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Friday, January 8, 2010


A ProMED-mail post

ProMED-mail is a program of the
International Society for Infectious Diseases

[With the continuing decline in the number of cases in the human
population of variant Creutzfeldt-Jakob disease -- abbreviated
previously as vCJD or CJD (new var.) in ProMED-mail -- it has been
decided to broaden the scope of the occasional ProMED-mail updates to
include some other prion-related diseases. In addition to vCJD, data
on other forms of CJD: sporadic, iatrogenic, familial, and GSS
(Gerstmann-Straussler-Scheinker disease), are included also since
they may have some relevance to the incidence and etiology of vCJD. - Mod.CP]

In this update:
[1] UK: National CJD Surveillance Unit - monthly statistics as of 5 Jan 2010
[2] France: Institut de Veille Sanitaire - monthly statistics as of 4 Jan 2010
[3] US National Prion Disease Center - not updated since 7 Nov 2009
[4] Portuguese vCJD case - pathology
[5] vCJD codon 129 heterozygote
[6] vCJD codon 129 heterozygote - Lancet paper
[7] Prion evolution & a new reagent

[1] UK: National CJD Surveillance Unit - monthly statistics as of 5 Jan 2010
Date: Tue 5 Jan 2010
Source: UK National CJD Surveillance Unit, monthly statistics [edited]

The number of deaths due to definite or probable vCJD cases remains
166. A total of 4 definite/probable patients are still alive, so that
the total number of definite or probable vCJD cases remains 170 for
the year 2009.

Although 2 new cases vCJE were recorded in 2009, the overall picture
is still consistent with the view that the vCJD outbreak in the UK is
in decline, albeit now with a pronounced tail. The 1st cases were
observed in 1995, and the peak number of deaths was 28 in the year
2000, followed by 20 in 2001, 17 in 2002, 18 in 2003, 9 in 2004, 5 in
2005, 5 in 2006, 5 in 2007, one in 2008, and 2 in 2009.

Totals for all types of CJD cases in the UK in the year 2009
During the 12 months of 2009, there have been 143 referrals, 59 cases
of sporadic CJD, one case of familial CJD, one case of iatrogenic
CJD, 3 cases of GSS, and 2 cases of vCJD.

Communicated by:

[2] France: Institut de Veille Sanitaire - monthly statistics as of 4 Jan 2010
Date: Mon 4 Jan 2010
Source: IVS - Maladie de Creutzfeldt-Jakob et maladies apparentees
[in French, trans. & summ. Mod.CP]

During the 12 months of 2009, there were 1486 referrals, 85 cases of
sporadic CJD, 10 cases of familial CJD, 3 cases of iatrogenic CJD,
and 2 confirmed cases of vCJD.

A total of 25 cases of confirmed or probable vCJD has now been
recorded in France since 1997. The 25 confirmed cases comprise 13
females and 12 males. All 25 are now deceased. Their median age is 37
(between 19 and 58). Seven were resident in the Ile-de-France and 18
in the provinces. All the identified cases have been Met-Met
homozygotes. No risk factor has been identified. One of the 25 had
made frequent visits to the United Kingdom.

Communicated by:

[3] US National Prion Disease Center - not updated since 7 Nov 2009
Date: Sat 7 Nov 2009
Source: US National Prion Disease Pathology Surveillance Center [edited]

(Report not updated since 7 Dec 2009): During the period 1 Jan 2009
to 7 Nov 2009, there were 341 referrals, of which 198 were classified
as Prion disease, comprising 133 cases of sporadic CJD, 33 of
familial CJD, and no cases of iatrogenic CJD or vCJD.

Communicated by:

[4] Portuguese vCJD case - pathology
Date: Fri 1 Jan 2010
Source: J Neurol Neurosurg Psychiatry 2010 Jan;81(1):112-4. [edited]

Title: Variant Creutzfeldt-Jakob disease: the first confirmed case
from Portugal shows early onset, long duration and unusual pathology.

Authors: Barbot C, Castro L, Oliveira C, Carpenter S.
At: Department of Neuropaediatrics, Hospital Maria Pia, Porto, Portugal.

