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re-Human Prion Diseases in the United States

Posted by flounder on 01 Jan 2010 at 18:11 GMT

I kindly disagree with your synopsis for the following reasons ;

Incidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with
mixed phenotype and co-occurrence of PrPSc types: an updated classification

Piero Parchi Æ Rosaria Strammiello Æ Silvio Notari Æ Armin Giese Æ Jan P. M.
Langeveld Æ Anna Ladogana Æ Inga Zerr Æ Federico Roncaroli Æ Patrich Cras Æ
Bernardino Ghetti Æ Maurizio Pocchiari Æ Hans Kretzschmar Æ Sabina Capellari

Received: 30 June 2009 / Revised: 16 August 2009 / Accepted: 17 August 2009
/ Published online: 29 August 2009

 The Author(s) 2009. This article is published with open access at


Six subtypes of sporadic Creutzfeldt-Jakob disease with distinctive
clinico-pathological features have been identified largely based on two
types of the abnormal prion protein, PrPSc, and the methionine (M)/valine
(V) polymorphic codon 129 of the prion protein. The existence of affected
subjects showing mixed phenotypic features and concurrent PrPSc types has
been reported but with inconsistencies among studies in both results and
their interpretation. The issue currently complicates diagnosis and
classification of cases and also has implications for disease pathogenesis.
To explore the issue in depth, we carried out a systematic regional study in
a large series of 225 cases. PrPSc types 1 and 2 concurrence was detected in
35% of cases and was higher in MM than in MV or VV subjects. The deposition
of either type 1 or 2, when concurrent, was not random and always
characterized by the coexistence of phenotypic features previously described
in the pure subtypes. PrPSc type 1 accumulation and related pathology
predominated in MM and MV cases, while the type 2 phenotype prevailed in
VVs. Neuropathological examination best identified the mixed types 1 and 2
features in MMs and most MVs, and also uniquely revealed the cooccurrence of
pathological variants sharing PrPSc type 2. In contrast, molecular typing
best detected the concurrent PrPSc types in VV subjects and MV cases with
kuru plaques. The present data provide an updated disease classification and
are of importance for future epidemiologic and transmission studies aimed to
identify etiology and extent of strain variation in sporadic
Creutzfeldt-Jakob disease.



Previous studies have addressed the issue of PrPSc types 1 and 2
co-occurrence in sCJD. Most of them raised the question of the influence of
the number of cases and brain areas analyzed and emphasized the possibility
that the cooccurrence of PrPSc types 1 and 2 is underestimated [13, 18, 20,
30, 37, 40, 43]. On the other hand, the use of a novel, potentially very
sensitive approach, later shown to have pitfalls related to the detection of
unspecific bands generated by partially digested PrPSc fragments [25],
likely led other investigators to overestimate the incidence of the
concurrent PrPSc types [35, 45]. Thus, the overall results on the phenomenon
of the coexistence of molecular and clinico-pathological sCJD subtypes are
at present inconclusive with respect to incidence, effect on disease
phenotype and criteria for disease classification. To contribute to the full
understanding of these issues, in the present study, we combined a
systematic analysis of several brain regions in a large series of case
including all codon 129 genotypes and the rarest phenotypes with the use of
a refined methodology for the detection of the PrPSc type concurrence, which
provides good sensitivity combined with high specificity [25].

After screening about 4,200 samples from a largely consecutive series of 200
cases, we estimated that PrPSc types 1 and 2 coexist in about 35% of sCJD
cases, which is overall consistent with figures from some of the previous
studies [13, 37, 43] in which the number of cases and areas analyzed were
significantly lower. This finding supports the idea that PrPSc types
co-occurrence involves a relevant but limited group of sCJD subjects and
indicates that the incidence of the phenomenon had not been significantly

As far as the characteristics of the CJD population with mixed phenotypes
are concerned, our data show that the PrPSc types 1 and 2 co-occur more
frequently in the MM than in the MV and VV genotypes. More specifically, the
large majority of sCJD cases with concurrent PrPSc types combines features
of the MM and MM 2C sCJD subtypes, in variable proportions. Most commonly,
in such cases, the MM1 phenotype is predominant over the MM 2C phenotype,
but the opposite situation also rarely occurs. The latter results
significantly differ from those obtained in most previous studies. Indeed,
Head et al. [13] mainly found a focal type 1 co-occurrence in MM and MV
subjects with dominant type 2, Schoch et al. [40] detected the mixed protein
types mostly in MV2 cases showing the type 1 only focally in subcortical
areas, and Uro-Coste et al. [43] mainly detected a random co-occurrence of
type 1 in MV or VV cases with dominant type 2. Given that only our study was
based on a large series of consecutive cases, we attribute such
heterogeneity of previous results to case selection biases, although
methodological differences may also have contributed [43].


Taken together, our data indicate that a protocol including the
neuropathologic assessment of the eight brain regions mentioned above and
PrPSc typing in four critical regions such as the temporal, parietal and
occipital neocortices, and medial thalamus is strongly recommended for a
reliable sCJD group classification addressing the issue of mixed phenotypes.
Indeed, by applying this protocol instead of examining all 21 brain regions,
we would have reached the same classification of cases in the present

We also wish to underline the importance of identifying correctly the sCJD
cases with mixed features for transmission purposes. Indeed, the question of
whether the concurrence of PrPSc types 1 and 2 in CJD reflects a coinfection
by two prion strains related to specific undiscovered human genotypes, or
determined by epigenetic factors remains unanswered and will largely rely on
transmission studies in which the careful selection of samples will be of
critical importance. Concerning this critical question, we find intriguing
that the large, confluent vacuoles and the perivacuolar pattern of PrPSc
deposition, we originally linked to sCJD MM 2C are also found in a subgroup
of MV 2K subjects in addition to MM/MV 1?2C. In addition, we have described
here the same morphological features in one case of fatal insomnia (i.e. the
MM2-thalamic subtype or MM 2T) which adds to two previously reported cases
[19, 30, 31]. Thus, it seems that large confluent vacuoles and the
perivacuolar pattern of PrPSc deposition may be found in sCJD associated
with all phenotypes linked to MM or MV at codon 129. Although this
observation remains difficult to interpret at present, it appears relevant
for our future understanding of the molecular basis and the extent of strain
variation in sCJD. In any case, our observation strongly suggests that the
phenomenon of mixed phenotypes in sCJD goes beyond PrPSc types 1 and 2
coexistence and also involves subtypes which shares the same PrPSc type.
This, in turn, further underlines the importance of combining
histopathological assessment and biochemical PrPSc typing for sCJD subtype

