here point to further complexities in the relationship
> between
>
> the physico-chemical properties of the prion protein,
>
> human disease phenotype, and prion agent strain.
>
> Acknowledgments
>
>
> snip...
>
>
> Type 1 PrPSc in Variant Creutzfeldt-Jakob Disease 157
>
> AJP January 2006, Vol. 168, No. 1 ...TSS
>
>
>
>
http://ajp.amjpathol.org/cgi/content/abstract/168/1/151maxtoshow=&HITS=10&hi
>
ts=10&RESULTFORMAT=&fulltext=prion&searchid=1136646133963_237&FIRSTINDEX=0&v
> olume=168&issue=1&journalcode=amjpathol
>
>
>
>
> Neuropathology and Applied Neurobiology
>
> (2005),
>
> 31
>
> , 565-579 doi: 10.1111/j.1365-2990.2005.00697.x
>
> © 2005 Blackwell Publishing Ltd
>
> 565
>
> Blackwell Science, LtdOxford, UKNANNeuropathology and
> Applied Neurobiology0305-1846Blackwell Publishing Ltd, 2005
>
> 316565579
>
> Review article
>
> Phenotypic variability in human prion diseases
>
> J. W. Ironside, D. L. Ritchie and M. W. Head
>
> National Creutzfeldt-Jakob Disease Surveillance Unit,
> Division of Pathology, University of Edinburgh,
> Edinburgh, UK
>
> J. W. Ironside, D. L. Ritchie and M. W. Head (2005)
>
> Neuropathology and Applied Neurobiology
>
> 31,
>
> 565-579
>
> Phenotypic variability in human prion diseases
>
> Human prion diseases are rare neurodegenerative disorders
>
> that can occur as sporadic, familial or acquired disorders.
>
> Within each of these categories there is a wide range
>
> of phenotypic variation that is not encountered in other
>
> neurodegenerative disorders. The identification of the
>
> prion protein and its key role in the pathogenesis of this
>
> diverse group of diseases has allowed a fuller
> understanding
>
> of factors that influence disease phenotype. In particular,
>
> the naturally occurring polymorphism at codon 129
>
> in the prion protein gene has a major influence on the
> disease
>
> phenotype in sporadic, familial and acquired prion
>
> diseases, although the underlying mechanisms remain
>
> unclear. Recent technical advances have improved our
>
> ability to study the isoforms of the abnormal prion protein
>
> in the brain and in other tissues. This has lead to the
> concept
>
> of molecular strain typing, in which different isoforms
>
> of the prion protein are proposed to correspond to
>
> individual strains of the transmissible agent, each with
>
> specific biological properties. In sporadic
> Creutzfeldt-Jakob
>
> disease there are at least six major combinations of codon
>
> 129 genotype and prion protein isotype, which appear to
>
> relate to distinctive clinical subgroups of this disease.
>
> However, these relationships are proving to be more complex
>
> than first considered, particularly in cases with more
>
> than a single prion protein isotype in the brain. Further
>
> work is required to clarify these relationships and to
>
> explain the mechanism of neuropathological targeting of
>
> specific brain regions, which accounts for the diversity of
>
> clinical features within human prion diseases.
>
>
> © 2005 Blackwell Publishing Ltd, Neuropathology and
> Applied Neurobiology, 31, 565-579
>
>
> BSE prions propagate as either variant CJD-like or
>
> sporadic CJD-like prion strains in transgenic mice
>
> expressing human prion protein
>
>
> The EMBO Journal Vol. 21 No. 23 pp. 6358±6366, 2002
>
>
> Emmanuel A.Asante, Jacqueline M.Linehan,
>
> Melanie Desbruslais, Susan Joiner,
>
> Ian Gowland, Andrew L.Wood, Julie Welch,
>
> Andrew F.Hill, Sarah E.Lloyd,
>
> Jonathan D.F.Wadsworth and
>
> John Collinge1
>
> MRC Prion Unit and Department of Neurodegenerative Disease,
>
> Institute of Neurology, University College, Queen Square,
>
> London WC1N 3BG, UK
>
> 1Corresponding author
>
> e-mail: j.collinge@prion.ucl.ac.uk
>
>
> Variant Creutzfeldt±Jakob disease (vCJD) has been
>
> recognized to date only in individuals homozygous for
>
> methionine at PRNP codon 129. Here we show that
>
> transgenic mice expressing human PrP methionine
>
> 129, inoculated with either bovine spongiform
>
> encephalopathy (BSE) or variant CJD prions, may
>
> develop the neuropathological and molecular phenotype
>
> of vCJD, consistent with these diseases being
>
> caused by the same prion strain. Surprisingly, however,
>
> BSE transmission to these transgenic mice, in
>
> addition to producing a vCJD-like phenotype, can also
>
> result in a distinct molecular phenotype that is
> indistinguishable
>
> from that of sporadic CJD with PrPSc
>
> type 2. These data suggest that more than one BSEderived
>
> prion strain might infect humans; it is therefore
>
> possible that some patients with a phenotype consistent
>
> with sporadic CJD may have a disease arising
>
> from BSE exposure.