We present clinical and autopsy findings in the 1st case of variant
Creutzfeldt-Jakob disease diagnosed and confirmed in Portugal. Onset
was at 11 years, the earliest onset reported, and the course (32
months) relatively long. Western blot showed protease resistant prion
protein, mainly of type 4 (2B) isoform. The cerebral cortex revealed
severe spongiform change with numerous amyloid plaques, which did not
fit the definition of florid plaques. In the striatum, spongiform
change was limited, but the extracellular space was dilated. Other
reports have found marked spongiform change in the striatum and
little in the cortex. Massive neuronal loss, in excess of what has
been described, was found in the thalamus and pontine grey. The
cerebellum showed, as expected, severe loss of granule cells,
moderate loss of Purkinje cells and marked immunopositivity for the
prion protein. Differences between our findings and previous ones
probably result from the patient's long survival.

Communicated by:
Terry S. Singeltary Sr.

[5] vCJD codon 129 heterozygote
Date: Fri 19 Dec 2009
Source: BBC News, Health [edited]

A 30-year-old man thought to have died in January [2009] from vCJD
belonged to a genetic group that had not shown any signs of the
disease, scientists say. In the UK, 166 people have died of vCJD,
linked to eating BSE [bovine spongiform encephalopathy] infected
beef, and all were thought to have shared a certain gene.

Writing in the Lancet, scientists say that the victim, a resident of,
Lanarkshire [Scotland], had a different version of the gene. They
estimate that up to 350 people in this group could get vCJD.
Scientists have always thought that a 2nd wave of vCJD cases would
emerge some time after the 1st. This is the 1st indication that this
theory is being born out, with the identification of the 1st probable
vCJD patient outside of the initial genetic group, BBC science
correspondent Pallab Ghosh reports.

The father believes his son was incubating the disease for much of
his life. It is probable because the diagnosis is based on
observations of the progression of the disease rather than
post-mortem tests which would have provided absolute confirmation of
the disease, he adds.

The case report written by Professor John Collinge of the National
Prion Clinic and colleagues is a reminder that the disease has not
gone away. Many thousands of people may be carrying the infection,
and although they will never show any symptoms, they have the
potential to infect others.

vCJD is caused by infectious agents called prions. Prion diseases
affect the structure of the brain or other neural tissue and are
currently untreatable. Disease-causing prions are thought to consist
of abnormally folded proteins, which spread by encouraging the normal
healthy prion protein found on the surface of most cells in the body
to change shape. Tests showed that the patient had a heterozygous
version of the gene which codes for the human prion amino acids
valine (V) or methionine (M). People can be V V (homozygous), M M
(homozygous) or M V (heterozygous). Since 1994, around 200 cases of
vCJD have been identified worldwide, and all those tested have been M
M homozygous. [However, genetic analysis of 2 out of 3 prion-positive
appendix samples in the tissue-based prevalence study in 2001-2004
showed that both were valine homozygous (VV) at codon 129 in the
prion protein gene (Ironside et al, Brit Med J 2006). - Mod.CP].
However, this most recent victim was M/V heterozygous. It is thought
that 47 percent of the population have this version of the gene.
Professor Collinge said: "The majority of the UK population have
potentially been exposed to BSE prions, but the extent of clinically
silent infection remains unclear. About 1/3rd of the UK population
are M/M homozygous. If individuals with other genotypes [M/V and V/V]
are similarly susceptible to developing prion disease after BSE prion
exposure, but with longer incubation periods, further cases would be expected."

The scientists have previously looked at another prion disease in New
Guinea called "kuru" [which was induced by eating infected human
brain tissue. - Mod.CP]. The original cases were all M/M, but more
recently, M/V cases have appeared. They say this indicates that M/V
people can get prion diseases like kuru but have a much longer
incubation period.

Communicated by:

[The abstract of the Lancet paper upon which the above report is
based is reproduced below. - Mod.CP]

[6] vCJD codon 129 heterozygote - Lancet paper
Date: Thu 18 Dec 2009
Source: Lancet 2009; 374: 2128 [edited]

[A Case Report published in the 18 Dec 2009 issue of the Lancet by
Professor John Collinge, MRC Prion Unit and National Prion Clinic,
UCL Institute of Neurology and National Hospital for Neurology and
Neurosurgery, London]

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. Two months later, he developed 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 [a
rapid movement of the eye between fixation points]. 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 2 crutches to walk. Medical history included
tonsillectomy and removal of a cervical lymph node 15 years
previously, but he had never had a blood transfusion 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 [magnetic
resonance imaging] of the brain was consistent with the pulvinar sign
(illustrated in the original text). Although not all
neuroradiologists consulted considered the pulvinar sign positive,
quantitative assessment showed symmetrical higher signal in the
pulvinar nuclei than the caudate nuclei (illustrated in the original
text). 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 diagnosis of variant
Creutzfeldt-Jakob disease (vCJD) was made on the basis of a
characteristic clinical onset and progression, 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 care givers 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
characteristic neuropathological features and tissue distribution of
infectivity, and a distinctive type 4 (London classification)
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 1/3rd of the UK
population are PRNP codon 129 methionine homozygous. If individuals
with other genotypes [V/V or V/M] 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.