The present data also show that the association of two PrP27-30 fragments,
which does not represent a bona-fide type 1 and 2 concurrence, may also be a
feature of some sCJD cases. Thus, the PrP27-30 profile in VV2 cases in the
cerebellum, thalamus and midbrain is sometime characterized by a doublet
comprising a 18.5 kDa in addition to the typical 19 kDa band, while the
western blot profile of PrP27-30 in the MV 2K cases appears almost
invariably characterized by the association of two PrPSc core fragments
including a classic 19 kDa type 2 band and a slower migrating band of about
20 kDa. Although these profiles truly represent concurrent PrPSc fragments,
and the 20 and 18.5 kDa fragments likely reflect specific PK cleavage sites,
the 20 and 18.5 kDa bands are distinguished from the type 1 and type 2
fragments because, at least to date, they were never detected independently
from types 1 and 2, and are not markers of specific clinico-pathological
phenotypes. Knowledge of these regional variations is nonetheless important
to avoid misinterpreting a PrPSc profile as novel when only one brain region
is analyzed [21].

Finally, the results obtained from the analyses of lesion profiles and
clinical features in the subgroups of sCJD cases with mixed features deserve
further comment. By showing that the relative load of each of the two
PrPSc types significantly correlates with disease duration, the relative
frequency of certain symptoms, and the ratio between cortical and cerebellar
pathology, our study provides further strong evidence for the PrPSc type
being a major biological determinant in human prion disease. In conclusion,
the present data add to our knowledge of the prevalence and phenotypic
spectrum of the sCJD variants with mixed molecular and pathological
features, provide an updated molecular classification of the disease
subtypes and will serve for future epidemiologic and transmission studies
aimed at disclosing the etiology and extent of strain variation in sCJD.

Acknowledgments We wish to thank Barbara Polischi and Sabrina Boninsegna for
her technical assistance. We also thank all the physicians who provided
clinical data and helped in the collection of tissues and all family members
who consented to the use of tissue for research. This study was funded in
the frame of the bilateral Italy (ISS)-USA (NIH, Office for Rare Diseases)
agreement on joint research on rare diseases, by the European Commission
(FOOD-CT- 2004-506579), the Italian Ministry of University, Research and
Technology (FIRB-2003-RBNE03FMCJ_006), the Federal Ministry of Health
(ZV2-1369-340): grant PHS P30 AG010133, and the Gino Galletti Foundation.

Keywords Prion protein  Brain mapping  Molecular typing 
Neurodegeneration  Classification

P. Parchi  R. Strammiello  S. Notari  S. Capellari Dipartimento di
Scienze Neurologiche, Universita` di Bologna, Bologna, Italy A. Giese  H.
Kretzschmar Institut fu¨r Neuropathologie, Ludwig-Maximilians-Universita¨t
Mu¨nchen, Munich, Germany J. P. M. Langeveld Central Veterinary Institute of
Wageningen UR, Lelystad, The Netherlands A. Ladogana  M. Pocchiari
Department of Cell Biology and Neurosciences, Istituto Superiore di Sanita`,
Rome, Italy I. Zerr Department of Neurology, National Reference Center for
TSE Surveillance, Georg-August University, Go¨ttingen, Germany F. Roncaroli
Division of Neuroscience and Mental Health, Department of Clinical
Neuroscience, Imperial College, London, UK P. Cras Born-Bunge Institute
(BBI), University of Antwerp (UA), Antwerp, Belgium B. Ghetti Department of
Pathology, Indiana University, Indianapolis, IN, USA P. Parchi (&)
Department of Neurological Sciences, Universtity of Bologna, Via Foscolo 7,
40123 Bologna, Italy e-mail:


MANY, MANY THANKS TO Parchi et al for this study, AND for the public access
to full text. ...TSS

Tuesday, August 11, 2009

Characteristics of Established and Proposed Sporadic Creutzfeldt-Jakob
Disease Variants

Brian S. Appleby, MD; Kristin K. Appleby, MD; Barbara J. Crain, MD, PhD;
Chiadi U. Onyike, MD, MHS; Mitchell T. Wallin, MD, MPH; Peter V. Rabins, MD,

Background: The classic Creutzfeldt-Jakob disease (CJD), Heidenhain, and
Oppenheimer-Brownell variants are sporadic CJD (sCJD) phenotypes frequently
described in the literature, but many cases present with neuropsychiatric
symptoms, suggesting that there may be additional sCJD phenotypes.

Objective: To characterize clinical, diagnostic, and molecular features of 5
sCJD variants.

Design: Retrospective analysis.

Setting: The Johns Hopkins and Veterans Administration health care systems.

Participants: Eighty-eight patients with definite or probable sCJD.

Main Outcome Measures: Differences in age at onset, illness progression,
diagnostic test results, and molecular subtype.

Results: The age at onset differed among sCJD variants (P=.03); the
affective variant had the youngest mean age at onset (59.7 years). Survival
time (P.001) and the time to clinical presentation (P=.003) differed among
groups. Patients with the classic CJD phenotype had the shortest median
survival time from symptom onset (66 days) and those who met criteria for
the affective sCJD variant had the longest (421 days) and presented to
clinicians significantly later (median time from onset to presentation, 92
days; P=.004). Cerebrospinal fluid analyses were positive for 14-3-3 protein
in all of the affective variants, regardless of illness duration. Periodic
sharp-wave complexes were not detected on any of the electroencephalography
tracings in the Oppenheimer-Brownell group; basal ganglia hyperintensity was
not detected on brain magnetic resonance imaging in this group either. All
of the Heidenhain variants were of the methionine/ methionine type 1
molecular subtype.

Conclusions: The classic CJD phenotype and the Heidenhain,
Oppenheimer-Brownell, cognitive, and affective sCJD variants differ by age
at disease onset, survival time, and diagnostic test results.
Characteristics of these 5 phenotypes are provided to facilitate further
clinicopathologic investigation that may lead to more reliable and timely
diagnoses of sCJD.