>
>
> snip...
>
>
> These studies further strengthen the evidence that vCJD
>
> is caused by a BSE-like prion strain. Also, remarkably, the
>
> key neuropathological hallmark of vCJD, the presence of
>
> abundant ¯orid PrP plaques, can be recapitulated on BSE
>
> or vCJD transmission to these mice. However, the most
>
> surprising aspect of the studies was the ®nding that an
>
> alternate pattern of disease can be induced in 129MM
>
> Tg35 mice from primary transmission of BSE, with a
>
> molecular phenotype indistinguishable from that of a
> subtype
>
> of sporadic CJD. This ®nding has important potential
>
> implications as it raises the possibility that some humans
>
> infected with BSE prions may develop a clinical disease
>
> indistinguishable from classical CJD associated with type 2
>
> PrPSc. This is, in our experience, the commonest molecular
>
> sub-type of sporadic CJD. In this regard, it is of interest
>
> that the reported incidence of sporadic CJD has risen
> in the
>
> UK since the 1970s (Cousens et al., 1997). This has been
>
> attributed to improved case ascertainment, particularly as
>
> much of the rise is reported from elderly patients and
>
> similar rises in incidence were noted in other European
>
> countries without reported BSE (Will et al., 1998).
>
> However, it is now clear that BSE is present in many
>
> European countries, albeit at a much lower incidence than
>
> was seen in the UK. While improved ascertainment is
>
> likely to be a major factor in this rise, that some of
> these
>
> additional cases may be related to BSE exposure cannot be
>
> ruled out. It is of interest in this regard that a 2-fold
>
> increase in the reported incidence of sporadic CJD in 2001
>
> has recently been reported for Switzerland, a country that
>
> had the highest incidence of cattle BSE in continental
>
> Europe between 1990 and 2002 (Glatzel et al., 2002). No
>
> epidemiological case±control studies with strati®cation of
>
> CJD cases by molecular sub-type have yet been reported.
>
> It will be important to review the incidence of sporadic
>
> CJD associated with PrPSc type 2 and other molecular
> subtypes
>
> in both BSE-affected and unaffected countries in the
>
>
> light of these ®ndings. If human BSE prion infection can
>
> result in propagation of type 2 PrPSc, it would be expected
>
> that such cases would be indistinguishable on clinical,
>
> pathological and molecular criteria from classical CJD. It
>
> may also be expected that such prions would behave
>
> biologically like those isolated from humans with sporadic
>
> CJD with type 2 PrPSc. The transmission properties of
>
> prions associated with type 2 PrPSc from BSE-inoculated
>
> 129MM Tg35 mice are being investigated by serial
>
> passage.
>
> We consider these data inconsistent with contamination
>
> of some of the 129MM Tg35 mice with sporadic CJD
>
> prions. These transmission studies were performed according
>
> to rigorous biosafety protocols for preparation of
>
> inocula and both the inoculation and care of mice, which
>
> are all uniquely identi®ed by sub-cutaneous transponders.
>
> However, crucially, the same BSE inocula have been used
>
> on 129VV Tg152 and 129MM Tg45 mice, which are
>
> highly sensitive to sporadic CJD but in which such
>
> transmissions producing type 2 PrPSc were not observed.