(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: 10759-64.

(5) Wadsworth JD, Asante E, Desbruslais M, et al. Human prion protein
with valine 129 prevents expression of variant CJD phenotype. Science
2004; 306: 1793-96.

[Acknowledgment: MRC Prion Unit and National Prion Clinic, UCL
Institute of Neurology and National Hospital for Neurology and
Neurosurgery, London, UK (D Kaski MRCP, S Mead PhD, H Hyare FRCR,
Prof J Collinge FRS, P Rudge FRCP); Institute of Neurological
Sciences, Glasgow University, Glasgow, UK (S Cooper MRCP, R Jampana
FRCR, J Overell FRCP); and National CJD Surveillance Unit, Western
General Hospital, Edinburgh, UK (Prof R Knight FRCP)]

Communicated by:

[To put this work in perspective, parts of a British Medical Journal
editorial by Maurizio Pocchiari are reproduced below. - Mod.CP.

Date: 21 May 2009
Source: BMJ 2009;338:b435 [edited]

"Prevalence of variant CJD in the UK
The number of cases of variant Creutzfeldt-Jakob disease (vCJD) in
the United Kingdom has decreased since 2000, but controversy remains
about how many people carry the infectious agent and will eventually
develop disease. Clewley and colleagues in a limited study add to the
debate by assessing 63 007 pairs of tonsils for the only available
marker of prion disease, the pathological, partially protease
resistant, prion protein. Although more than half of the samples came
from people born between 1961 and 1995, when the risk of exposure to
bovine spongiform encephalopathy (BSE) infection was high, no
convincingly positive tonsil specimens were detected. This study
estimated that the prevalence of vCJD in the British population is
zero, but with a large confidence interval of 0 to 113 per million.

This result agrees with one UK survey of 2000 tonsil specimens, but
it differs from another survey of 1427 tonsils and 11 247 appendices,
which found that more than 10 000 people might be incubating the
disease. However, despite the discrepancy, the 95 percent confidence
intervals of the 2 studies overlap, indicating that the results do
not differ significantly and that many people in the UK may be carriers.

The chance that no one in the UK is incubating the disease, as
suggested by the lower confidence limit of Clewley and colleagues'
study, is unlikely because backup calculations predict up to 100 new
cases of vCJD in the next 50 years. This prediction seems reasonable
unless most cases of vCJD were missed by surveillance in the past years.

Until December 2008, all 210 people reported to have vCJD (164 in the
UK, 46 in other countries) were homozygous for methionine at the
polymorphic codon 129 of the prion protein gene (PRNP), suggesting
that genetic factors strongly influence the development of disease.
Whether people who are heterozygous for methionine and valine or
homozygous for valine at this codon (about 60 percent of the
population) will develop vCJD in the future is still unknown.
However, data from gene targeted transgenic mice indicate that these
people are also susceptible to BSE and vCJD, although incubation
periods are longer than in those who are homozygous for methionine."

Interested readers should consult the original article for further
information and references. - Mod.CP]

[7] Prion evolution & a new reagent
Date: 1 Jan 2010
Source: BBC Health News [edited]

Abnormal prion proteins cause at least 20 fatal diseases. Scientists
have shown for the 1st time that "lifeless" prion proteins, devoid of
all genetic material, can evolve just like higher forms of life. The
Scripps Research Institute in the US says the prions can change to
suit their environment and go on to develop drug resistance.

Prions are associated with 20 different brain diseases in humans and
animals. The scientists say their work suggests new approaches might
be necessary to develop therapies for these diseases. In the study,
published in the journal Science [see below], the scientists
transferred prion populations from brain cells to other cells in
culture and observed the prions that adapted to the new cellular
environment out-competed their brain-adapted counterparts. When
returned to the brain cells, the brain-adapted prions again took over
the population.