Arch Neurol. 2009;66(2):208-215



snip...see full text ;


Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in
the United States 2003 revisited 2009

August 10, 2009


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. North America
seems to have the most species with documented Transmissible Spongiform
Encephalopathy's, most all of which have been rendered and fed back to food
producing animals and to humans for years. If you look at the statistics,
sporadic CJD seems to be rising in the USA, and has been, with atypical
cases of the sCJD. I find deeply disturbing in the year of 2009, that Human
Transmissible Spongiform Encephalopathy of any strain and or phenotype, of
all age groups, and I stress all age groups, because human TSE's do not know
age, and they do not know borders. someone 56 years old, that has a human
TSE, that has surgery, can pass this TSE agent on i.e. friendly fire, and or
passing it forward, and there have been documented nvCJD in a 74 year old.
Remembering also that only sporadic CJD has been documented to transmit via
iatrogenic routes, until recently with the 4 cases of blood related
transmission, of which the origin is thought to be nvCJD donors. However
most Iatrogenic CJD cases are nothing more than sporadic CJD, until the
source is proven, then it becomes Iatrogenic. An oxymoron of sorts, because
all sporadic CJD is, are multiple forms, or strains, or phenotypes of
Creutzfeldt Jakob Disease, that the route and source and species have not
been confirmed and or documented. When will the myth of the UKBSEnvCJD only
theory be put to bed for good. This theory in my opinion, and the following
there from, as the GOLD STANDARD, has done nothing more than help spread
this agent around the globe. Politics and money have caused the terrible
consequences to date, and the fact that TSEs are a slow incubating death,
but a death that is 100% certain for those that are exposed and live long
enough to go clinical. once clinical, there is no recourse, to date. But,
while sub-clinical, how many can one exposed human infect? Can humans
exposed to CWD and scrapie strains pass it forward as some form of sporadic
CJD in the surgical and medical arenas? why must we wait decades and decades
to prove this point, only to expose millions needlessly, only for the sake
of the industries involved? would it not have been prudent from the
beginning to just include all TSE's, and rule them out from there with
transmission studies and change policies there from, as opposed to doing
just the opposite? The science of TSE's have been nothing more than a
political circus since the beginning, and for anyone to still believe in
this one strain, one group of bovines, in one geographical location, with
only one age group of human TSE i.e. nvCJD myth, for anyone to believe this
today only enhances to spreading of these human and animal TSE's. This is
exactly why we have been in this quagmire.

The ones that believe that there is a spontaneous CJD in 85%+ of all cases
of human TSE, and the ones that do not believe that cattle can have this
same phenomenon, are two of the same, the industry, and so goes the
political science aspect of this tobacco and or asbestos scenario i.e.
follow the money. I could go into all angles of this man made nightmare, the
real facts and science, for instance, the continuing rendering technology
and slow cooking with low temps that brewed this stew up, and the fact that
This is what supposedly amplified the TSE agent via sheep scrapie, and
spread via feed in the U.K. bovine, and other countries exporting the
tainted product. BUT most everyone ignores this fact, and the fact that the
U.S. has been recycling more TSE, from more species with TSEs, than any
other country documented, but yet, it's all spontaneous, and the rise in
sporadic CJD in the U.S. is a happenstance of bad luck ??? I respectfully
disagree. To top that all off, the infamous BSE-FIREWALL that the USDA
always brags about was nothing more than ink on paper, and I can prove this.
YOU can ignore it, but this is FACT (see source, as late as 2007, in one
recall alone, some 10,000,000 MILLION POUNDS OF BANNED MAD COW FEED WENT OUT
INTO COMMERCE TO BE FED OUT, and most was never recovered. This was banned
blood laced, meat and bone meal. 2006 was a banner year for banned mad cow
protein going into commerce in the U.S. (see source of FDA feed ban warning
letter below). I stress that the August 4, 1997 USA mad cow feed ban and
this infamous BSE firewall, was nothing more than ink on paper, it was never

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 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. 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 sub- clinical to clinical
disease, and key to all this, is to stop the amplification and transmission
of this agent, the spreading of, no matter what strain. In my opinion, to
continue with this myth that the U.K. strain of BSE one strain TSE in cows,
and the nv/v CJD one strain TSE humans, and the one geographical location
source i.e. U.K., and that all the rest of human TSE are just one single
strain i.e. sporadic CJD, a happenstance of bad luck that just happens due
to a twisted protein that just twisted the wrong way, IN 85%+ OF ALL HUMAN
TSEs, when to date there are 6 different phenotypes of sCJD, and growing per
Gambetti et al, and that no other animal TSE transmits to humans ??? With
all due respect to all Scientist that believe this, I beg to differ. 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 i.e. Heidenhain Variant CJD, 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. ...

please see history, and the ever evolving TSE science to date ;

Saturday, June 13, 2009

Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in
the United States 2003 revisited 2009

WHO WILL WATCH THE CHILDREN for CJD over the next 5 decades ?




Monday, October 19, 2009

Atypical BSE, BSE, and other human and animal TSE in North America Update
October 19, 2009


Sunday, September 6, 2009






CVM Annual Report Fiscal Year 2008: October 1, 2007-September 30, 2008


BSE Feed Rule Enforcement: A Decade of Success OFF TO A FAST START




Sent: Tuesday, November 03, 2009 9:07 PM

Subject: [BSE-L] re-FOIA REQUEST ON FEED RECALL PRODUCT contaminated with
prohibited material Recall # V-258-2009 and Recall # V-256-2009 (CONFIRMED


Thursday, November 05, 2009

Incidence and spectrum of sporadic Creutzfeldt-Jakob disease variants with
mixed phenotype and co-occurrence of PrPSc types: an updated classification


An Unusual Case of Variant CJD 18 December 2009

A Case Report published in this week's The Lancet, written by Professor John
Collinge, MRC Prion Unit and National Prion Clinic, UCL Institute of
Neurology and National Hospital for Neurology and Neurosurgery, London,
reports the particular genetic make-up of a 30-year old man who has died of
variant Creutzfeldt-Jakob disease (vCJD). The case report suggests that
there could be other people with the condition who at the moment have no

vCJD is caused by infectious agents called prions, which are made primarily
of protein. The prions which cause vCJD are the same as those that cause
bovine spongiform encephalopathy (BSE, also known as mad cow disease) in
cows. Prion diseases affect the structure of the brain or other neural
tissue, and all are currently untreatable and eventually fatal.
Disease-causing prions are thought to consist of abnormally folded proteins
that spread by encouraging the normal healthy prion protein found on the
surface of most cells in the body to change shape. Prion diseases share
similar disease mechanisms with Alzheimer's, Parkinson's, and other
neurodegenerative brain diseases.