>
> Furthermore, in an independent experiment, separate
>
> inbred lines of wild-type mice, which are highly resistant
>
> to sporadic CJD prions, also propagated two distinctive
>
> PrPSc types on challenge with either BSE or vCJD. No
>
> evidence of spontaneous prion disease or PrPSc has been
>
> seen in groups of uninoculated or mock-inoculated aged
>
> 129MM Tg35 mice.
>
> While distinctive prion isolates have been derived from
>
> BSE passage in mice previously (designated 301C and
>
> 301V), these, in contrast to the data presented here, are
>
> propagated in mice expressing different prion proteins
>
> (Bruce et al., 1994). It is unclear whether our ®ndings
>
> indicate the existence of more than one prion strain in
>
> individual cattle with BSE, with selection and preferential
>
> replication of distinct strains by different hosts, or that
>
> `mutation' of a unitary BSE strain occurs in some types of
>
> host. Western blot analysis of single BSE isolates has not
>
> shown evidence of the presence of a proportion of
>
> monoglycosylated dominant PrPSc type in addition to the
>
> diglycosylated dominant pattern (data not shown).
>
> Extensive strain typing of large numbers of individual
>
> BSE-infected cattle either by biological or molecular
>
> methods has not been reported.
>
> Presumably, the different genetic background of the
>
> different inbred mouse lines is crucial in determining
>
> which prion strain propagates on BSE inoculation. The
>
> transgenic mice described here have a mixed genetic
>
> background with contributions from FVB/N, C57BL/6 and
>
> 129Sv inbred lines; each mouse will therefore have a
>
> different genetic background. This may explain the
>
> differing response of individual 129MM Tg35 mice, and
>
> the difference between 129MM Tg35 and 129MM Tg45
>
> mice, which are, like all transgenic lines, populations
>
> derived from single founders. Indeed, the consistent
>
> distinctive strain propagation in FVB and C57BL/6 versus
>
> SJL and RIIIS lines may allow mapping of genes relevant
>
> to strain selection and propagation, and these studies
> are in
>
> progress.
>
> That different prion strains can be consistently isolated
>
> in different inbred mouse lines challenged with BSE
>
> prions argues that other species exposed to BSE may
>
> develop prion diseases that are not recognizable as being
>
> caused by the BSE strain by either biological or molecular
>
> strain typing methods. As with 129MM Tg35 mice, the
>
> prions replicating in such transmissions may be
> indistinguishable
>
> from naturally occurring prion strains. It
>
> remains of considerable concern whether BSE has transmitted
>
> to, and is being maintained in, European sheep
>
> ¯ocks. Given the diversity of sheep breeds affected by
>
> scrapie, it has to be considered that some sheep might have
>
> become infected with BSE, but propagated a distinctive
>
> strain type indistinguishable from those of natural sheep
>
> scrapie. ...
>
>
> The EMBO Journal Vol. 21 No. 23 pp. 6358±6366, 2002
>
> 6358 ãEuropean Molecular Biology Organization
>
>
>
>
>
> http://embojournal.npgjournals.com/cgi/reprint/21/23/6358
>
>
>
>
>
>
> J Neuropsychiatry Clin Neurosci 17:489-495, November 2005
> doi: 10.1176/appi.neuropsych.17.4.489
> © 2005 American Psychiatric Publishing, Inc.
>
>
> Psychiatric Manifestations of Creutzfeldt-Jakob
> Disease: A 25-Year Analysis
> Christopher A. Wall, M.D., Teresa A. Rummans, M.D.,
> Allen J. Aksamit, M.D.,
> Lois E. Krahn, M.D. and V. Shane Pankratz, Ph.D.
> Received April 20, 2004; revised September 9, 2004;
> accepted September 13,
> 2004. From the Mayo Clinic, Department of Psychiatry
> and Psychology,
> Rochester, Minnesota; Mayo Clinic, Department of
> Neurology, Rochester,
> Minnesota. Address correspondence to Dr. Wall, Mayo
> Clinic, Department of
> Psychiatry and Psychology, Mayo Building-W11A, 200
> First St., SW, Rochester,
> MN 55905; wall.chris@mayo.edu (E-mail).