Charles Weissmann, head of Scripps Florida's department of
infectology who led the study, said: "On the face of it, you have
exactly the same process of mutation and adaptive change in prions as
you see in viruses. This is a timely reminder that prion concerns are
not going away and that controls to stop abnormal prions being
transmitted to humans through the food system or through blood
transfusions must be vigorously maintained."

Professor John Collinge, Medical Research Council Prion Unit stated
that: "This means that this pattern of Darwinian evolution appears to
be universally active. In viruses, mutation is linked to changes in
nucleic acid sequence that leads to resistance. Now, this
adaptability has moved one level down -- to prions and protein
folding -- and it's clear that you do not need nucleic acid (DNA or
RNA) for the process of evolution."

Mammalian cells normally produce cellular prion protein or PrPC.
During infections, such as the human form of mad cow disease, known
as vCJD, abnormal or mis-folded proteins convert the normal host
prion protein into its toxic form by changing its conformation or
shape. "It was generally thought that once cellular prion protein was
converted into the abnormal form, there was no further change," Prof.
Weissmann said. "But there have been hints that something was
happening. When you transmit prions from sheep to mice, they become
more virulent over time. Now we know that the abnormal prions
replicate and create variants, perhaps at a low level initially. But
once they are transferred to a new host, natural selection will
eventually choose the more virulent and aggressive variants."

Professor John Collinge, of the Medical Research Council's (MRC)
Prion Unit, described the research as exciting confirmation of a
hypothesis that he had proposed 2 years ago, that there could be a
"cloud" or whole array of prion proteins in the body. He called it
the cloud hypothesis: "The prion protein is not a clone, it is a
quasi-species that can create different protein strains even in the
same animal. The abnormal prion proteins multiply by converting
normal prion proteins. The implication of Charles Weissmann's work is
that it would be better to cut off that supply of normal prion
proteins rather than risk the abnormal prion adapting to a drug and
evolving into a new more virulent form. You would do this by trying
to block the sites on the normal prion protein that the abnormal form
locks on to to do its conversion. We know there is an antibody that
can do this in mice, and the Medical Research Council's Prion Unit
have managed to engineer a human antibody to do this. It is currently
undergoing safety tests, and we hope to move to clinical trials by
the end of 2011."

Professor Collinge said the MRC was also trying to find more
conventional chemical compounds to do this and has been collaborating
with the chemical company GlaxoSmithKline (GSK). He said: "They have
given us access to their chemical libraries, which contain millions
of compounds, and we have already identified some that may work well.
This is a timely reminder that prion concerns are not going away and
that controls to stop abnormal prions being transmitted to humans
through the food system or through blood transfusions must be
vigorously maintained."

Communicated by:

[The abstract and the reference for the Science paper descried above
are the following: Science DOI: 10.1126/science.1183218, Published
Online 31 Dec 2009.
Darwinian Evolution of Prions in Cell Culture. By Jiali Li, Shawn
Browning, Sukhvir P. Mahal, Anja M. Oelschlegel, Charles Weissmann
At: Department of Infectology, Scripps Florida, 130 Scripps Way,
Jupiter, FL 33458, USA.

Abstract: "Prions are infectious proteins consisting mainly of PrPSc,
a sheet-rich conformer of the normal host protein PrPC, and occur in
different strains. Strain identity is thought to be encoded by PrPSc
conformation. We found that biologically cloned prion populations
gradually became heterogeneous by accumulating "mutants," and
selective pressures resulted in the emergence of different mutants as
major constituents of the evolving population. Thus, when transferred
from brain to cultured cells, "cell-adapted" prions out competed
their "brain-adapted" counterparts, and the opposite occurred when
prions were returned from cells to brain. Similarly, the inhibitor
swainsonine selected for a resistant substrain, whereas in its
absence, the susceptible substrain outgrew its resistant counterpart.
Prions, albeit devoid of a nucleic acid genome, are thus subject to
mutation and selective amplification."