The 30-year-old man was admitted to hospital in June, 2008, with a 13-month
history of personality change, progressive unsteadiness, and intellectual
decline. He complained of severe leg pain and poor memory. Two months later
he developed visual hallucinations. His symptoms worsened over the next
three months. An MRI scan and other tests led to a diagnosis of vCJD. The
man died in January 2009.

The case is unusual because tests showed the man had a particular genotype
at his human prion protein gene (PRNP 129 codon), which can code for the
amino acids valine (V) or methionine (M). People can be VV (homozygous), MM
(again homozygous), or MV (heterozygous). Since 1994, around 200 cases of
vCJD have been identified worldwide, and all those tested have been MM
homozygous. However, the man in this Case Report was heterozygous.

Other prion diseases such as kuru or CJD associated with the use of
pituitary hormones tend to have longer incubation periods in people who are
PRNP heterozygous than those who are MM homozygous. The authors have
recently reported some heterozygous patients with kuru had been incubating
the disease over 50 years. Thus the authors believe there could be other
cases like this one in which people are infected with vCJD but experiencing
a long incubation period.

The authors say:

"The majority of the UK population have potentially been exposed to BSE
prions but the extent of clinically silent infection remains unclear. About
a third of the UK population are PRNP codon 129 methionine homozygous. If
individuals with other genotypes are similarly susceptible to developing
prion disease after BSE prion exposure, but with longer incubation periods,
further cases, which may or may not meet diagnostic criteria for vCJD, would
be expected in these PRNP codon 129 genotypes."

They conclude:

"However, prion disease susceptibility and incubation periods are also
affected by other genetic loci, and the possibility remains that cases of
vCJD to date may have unusual combinations of genotypes at these loci, yet
to be fully characterised."

Press contact: 020 7637 6011

Case Report

Variant CJD in an individual heterozygous for PRNP codon 129

Diego Kaski, Simon Mead, Harpreet Hyare, Sarah Cooper, Ravi Jampana, James
Overell, Richard Knight, John Collinge, Peter Rudge

A 30-year-old man was admitted to hospital in June, 2008, with a 13-month
history of personality change, progressive unsteadiness, and intellectual
decline. He complained of severe leg pain and poor memory. 2 months later he
de-veloped visual hallucinations and falsely believed he had an abdominal
tumour. Symptoms worsened over the next 3 months. In October, 2008, his
score on the mini mental state examination was 26/30. Pursuit eye movements
were saccadic. He had a pout reflex. There was mild ataxia in the arms. His
legs were severely ataxic with brisk tendon reflexes and a left extensor
plantar response. He needed two crutches to walk. Medical history included
tonsillectomy and removal of a cervical lymph node 15 years previously but
he had never had a blood trans-fusion or received implantation of other
human tissues.

EEG showed slow wave activity. CSF protein, glucose, and cell count were
normal but the 14-3-3 protein was positive. MRI of the brain was consistent
with the pulvinar sign (figure A). Although not all neuroradiologists
con-sulted considered the pulvinar sign positive, quantitative assessment
showed symmetrical higher signal in the pul-vinar nuclei than the caudate
nuclei (figure B). Extensive screens for genetic, metabolic, and autoimmune
diseases, including those induced by neoplasia, were negative. PRNP analysis
did not show any known disease-associated mutations; codon 129 was
heterozygous. A clinical diag-nosis of variant Creutzfeldt-Jakob disease
(vCJD) was made on the basis of a characteristic clinical onset and
progres-sion, exclusion of other diagnoses, and MRI findings. Sporadic CJD
was judged unlikely given the combination of young age, clinical features,
MRI findings, and absence of pseudoperiodic complexes on EEG. His carers did
not want further investigation. His condition deteriorated and he died in
January, 2009. Autopsy was not done.

Human prion diseases have acquired, sporadic, and inherited aetiologies,
show wide phenotypic heterogeneity, and are associated with propagation of
infectious prions of many distinct strain types.1 Since 1994, about 200
cases of vCJD, causally related to exposure to bovine spongiform
encephalopathy (BSE) prions, have been identified world-wide. vCJD is
generally seen in young adults, has charac-teristic neuropathological
features and tissue distribution of infectivity, and a distinctive type 4
(London classifica-tion) molecular strain type.1 A polymorphism at codon 129
(encoding methionine or valine) of the human prion protein gene (PRNP),
constitutes a powerful susceptibility factor in all types of prion disease.
In vCJD, every case genotyped to date has been methionine homozygous. In the
other acquired prion diseases, cases have occurred in all genotypes but with
different mean incubation periods,1 which can span decades;2 PRNP codon 129
heterozygotes generally have the longest incubation periods. There is a
report of a recipient of a blood transfusion from a donor incubating vCJD
who died of unrelated causes but showed signs of prion infection at autopsy
and was PRNP codon 129 heterozygous.3 Animal studies have suggested that
different clinicopathological phenotypes could occur in people with various
PRNP codon 129 genotypes.4,5 The majority of the UK population have
potentially been exposed to BSE prions but the extent of clinically silent
infection remains unclear. About a third of the UK population are PRNP codon
129 methionine homozygous. If individuals with other genotypes are similarly
susceptible to developing prion disease after BSE prion exposure, but with
longer incubation periods, further cases, which may or may not meet
diagnostic criteria for vCJD, would be expected in these PRNP codon 129
genotypes. However, prion disease susceptibility and incubation periods are
also affected by other genetic loci, and the possibility remains that cases
of vCJD to date may have unusual combinations of genotypes at these loci,
yet to be fully characterised.

Figure: MRI (A) Increased signal intensity in the pulvinar nucleus
bilaterally (arrow). (B) MR signal intensity in the pulvinar (Pu) is higher
than in the head of the caudate nuclei (C), putamen (P), and right frontal
white matter (FWM).


All authors were involved in discussion about diagnosis, care of the
patient, and preparation of the report. Written consent to publish was

Conflicts of interest

JC is a director and shareholder of D-Gen Ltd, an academic spin-out company
in the field of prion disease diagnosis, decontamination, and therapy. The
other authors declare that they have no conflicts of interest.


1 Collinge J. Prion diseases of humans and animals: their causes and
molecular basis. Annu Rev Neurosci 2001; 24: 519-50.

2 Collinge J, Whitfield J, McKintosh E, et al. Kuru in the 21st century-an
acquired human prion disease with very long incubation periods. Lancet 2006;
367: 2068-74.