>
> This study characterizes the type and timing of
> psychiatric manifestations
> in sporadic Creutzfeldt-Jakob disease (sCJD).
> Historically, sCJD has been
> characterized by prominent neurological symptoms, while
> the variant form
> (vCJD) is described as primarily psychiatric in
> presentation and course: A
> retrospective review of 126 sCJD patients evaluated at
> the Mayo Clinic from
> 1976-2001 was conducted. Cases were reviewed for
> symptoms of depression,
> anxiety, psychosis, behavior dyscontrol, sleep
> disturbances, and
> neurological signs during the disease course. Eighty
> percent of the cases
> demonstrated psychiatric symptoms within the first 100
> days of illness, with
> 26% occurring at presentation. The most commonly
> reported symptoms in this
> population included sleep disturbances, psychotic
> symptoms, and depression.
> Psychiatric manifestations are an early and prominent
> feature of sporadic
> CJD, often occurring prior to formal diagnosis.
>
>
> snip...
>
>
> CONCLUSIONS
>
> Historically, psychiatric manifestations have been
> described as a relatively
> infrequent occurrence in the sporadic form of
> creutzfeldt-Jakob disease.
> However, our findings suggest otherwise. In this study,
> a vast majority of
> the cases were noted to have at least one psychiatric
> symptom during the
> course of illness, with nearly one-quarter occurring in
> the prodromal or
> presenting phase of the illness. After comparing the
> frequency of
> neuropsychiatric symptoms in sporadic CJD to studies
> describing the variant
> form of CJD, we found that there are fewer clinical
> differences than
> previously reported.5-7 While the age of patients
> with vCJD presentation
> is significantly younger and the course of illness is
> longer, the type and
> timing of psychiatric manifestations appear similar
> between these two
> diseases. ...snip...
>
>
>
>
> http://neuro.psychiatryonline.org/cgi/content/abstract/17/4/489
>
>
>
>
>
> Personal Communication
>
>
> -------- Original Message --------
>
>
>
> Subject: re-BSE prions propagate as
>
> either variant CJD-like or sporadic CJD Date: Thu, 28
> Nov 2002 10:23:43
>
> -0000 From: "Asante, Emmanuel A" To:
> "'flounder@wt.net'"
>
> Dear Terry,
>
> I have been asked by Professor Collinge to respond to
> your request. I am
>
> a Senior Scientist in the MRC Prion Unit and the lead
> author on the
>
> paper. I have attached a pdf copy of the paper for your
> attention. Thank
>
> you for your interest in the paper.
>
> In respect of your first question, the simple answer
> is, yes. As you
>
> will find in the paper, we have managed to associate
> the alternate
>
> phenotype to type 2 PrPSc, the commonest sporadic CJD.
>
> It is too early to be able to claim any further
> sub-classification in
>
> respect of Heidenhain variant CJD or Vicky Rimmer's
> version. It will
>
> take further studies, which are on-going, to establish
> if there are
>
> sub-types to our initial finding which we are now
> reporting. The main
>
> point of the paper is that, as well as leading to the
> expected new
>
> variant CJD phenotype, BSE transmission to the
> 129-methionine genotype
>
> can lead to an alternate phenotype which is
> indistinguishable from type
>
> 2 PrPSc.
>
>
>
> I hope reading the paper will enlighten you more on the
> subject. If I
>
> can be of any further assistance please to not hesitate
> to ask. Best wishes.
>
>
>
> Emmanuel Asante
>
> <> ____________________________________
>
> Dr. Emmanuel A Asante MRC Prion Unit & Neurogenetics
> Dept. Imperial
>
> College School of Medicine (St. Mary's) Norfolk Place,
> LONDON W2 1PG
>
> Tel: +44 (0)20 7594 3794 Fax: +44 (0)20 7706 3272 email:
>
> e.asante@ic.ac.uk (until 9/12/02)
>
> New e-mail: e.asante@prion.ucl.ac.uk (active from now)
>
> ____________________________________TSS
>
>
>
>
> Human Prion Protein with
>
> Valine 129 Prevents Expression
>
> of Variant CJD Phenotype
>
>
> Jonathan D. F. Wadsworth, Emmanuel A. Asante,
>
> Melanie Desbruslais, Jacqueline M. Linehan, Susan Joiner,
>
> Ian Gowland, Julie Welch, Lisa Stone, Sarah E. Lloyd,
>
> Andrew F. Hill,* Sebastian Brandner, John Collinge.