From a theoretical standpoint, this work has great significance.
Nonetheless, the immediate interest of the BBC News report is the
information that Professor John Collinge's MRC group has succeeded in
engineering a humanised monoclonal antibody that interacts with the
sites on the normal prion protein that the abnormal form locks onto
to achieve its conversion and that it is hoped eventually to move to
clinical trials of this reagent. - Mod.CP]

[see also:
Prion disease update 2009 (10) 20091103.3784
vCJD - Italy: susp. 20091024.3671
Prion disease update 2009 (09) 20091005.3461
Prion disease update 2009 (08) 20090908.3170
Prion disease update 2009 (07) 20090806.2783
Prion disease update 2009 (06) 20090706.2433
Prion disease update 2009 (05) 20090602.2054
Prion disease update 2009 (04) 20090406.1337
vCJD, 5th death - Spain (Cantabria) 20090307.0953
Prion disease update 2009 (03) 20090305.0918
Prion disease update 2009 (02) 20090202.0463
Prion disease update 2009 (01) 20090108.0076
Prion disease update 2008 (14): new vCJD wave imminent? 20081218.3980
Prion disease update 2008 (13) 20081201.3780
Prion disease update 2008 (12) 20081103.345
Prion disease update 2008 (11) 20081006.3159
vCJD, mother & son - Spain: (Leon) 20080926.3051
Prion disease update 2008 (10) 20080902.2742
vCJD - Spain: susp. 20080410.1311
Prion disease update 2008 (05) 20080408.1285
Prion disease update 2008 (01): correction 20080104.0046
Prion disease update 2008 (01) 20080102.0014
Prion disease update 2007 (08) 20071205.3923
Prion disease update 2007 (07) 20071105.3602
Prion disease update 2007 (06) 20071003.3269
Prion disease update 2007 (05) 20070901.2879
Prion disease update 2007 (04) 20070806.2560
Prion disease update 2007 (03) 20070702.2112
Prion disease update 2007 (02) 20070604.1812
Prion disease update 2007 20070514.1542
CJD (new var.) update 2007 (05) 20070403.1130
CJD (new var.) update 2007 (04) 20070305.0780
CJD (new var.) update 2007 (03) 20070205.0455
CJD (new var.) update 2007 (02): South Korea, susp 20070115.0199
CJD (new var.), blood transfusion risk 20061208.3468
CJD, transmission risk - Canada (ON) 20061207.3457
CJD (new var.) update 2006 (12) 20061205.3431
CJD (new var.) update 2006 (11) 20061106.3190
CJD (new var.) update 2006 (10) 20061002.2820
CJD (new var.) - Netherlands: 2nd case 20060623.1741
CJD (new var.) - UK: 3rd transfusion-related case 20060209.0432
CJD (new var.) update 2006 (02) 20060206.0386
CJD (new var.) update 2006 20060111.0101
CJD (new var.) update 2005 (12) 20051209.3547
CJD (new var.) update 2005 (11) 20051108.3270
CJD (new var.) update 2005 (10) 20051006.2916
CJD (new var.) update 2005 (02) 20050211.0467
CJD (new var.) - UK: update 2005 (01) 20050111.0095
CJD, genetic susceptibility 20041112.3064
CJD (new var.) - UK: update 2004 (14) 20041206.3242
CJD (new var.) - UK: update 2004 (10) 20040909.2518
CJD (new var.) - UK: update 2004 (02) 20040202.0400
CJD (new var.) - UK: update 2004 (01) 20040106.0064
CJD (new var.) - France: 8th case 20041022.2864
CJD (new var.) - France: 9th case 20041123.3138
CJD (new var.), blood supply - UK 20040318.0758
CJD (new var.), carrier frequency study - UK 20040521.1365
CJD (new var.) - UK: update 2003 (13) 20031216.3072
CJD (new var.) - UK: update 2003 (01) 20030108.0057
CJD (new var.) - UK: update Dec 2002 20021207.5997
CJD (new var.) - UK: update Jan 2002 20020111.3223
CJD (new var.), incidence & trends - UK (02) 20011124.2875
CJD (new var.), incidence & trends - UK 20011115.2816
CJD (new var.) - UK: reassessment 20011029.2671
CJD (new var.) - UK: update Oct 2001 20011005.2419
CJD (new var.) - UK: regional variation (02) 20010907.2145
CJD (new var.) - UK: update Sep 2001 20010906.2134
CJD (new var.) - UK: update Aug 2001 20010808.1872
CJD (new var.) - UK: 9th Annual Report 20010628.1231
CJD (new var.) - UK: update June 2001 20010622.1188
CJD (new var.) - UK: update 3 Jan 2001 20010104.0025]

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1 comment:

Terry S. Singeltary Sr. said...

Saturday, January 2, 2010

Human Prion Diseases in the United States January 1, 2010 ***FINAL***

THIS is inaccurate, please see facts ;

my comments to PLosone here ;

I kindly disagree with your synopsis for the following reasons ;