3 Peden AH, Head MW, Ritchie DL, Bell JE, Ironside JW. Preclinical vCJD
after blood transfusion in a PRNP codon 129 heterozygous patient. Lancet
2004; 364: 527-29.

4 Asante E, Linehan J, Gowland I, et al. Dissociation of pathological and
molecular phenotype of variant Creutzfeldt-Jakob disease in transgenic human
prion protein 129 heterozygous mice. Proc Natl Acad Sci USA 2006; 103:

5 Wadsworth JD, Asante E, Desbruslais M, et al. Human prion protein with
valine 129 prevents expression of variant CJD phenotype. Science 2004; 306:

Monday, December 14, 2009

Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease
Are Encoded by Distinct Prion Types

Saturday, December 05, 2009

Molecular Model of Prion Transmission to Humans


Tuesday, August 11, 2009

Characteristics of Established and Proposed Sporadic Creutzfeldt-Jakob
Disease Variants


Friday, December 11, 2009 Sporadic Creutzfeldt-Jakob disease causing a
2-years slowly progressive isolated dementia


Sunday, August 09, 2009

CJD...Straight talk with...James Ironside...and...Terry Singeltary... 2009


Thursday, December 17, 2009

An Unusual Case of Variant CJD 18 December 2009


(American Journal of Pathology. 2009;175:2566-2573.) © 2009 American Society
for Investigative Pathology DOI: 10.2353/ajpath.2009.090623

Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease
Are Encoded by Distinct Prion Types

Wiebke M. Wemheuer*, Sylvie L. Benestad, Arne Wrede*, Ulf Schulze-Sturm*,
Wilhelm E. Wemheuer, Uwe Hahmann*, Joanna Gawinecka, Ekkehard Schütz, Inga
Zerr, Bertram Brenig, Bjørn Bratberg, Olivier Andréoletti¶ and Walter J.
Schulz-Schaeffer* From the Prion and Dementia Research Unit,* Department of
Neuropathology, and the National Transmissible Spongiform Encephalopathies
Reference Center, Department of Neurology, University Medical Center
Goettingen, Goettingen, Germany; the Department of Pathology, National
Veterinary Institute, Oslo, Norway; the Institute of Veterinary Medicine,
Faculty for Agricultural Sciences, University of Goettingen, Goettingen,
Germany; and Animal Health,¶ Interactions Hôte Agent Pathogène, Ecole
Nationale Vétérinaire de Toulouse, Toulouse, France

Transmissible spongiform encephalopathies such as scrapie in sheep,
Creutzfeldt-Jakob disease (CJD) in humans, and bovine sporadic
encephalopathy in cattle are characterized by the accumulation of a
misfolded protein: the pathological prion protein. Ever since bovine
sporadic encephalopathy was discovered as the likely cause of the new
variant of CJD in humans, parallels between human and animal transmissible
spongiform encephalopathies must be viewed under the aspect of a disease
risk for humans. In our study we have compared prion characteristics of
different forms of sheep scrapie with those of different phenotypes of
sporadic CJD. The disease characteristics of sporadic CJD depend
considerably on the prion type 1 or 2. Our results show that there are
obvious parallels between sporadic CJD type 1 and the so-called
atypical/Nor98 scrapie. These parelleles apply to the deposition form of
pathological prion protein in the brain, detected by the
paraffin-embedded-tissue blot and the prion aggregate stability with regard
to denaturation by the chaotropic salt guanidine hydrochloride. The same
applies to sporadic CJD type 2 and classical scrapie. The observed parallels
between types of sporadic CJD and types of sheep scrapie demonstrate that
distinct groups of prion disease exist in different species. This should be
taken into consideration when discussing interspecies transmission.


UPDATE ON THIS STUDY, further into this study ;

Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease
Are Encoded by Distinct Prion Types


Different Scrapie Prion Types Show Similarities to Human Prion Types: PrPsc
Deposition Pattern and Western Blot Results

After proteinase K-digestion and Western blot analysis, two different prion
protein types were detectable in clinically distinct human Creutzfeldt-Jakob
diseases.30 Depending on the PrPSc types 1 or 2 (Figure 1C) a difference in
the form of PrPSc aggregates and the neuroanatomical distribution in the
brain could be observed similar to differences identified in sheep scrapie.
In patients with CJD that accumulate PrPSc type 1, reticular/synaptic were
detected in cortical structures (Figure 3F), subcortical nuclei, and the
cerebellar cortex (Figure 4D). By contrast, prion aggregates in patients
accumulating PrPSc type 2 appeared to be complex as they displayed in
particular perivacuolar, intra- and perineuronal, and/or plaque-like forms
(Figures 3C and 5B). These differences concerning the deposition form of
PrPSc aggregates were independent of the methionine/valine polymorphism at
codon 129 of the PRNP. The topographical pattern of PrPSc distribution
between these two prion types differed as follows: type 1 deposits were
typically restricted to gray matter structures, while all type 2 patients
showed deposits in the white matter. In patients with type 1 PrPSc the
midbrain and brain stem structures were relatively spared, but in patients
with type 2 PrPSc brain stem and midbrain were heavily affected. Although
these prion type-related topographical differences are not completely
identical to those in sheep scrapie, a comparable connection between prion
type and deposition pattern is evident.

Aggregate Stability Regarding Denaturation

Similar to scrapie in sheep, the stability of PrPSc aggregates of human
sporadic CJD against denaturation with GdnHCl showed two groups:
denaturation-resistant and denaturation-sensitive PrPSc aggregates. This
property correlated with the prion protein type according to Parchi et al8
and is independent from the physiologically occurring methionine/valine
polymorphism at codon 129 of the PRNP. By membrane adsorption after GdnHCl
denaturation and proteinase K-digestion, human PrPSc type 1 proved to be
less stable than human PrPSc type 2. While human PrPSc type 2 was detectable
up to GdnHCl concentrations between 3M and 4M, human PrPSc type 1 was stable
up to 2M GdnHCl. Neither methionine nor valine at codon 129 in type 1 or
type 2 seemed to alter the stability of the prion protein aggregates (Figure

Summarizing the results, striking parallels between human PrPSc type 1 and
atypical/Nor98 scrapie as well as human PrPSc type 2 and classical scrapie
are observed with regard to PrPSc deposition and stability of the prion


In humans, different prion types are linked with clinically and
neuropathologically distinct prion diseases.8 The present work emphasizes
that the differences in deposition characteristics and stability with regard
to denaturation between atypical/Nor98 and classical scrapie also account
for different prion types. Moreover, the two scrapie types that have been
characterized show a number of striking similarities with human PrPSc types
in sporadic CJD. Hence, we propose that the existence of different PrPSc
types might be a common denominator of prion diseases in humans and animals.
Since these two prion types show an across-the-species comparability with
similar biochemical and pathological characteristics, it is most likely that
they exist due to a different conformational pattern of the disease-related
prion protein.