>
> Variant Creutzfeldt-Jakob disease (vCJD) is a unique
> and highly distinctive
>
> clinicopathological and molecular phenotype of human
> prion disease
>
> associated with infection with bovine spongiform
> encephalopathy (BSE)-like
>
> prions. Here, we found that generation of this
> phenotype in transgenic mice
>
> required expression of human prion protein (PrP) with
> methionine 129.
>
> Expression of human PrP with valine 129 resulted in a
> distinct phenotype and,
>
> remarkably, persistence of a barrier to transmission of
> BSE-derived prions on
>
> subpassage. Polymorphic residue 129 of human PrP
> dictated propagation of
>
> distinct prion strains after BSE prion infection. Thus,
> primary and secondary
>
> human infection with BSE-derived prions may result in
> sporadic CJD-like or
>
> novel phenotypes in addition to vCJD, depending on the
> genotype of the prion
>
> source and the recipient.
>
>
> snip...
>
>
> 3 DECEMBER 2004 VOL 306 SCIENCE
>
>
>
>
> http://www.sciencemag.org
>
>
>
>
> Characterization of two distinct prion strains
>
> derived from bovine spongiform encephalopathy
>
> transmissions to inbred mice
>
>
> Sarah E. Lloyd, Jacqueline M. Linehan, Melanie Desbruslais,
>
> Susan Joiner, Jennifer Buckell, Sebastian Brandner,
>
> Jonathan D. F. Wadsworth and John Collinge
>
> Correspondence
>
> John Collinge
>
> j.collinge@prion.ucl.ac.uk
>
> MRC Prion Unit and Department of Neurodegenerative
> Disease, Institute of Neurology,
>
> University College, London WC1N 3BG, UK
>
> Received 9 December 2003
>
> Accepted 27 April 2004
>
> Distinct prion strains can be distinguished by
> differences in incubation period, neuropathology
>
> and biochemical properties of disease-associated prion
> protein (PrPSc) in inoculated mice.
>
> Reliable comparisons of mouse prion strain properties
> can only be achieved after passage in
>
> genetically identical mice, as host prion protein
> sequence and genetic background are known
>
> to modulate prion disease phenotypes. While multiple
> prion strains have been identified in
>
> sheep scrapie and Creutzfeldt-Jakob disease, bovine
> spongiform encephalopathy (BSE) is
>
> thought to be caused by a single prion strain. Primary
> passage of BSE prions to different lines
>
> of inbred mice resulted in the propagation of two
> distinct PrPSc types, suggesting that two
>
> prion strains may have been isolated. To investigate
> this further, these isolates were
>
> subpassaged in a single line of inbred mice (SJL) and
> it was confirmed that two distinct prion
>
> strains had been identified. MRC1 was characterized by
> a short incubation time (110±3 days),
>
> a mono-glycosylated-dominant PrPSc type and a
> generalized diffuse pattern of PrP-immunoreactive
>
> deposits, while MRC2 displayed a much longer incubation
> time (155±1 days),
>
> a di-glycosylated-dominant PrPSc type and a distinct
> pattern of PrP-immunoreactive deposits
>
> and neuronal loss. These data indicate a crucial
> involvement of the host genome in modulating
>
> prion strain selection and propagation in mice. It is
> possible that multiple disease phenotypes
>
> may also be possible in BSE prion infection in humans
> and other animals.
>
>
> snip...