Prion Types Depend on Conformation

The interpretation that the conformation of PrPSc accounts for prion types
is supported by different proteinase K-cleavage sites of human prion types9
and the propagation of mutation-associated prion characteristics in human
transgenic mice without PRNP-point mutation. 31 However, differences in
protein stability as they have been found in this study, provide direct
evidence for a conformational distinction between these molecules.32 Further
support for the relation between type and conformation is also given by
experiments focusing on the size of prion protein aggregates. Using virus
removal filters, Kobayashi et al33 were able to show differences in the size
of CJD type 1 and type 2 aggregates: PrPSc type 2 forms larger aggregates
than PrPSc type 1, independent of whether the disease was sporadic,
iatrogenic or acquired. This difference is clearly reflected by the
morphology of the PrPSc depositions we have found in sheep scrapie and human
CJD. Sporadic CJD type 1 and atypical/ Nor98 scrapie are characterized by
fine (reticular) deposits, whereas CJD type 2 and classical scrapie display
a complex aggregate pattern, regardless of the respective genotypes at the
polymorphic positions of the PRNP that were investigated.

Prion Type Characteristics Versus Prion Strain Characteristics

Structural differences of the disease-associated protein have also been
proposed as an explanation for the existence of strains. Partial digestion
of the disease-associated protein with proteinase K as well as differences
in antibody binding after the protein was partially denatured were used to
identify structural characteristics in correlation with strain properties
and different clinical TSE forms.23,34,35 It needs to be considered that the
kinetics of proteinase K-digestion of PrPSc are markedly influenced by
detergent effects in the buffer, demonstrating that the accessibility of the
cleavage sites are variable.35 In contrast, differences in the stability
against total unfolding of PrPSc seem to be a usable criterion to identify
conformational differences or conformational motives. Whereas detergents
affect the tertiary structure of a protein by interacting with hydrophilic
and hydrophobic areas of protein molecules, chaotropic salts like GdnHCl
destroy the hydrogen bonds in -helices and -sheets leading to an irregular
coiled polypeptide chain.36 This is in line with the observation that
detergents remove prion infectivity only partially, whereas chemicals that
destroy secondary structures like chaotropic salts are highly effective. 37
However, detectable differences regarding the stability against denaturation
with GdnHCl shown for various prion strains in hamsters seem to be very
small compared with the ones that can be shown here for the prion types of
human and ovine prion diseases. Strains could thus correspond to structural
differences that are less marked than those defining types and are probably
constant only under defined conditions. Influences of polymorphisms or
interactions with other genetic factors like the promotor region,
species-specific factors like the recently detected incorporation of
polyanionic molecules into prions,38 glycosaminoglycans or other yet unknown
factors of the original host may also lead to different strains in a new
host within the prion types of the original species.5,39 The existence of
prion types does not exclude the existence of strains. The same variations
that account for strains might be the reason for differences in the clinical
disease course of the natural host.

Two Different Prion Types also in BSE?

Parallel to human sporadic CJD and our results in sheep scrapie, there is
increasing evidence that two prion types also exist in cattle BSE. Two
presumably sporadic forms of BSE known as H-type BSE14 and bovine
amyloidotic spongiform encephalopathy, also called L-type BSE,15 have been
described in cattle in addition to typical/classical BSE.40 The small
variation in the apparent molecular weight of the unglycosylated band of
bovine amyloidotic spongiform encephalopathy is considered to be well within
the range of classical BSE,41,42 which would leave H-type BSE with a
considerably larger unglycosylated fragment in Western blot analysis than
the second BSE type. Interestingly, bovine amyloidotic spongiform
encephalopathy converts into classical BSE after serial passages in
bovine-transgenic mice,43 although displaying clinically different diseases
in cattle.44 From the latter experiment the authors concluded that different
strains were responsible for different phenotypes. Obviously the different
clinical diseases were generated by agents that belong to a single prion
type. These results together with our observations emphasize the need to
differentiate strictly between prion types and prion strains and demonstrate
that even in cattle BSE, one prion type may contain different prion strains.

Prion Type Displays Parallels in the Pathophysiology of Disease between

Biochemical and morphological similarities have been used to draw parallels
between forms of BSE and human prion diseases.15 Parallels between species
can also be observed with regard to the route of prion infection: in
classical BSE, variant CJD, and classical scrapie, all of which presumably
belong to one class of prion type (type 2 in humans) according to the
observations made above, the oral route of infection has been identified.
These TSEs use the dorsal motor nucleus of the vagus nerve as an entry site
into the brain.29,45,46 This observation suggests that distinct prion types
in human and animal TSEs possibly have an impact on the pathogenesis of
prion diseases.


As the prion protein is a highly conserved protein in terms of evolution,
parallels between characteristics of prion types in TSEs of different
species are of interest. In the present study, we report previously unknown
similarities between sheep scrapie forms and human sporadic CJD types. We
propose that the observed similarities between sheep scrapie and sporadic
CJD in humans justify new interspecies groups of prion diseases in which
prion types, not prion strains, are the major determinant for prion disease
forms. While epidemiology implies that classical scrapie is not related to
human TSEs,47 the atypical/Nor98 scrapie risk for human transmission has not
yet been elucidated. Currently there is no compelling evidence that sCJD has
a different origin than sporadic genesis. However, the finding of prion
types with an across-the-species comparability might provide further
understanding of the pathogenesis in prion diseases.

Acknowledgments We thank Tatjana Pfander, Nadine Rupprecht, and Kerstin
Brekerbohm for their skillful technical assistance.

hmmm, this is getting interesting now...

Sporadic CJD type 1 and atypical/ Nor98 scrapie are characterized by fine
(reticular) deposits,

see also ;

All of the Heidenhain variants were of the methionine/ methionine type 1
molecular subtype.