>
>
> Journal of General Virology (2004), 85, 2471-2478 DOI
> 10.1099/vir.0.79889-0
>
>
>
>
> http://vir.sgmjournals.org/cgi/content/abstract/85/8/2471
>
>
>
>
>
> Medical Sciences
> Identification of a second bovine amyloidotic
> spongiform encephalopathy: Molecular similarities with
> sporadic Creutzfeldt-Jakob disease
>
> Cristina Casalone *, Gianluigi Zanusso , Pierluigi
> Acutis *, Sergio Ferrari , Lorenzo Capucci , Fabrizio
> Tagliavini ¶, Salvatore Monaco ||, and Maria Caramelli *
>
> *Centro di Referenza Nazionale per le Encefalopatie
> Animali, Istituto Zooprofilattico Sperimentale del
> Piemonte, Liguria e Valle d'Aosta, Via Bologna, 148,
> 10195 Turin, Italy; Department of Neurological and
> Visual Science, Section of Clinical Neurology,
> Policlinico G.B. Rossi, Piazzale L.A. Scuro, 10, 37134
> Verona, Italy; Istituto Zooprofilattico Sperimentale
> della Lombardia ed Emilia Romagna, Via Bianchi, 9,
> 25124 Brescia, Italy; and ¶Istituto Nazionale
> Neurologico "Carlo Besta," Via Celoria 11, 20133 Milan,
> Italy
>
>
> Edited by Stanley B. Prusiner, University of
> California, San Francisco, CA, and approved December
> 23, 2003 (received for review September 9, 2003)
>
> Transmissible spongiform encephalopathies (TSEs), or
> prion diseases, are mammalian neurodegenerative
> disorders characterized by a posttranslational
> conversion and brain accumulation of an insoluble,
> protease-resistant isoform (PrPSc) of the host-encoded
> cellular prion protein (PrPC). Human and animal TSE
> agents exist as different phenotypes that can be
> biochemically differentiated on the basis of the
> molecular mass of the protease-resistant PrPSc
> fragments and the degree of glycosylation.
> Epidemiological, molecular, and transmission studies
> strongly suggest that the single strain of agent
> responsible for bovine spongiform encephalopathy (BSE)
> has infected humans, causing variant Creutzfeldt-Jakob
> disease. The unprecedented biological properties of the
> BSE agent, which circumvents the so-called "species
> barrier" between cattle and humans and adapts to
> different mammalian species, has raised considerable
> concern for human health. To date, it is unknown
> whether more than one strain might be responsible for
> cattle TSE or whether the BSE agent undergoes
> phenotypic variation after natural transmission. Here
> we provide evidence of a second cattle TSE. The
> disorder was pathologically characterized by the
> presence of PrP-immunopositive amyloid plaques, as
> opposed to the lack of amyloid deposition in typical
> BSE cases, and by a different pattern of regional
> distribution and topology of brain PrPSc accumulation.
> In addition, Western blot analysis showed a PrPSc type
> with predominance of the low molecular mass glycoform
> and a protease-resistant fragment of lower molecular
> mass than BSE-PrPSc. Strikingly, the molecular
> signature of this previously undescribed bovine PrPSc
> was similar to that encountered in a distinct subtype
> of sporadic Creutzfeldt-Jakob disease.
>
>
>
> --------------------------------------------------------------------------
--
> ----
>
> C.C. and G.Z. contributed equally to this work.
>
> ||To whom correspondence should be addressed.
>
> E-mail: salvatore.monaco@mail.univr.it .
>
> www.pnas.org/cgi/doi/10.1073/pnas.0305777101
>
>
> snip...
>
>
> Phenotypic Similarities Between BASE and sCJD. The
> transmissibility
>
> of CJD brains was initially demonstrated in primates
> (27), and
>
> classification of atypical cases as CJD was based on
> this property
>
> (28). To date, no systematic studies of strain typing
> in sCJD have
>
> been provided, and classification of different subtypes
> is based
>
> on clinical, neuropathological, and molecular features
> (the polymorphic
>
> PRNP codon 129 and the PrPSc glycotype) (8, 9, 15, 19).
>
> The importance of molecular PrPSc characterization in
> assessing
>
> the identity of TSE strains is underscored by several
> studies,
>
> showing that the stability of given disease-specific
> PrPSc types is
>
> maintained upon experimental propagation of sCJD, familial
>
> CJD, and vCJD isolates in transgenic PrP-humanized mice (8,
>
> 29). Similarly, biochemical properties of BSE- and
> vCJDassociated
>
> PrPSc molecules remain stable after passage to mice
>
> expressing bovine PrP (30). Recently, however, it has been
>
> reported that PrP-humanized mice inoculated with BSE
> tissues
>
> may also propagate a distinctive PrPSc type, with a
> ''monoglycosylated-
>
> dominant'' pattern and electrophoretic mobility of the
>
> unglycosylated fragment slower than that of vCJD and
> BSE (31).