Tuesday, July 29, 2008 Heidenhain Variant Creutzfeldt Jakob Disease Case


Heidenhain Variant Creutzfeldt Jakob Disease autopsy case report 'MOM'

DIVISION OF NEUROPATHOLOGY University of Texas Medical Branch 114 McCullough
Bldg. Galveston, Texas 77555-0785


DATE: 4-23-98

TO: Mr. Terry Singeltary @ -------

FROM: Gerald Campbell

FAX: (409) 772-5315 PHONE: (409) 772-2881

Number of Pages (including cover sheet):



This document accompanying this transmission contains confidential
information belonging to the sender that is legally privileged. This
information is intended only for the use of the individual or entry names
above. If you are not the intended recipient, you are hereby notified that
any disclosure, copying distribution, or the taking of any action in
reliances on the contents of this telefaxed information is strictly
prohibited. If you received this telefax in error, please notify us by
telephone immediately to arrange for return of the original
documents. -------------------------- Patient Account: 90000014-518 Med.
Rec. No.: (0160)118511Q Patient Name: POULTER, BARBARA Age: 63 YRS DOB:
10/17/34 Sex: F Admitting Race: C

Attending Dr.: Date / Time Admitted : 12/14/97 1228 Copies to:

UTMB University of Texas Medical Branch Galveston, Texas 77555-0543 (409)
772-1238 Fax (409) 772-5683 Pathology Report

FINAL AUTOPSY DIAGNOSIS Autopsy' Office (409)772-2858

Autopsy NO.: AU-97-00435

AUTOPSY INFORMATION: Occupation: Unknown Birthplace: Unknown Residence:
Crystal Beach Date/Time of Death: 12/14/97 13:30 Date/Time of Autopsy:
12/15/97 15:00 Pathologist/Resident: Pencil/Fernandez Service: Private
Restriction: Brain only


I. Brain: Creutzfeldt-Jakob disease, Heidenhain variant.

snip...see full text ;



Parallels between different forms of sheep scrapie and types of
Creutzfeldt-Jakob disease (CJD)

Wiebke M. Wemheuer1, Sylvie L. Benestad2, Arne Wrede1, Wilhelm E. Wemheuer3,
Tatjana Pfander1, Bjørn Bratberg2, Bertram Brenig3,Walter J.
Schulz-Schaeffer1 1University Medical Center Goettingen, Germany; 2Institute
of Veterinary Medicine Oslo, Norway; 3Institute of Veterinary Medicine
Goettingen, Germany

Background: Scrapie in sheep and goats is often regarded as the archetype of
prion diseases. In 1998, a new form of scrapie - atypical/Nor98 scrapie -
was described that differed from classical scrapie in terms of epidemiology,
Western blot profile, the distribution of pathological prion protein (PrPSc)
in the body and its stability against proteinase K. In a similar way,
distinct disease types exist in sporadic Creutzfeldt-Jakob disease (CJD).
They differ with regard to their clinical outcome, Western blot profile and
PrPSc deposition pattern in the central nervous system (CNS).

Objectives: The comparison of PrPSc deposits in sheep scrapie and human
sporadic CJD.

Methods: Tissues of the CNS of sheep with classical scrapie, sheep with
atypical/Nor98 scrapie and 20 patients with sporadic CJD were examined using
the sensitive Paraffin Embedded Tissue (PET) blot method. The results were
compared with those obtained by immunohistochemistry. With the objective of
gaining information on the protein conformation, the PrPSc of classical and
atypical/Nor98 sheep scrapie and sporadic CJD was tested for its stability
against denaturation with guanidine hydrochloride (GdnHCl) using a Membrane
Adsorption Assay.

Results: The PrPSc of atypical/Nor98 scrapie cases and of CJD prion type 1
patients exhibits a mainly reticular/synaptic deposition pattern in the
brain and is relatively sensitive to denaturation with GdnHCl. In contrast
classical scrapie cases and CJD prion type 2 patients have a more complex
PrPSc deposition pattern in common that consists of larger PrPSc aggregates
and the PrPSc itself is comparatively stable against denaturation.

Discussion: The similarity between CJD types and scrapie types indicates
that at least two comparable forms of the misfolded prion protein exist
beyond species barriers and can elicit prion diseases. It seems therefore
reasonable to classify classical and atypical/Nor98 scrapie - in analogy to
the existing CJD types - as different scrapie types.

Monday, November 30, 2009


Monday, December 1, 2008

When Atypical Scrapie cross species barriers


This is provided by the statistically significant increase in the incidence
of sheep scrape from 1985, as determined from analyses of the submissions
made to VI Centres, and from individual case and flock incident studies.

1: J Infect Dis 1980 Aug;142(2):205-8

Oral transmission of kuru, Creutzfeldt-Jakob disease, and scrapie to
nonhuman primates.

Gibbs CJ Jr, Amyx HL, Bacote A, Masters CL, Gajdusek DC.

Kuru and Creutzfeldt-Jakob disease of humans and scrapie disease of sheep
and goats were transmitted to squirrel monkeys (Saimiri sciureus) that were
exposed to the infectious agents only by their nonforced consumption of
known infectious tissues. The asymptomatic incubation period in the one
monkey exposed to the virus of kuru was 36 months; that in the two monkeys
exposed to the virus of Creutzfeldt-Jakob disease was 23 and 27 months,
respectively; and that in the two monkeys exposed to the virus of scrapie
was 25 and 32 months, respectively. Careful physical examination of the
buccal cavities of all of the monkeys failed to reveal signs or oral
lesions. One additional monkey similarly exposed to kuru has remained
asymptomatic during the 39 months that it has been under observation.


The successful transmission of kuru, Creutzfeldt-Jakob disease, and scrapie
by natural feeding to squirrel monkeys that we have reported provides
further grounds for concern that scrapie-infected meat may occasionally give
rise in humans to Creutzfeldt-Jakob disease.

PMID: 6997404




A The Present Position with respect to Scrapie A] The Problem

Scrapie is a natural disease of sheep and goats. It is a slow and inexorably
progressive degenerative disorder of the nervous system and it ia fatal. It
is enzootic in the United Kingdom but not in all countries.

The field problem has been reviewed by a MAFF working group (ARC 35/77). It
is difficult to assess the incidence in Britain for a variety of reasons but
the disease causes serious financial loss; it is estimated that it cost
Swaledale breeders alone $l.7 M during the five years 1971-1975. A further
inestimable loss arises from the closure of certain export markets, in
particular those of the United States, to British sheep.

It is clear that scrapie in sheep is important commercially and for that
reason alone effective measures to control it should be devised as quickly
as possible.

Recently the question has again been brought up as to whether scrapie is
transmissible to man. This has followed reports that the disease has been
transmitted to primates. One particularly lurid speculation (Gajdusek 1977)
conjectures that the agents of scrapie, kuru, Creutzfeldt-Jakob disease and
transmissible encephalopathy of mink are varieties of a single "virus". The
U.S. Department of Agriculture concluded that it could "no longer justify or
permit scrapie-blood line and scrapie-exposed sheep and goats to be
processed for human or animal food at slaughter or rendering plants" (ARC
84/77)" The problem is emphasised by the finding that some strains of
scrapie produce lesions identical to the once which characterise the human

Whether true or not. the hypothesis that these agents might be transmissible
to man raises two considerations. First, the safety of laboratory personnel
requires prompt attention. Second, action such as the "scorched meat" policy
of USDA makes the solution of the acrapie problem urgent if the sheep
industry is not to suffer grievously.



Nature. 1972 Mar 10;236(5341):73-4.

Transmission of scrapie to the cynomolgus monkey (Macaca fascicularis).
Gibbs CJ Jr, Gajdusek DC.

Nature 236, 73 - 74 (10 March 1972); doi:10.1038/236073a0

Transmission of Scrapie to the Cynomolgus Monkey (Macaca fascicularis)


National Institute of Neurological Diseases and Stroke, National Institutes
of Health, Bethesda, Maryland

SCRAPIE has been transmitted to the cynomolgus, or crab-eating, monkey
(Macaca fascicularis) with an incubation period of more than 5 yr from the
time of intracerebral inoculation of scrapie-infected mouse brain. The
animal developed a chronic central nervous system degeneration, with ataxia,
tremor and myoclonus with associated severe scrapie-like pathology of
intensive astroglial hypertrophy and proliferation, neuronal vacuolation and
status spongiosus of grey matter. The strain of scrapie virus used was the
eighth passage in Swiss mice (NIH) of a Compton strain of scrapie obtained
as ninth intracerebral passage of the agent in goat brain, from Dr R. L.
Chandler (ARC, Compton, Berkshire).

Epidemiology of Scrapie in the United States 1977

Tuesday, April 28, 2009

Nor98-like Scrapie in the United States of America

Scrapie USA


Like lambs to the slaughter 31 March 2001 by Debora MacKenzie Magazine issue

FOUR years ago, Terry Singeltary watched his mother die horribly from a
degenerative brain disease. Doctors told him it was Alzheimer's, but
Singeltary was suspicious. The diagnosis didn't fit her violent symptoms,
and he demanded an autopsy. It showed she had died of sporadic
Creutzfeldt-Jakob disease.

Most doctors believe that sCJD is caused by a prion protein deforming by
chance into a killer. But Singeltary thinks otherwise. He is one of a number
of campaigners who say that some sCJD, like the variant CJD related to BSE,
is caused by eating meat from infected animals. Their suspicions have
focused on sheep carrying scrapie, a BSE-like disease that is widespread in
flocks across Europe and North America.

Now scientists in France have stumbled across new evidence that adds weight
to the campaigners' fears. To their complete surprise, the researchers found
that one strain of scrapie causes the same brain damage in ...


R.I.P. MOM hvCJD confirmed DECEMBER 14, 1997

Monday, December 14, 2009

Similarities between Forms of Sheep Scrapie and Creutzfeldt-Jakob Disease
Are Encoded by Distinct Prion Types

Tuesday, August 18, 2009 BSE-The Untold Story - joe gibbs and singeltary
1999 - 2009 Greetings,


Wednesday, December 30, 2009

Is there evidence of vertical transmission of variant CJD ?


Alzheimer's and CJD


Terry S. Singeltary Sr. P.O. Box 42 Bacliff, Texas USA

Friday, January 01, 2010

Human Prion Diseases in the United States


-------------------- BSE-L@LISTS.AEGEE.ORG --------------------

No competing interests declared.

RE: re-Human Prion Diseases in the United States part 2

flounder replied to flounder on 02 Jan 2010 at 21:26 GMT

I would kindly like to add to my initial concerns, something I brought up years ago, and I believe that still hold true today, more so even than when I first stated these concerns in 2003 ;

routine passive mortality CJD surveillance USA ?

THIS has been proven not to be very useful in the U.K.;



One reason for this was the _inaccuracy_ in coding of cases correctly certified as CJD Coding is carried out by staff who are not medically qualified and it is not surprising that coding errors occur in the processing of large numbers of certificates. In 1982, 12,000 certificates per week were processed at the office of population censuses and surveys by 15 coders and 6 checkers (Alderson et al., 1983). The occurrence of both inter- and intra-observer coding errors has been described (Curb et al., 1983) and the _inaccuracies_ of BOTH certification and coding discovered in this study _support_ the introduction of a more accurate system of death certificates and a more detailed and specific coding system...


Draft Proposal For The Monitoring of Creutzfeldt-Kakob Disease 1989 Dr. R. Will



Cases of CJD may be identified from death certificates, but this alone is unlikely to provide adequate monitoring. ERRORS are made in certification and diagnosis; in the Oxford study death certificates were obtained on a series of known confirmed cases and CJD was mentioned in only 66% of certificates. In another series of 175 certified cases, 42 patients were judged not to have suffered from CJD after examination of case notes (7)...

full text;

AS implied in the Inset 25 we must not _ASSUME_ that transmission of BSE to other species will invariably present pathology typical of a scrapie-like disease.


Confucius is confused again? how in 1996 and earlier can the 28 sporadic CJD victims and the one-in-a-million there from, how can it still be one in a million in 2008, with the sporadic CJD count rising to 205, still be one-in-a-million? and the years in-between, steady rise just about every year, and it still be only one-in-a-million, year after year after years? I suppose just more of that fuzzy math, which you can see here;


Please see my complete comment to this synopsis here ;

Saturday, January 2, 2010

Human Prion Diseases in the United States January 1, 2010


No competing interests declared.

RE: RE: re-Human Prion Diseases in the United States part 2

flounder replied to flounder on 02 Jan 2011 at 20:00 GMT

Wednesday, December 29, 2010



Wednesday, December 29, 2010

CWD Update 99 December 13, 2010


Terry S. Singeltary Sr. P.O. Box 42 Bacliff, Texas USA 77518

No competing interests declared.