>
> Strikingly, this PrPSc type shares its molecular
> properties with the
>
> a PrPSc molecule found in classical sCJD. This
> observation is at
>
> variance with the PrPSc type found in MV2 sCJD cases and in
>
> cattle BASE, showing a monoglycosylated-dominant
> pattern but
>
> faster electrophoretic mobility of the
> protease-resistant fragment
>
> as compared with BSE. In addition to molecular properties
>
> of PrPSc, BASE and MV2 sCJD share a distinctive pattern of
>
> intracerebral PrP deposition, which occurs as
> plaque-like and
>
> amyloid-kuru plaques. Differences were, however,
> observed in
>
> the regional distribution of PrPSc. While inMV2 sCJD
> cases the
>
> largest amounts of PrPSc were detected in the cerebellum,
>
> brainstem, and striatum, in cattle BASE these areas
> were less
>
> involved and the highest levels of PrPSc were recovered
> from the
>
> thalamus and olfactory regions.
>
> In conclusion, decoding the biochemical PrPSc signature of
>
> individual human and animal TSE strains may allow the
> identification
>
> of potential risk factors for human disorders with
>
> unknown etiology, such as sCJD. However, although BASE and
>
> sCJD share several characteristics, caution is dictated
> in assessing
>
> a link between conditions affecting two different mammalian
>
> species, based on convergent biochemical properties of
> diseaseassociated
>
> PrPSc types. Strains of TSE agents may be better
>
> characterized upon passage to transgenic mice. In the
> interim
>
> until this is accomplished, our present findings
> suggest a strict
>
> epidemiological surveillance of cattle TSE and sCJD
> based on
>
> molecular criteria.
>
>
>
>
> http://www.pnas.org/cgi/reprint/0305777101v1
>
>
>
> [Docket No. 03-025IFA] FSIS Prohibition of the Use of Specified Risk
> Materials for Human Food and Requirement for the Disposition of
> Non-Ambulatory Disabled Cattle
>
> 03-025IFA
> 03-025IFA-2
> Terry S. Singeltary
>
>
> Page 1 of 17
>
> From: Terry S. Singeltary Sr. [flounder9@verizon.net]
>
> Sent: Thursday, September 08, 2005 6:17 PM
>
> To: fsis.regulationscomments@fsis.usda.gov
>
> Subject: [Docket No. 03-025IFA] FSIS Prohibition of the Use of Specified
> Risk Materials for Human Food and Requirements
>
> for the Disposition of Non-Ambulatory Disabled Cattle
>
> Greetings FSIS,
>
> I would kindly like to submit the following to [Docket No. 03-025IFA] FSIS
> Prohibition of the Use of Specified Risk Materials for Human Food and
>
> Requirements for the Disposition of Non-Ambulatory Disabled Cattle
>
> THE BSE/TSE SUB CLINICAL Non-Ambulatory Disabled Cattle
>
> Broken bones and such may be the first signs of a sub clinical BSE/TSE
> Non-Ambulatory Disabled Cattle ;
>
> SUB CLINICAL PRION INFECTION
>
> MRC-43-00
>
> Issued: Monday, 28 August 2000
>
> NEW EVIDENCE OF SUB-CLINICAL PRION INFECTION: IMPORTANT RESEARCH
>
> FINDINGS RELEVANT TO CJD AND BSE
>
>
> Terry S. Singeltary Sr.
>
> P.O. Box 42
>
> Bacliff, Texas USA 77518
>
> 9/13/2005
>
>
> snip...
>
>
> http://www.fsis.usda.gov/OPPDE/Comments/03-025IFA/03-025IFA-2.pdf
>
>
>
>
>
> SNIP...END...TSS
>
>
>
>
> #################### https://lists.aegee.org/bse-l.html
> ####################
>




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