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Friday, February 5, 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 1 Feb
2010 - 1st vCJD fatality in 2010
[2] France: Institut de Veille Sanitaire: monthly statistics as of 2 Feb 2010
[3] US National Prion Disease Center: cases examined as of 31 Dec 2009
[4] CJD/vCJD surveillance in the USA
[5] Prions from recombinant protein

[1] UK: National CJD Surveillance Unit: monthly statistics as of 1 Feb
2010 - 1st vCJD fatality in 2010
Date: Mon 1 Feb 2010
Source: UK National CJD Surveillance Unit, monthly statistics [edited]

The number of deaths due to definite or probable vCJD cases has now
increased to 167. A total of 3 definite/probable patients are still
alive so that the total number of definite or probable vCJD cases is
now 170. So far, one fatality has occurred in 2010.

Although 2 new deaths due to vCJD were recorded in 2009 and one death
so far in 2010, 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, 2 in 2009, and one so far in 2010.

Totals for all types of CJD cases in the UK so far in the year 2010
During the 1st month or 2010, there have been 11 referrals, 5 fatal
cases of sporadic CJD, one fatal case of vCJD, and none of familial
CJD, iatrogenic CJD, or GSS.

Communicated by:

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

During the 1st months of 2010, there were 135 referrals, 5 cases of
sporadic CJD, and none of familial CJD, iatrogenic CJD, or vCJD.

A total of 25 cases of confirmed or probable vCJD has now been
recorded in France since records began in 1992. There was 1 case in
1996, 1 in 2000, 1 in 2001, 3 in 2002, 2 in 2004, 6 in 2005, 6 in
2006, 3 in 2007, and 2 in 2009.

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

Communicated by:

[3] US National Prion Disease Center: cases examined as of 31 Dec 2009
Date: 31 Dec 2009
Source: US National Prion Disease Pathology Surveillance Center [edited]

During the period 1 Jan 2009 to 31 Dec 2009, there were 391 referrals,
of which 233 were classified as prion disease, comprising 158 fatal
cases of sporadic CJD, 35 of familial CJD, and no cases of iatrogenic
CJD or vCJD.

Communicated by:

[4] CJD/vCJD surveillance in the USA
Date: Fri 1 Jan 2010
Source: PLoS ONE 5(1): e8521. doi:10.1371/journal.pone.0008521 [edited]

Human Prion Diseases in the United States
By Robert C. Holman1, Ermias D. Belay1, Krista Y. Christensen1, Ryan
A. Maddox1, Arialdi M. Minino2, Arianne M. Folkema1, Dana L.
Haberling1, Teresa A. Hammett1, Kenneth D. Kochanek2, James J.
Sejvar1, Lawrence B. Schonberger1

At: 1 Division of Viral and Rickettsial Diseases, National Center for
Zoonotic, Vector-borne and Enteric Diseases, Centers for Disease
Control and Prevention (CDC), U.S. Department of Health and Human
Services (USDHHS), Atlanta, Georgia, United States of America, 2
Division of Vital Statistics, National Center for Health Statistics,
Centers for Disease Control and Prevention (CDC), U.S. Department of
Health and Human Services (USDHHS), Hyattsville, Maryland, United
States of America

Background: Prion diseases are a family of rare, progressive,
neurodegenerative disorders that affect humans and animals. The most
common form of human prion disease, Creutzfeldt-Jakob disease (CJD),
occurs worldwide. Variant CJD (vCJD), a recently emerged human prion
disease, is a zoonotic foodborne disorder that occurs almost
exclusively in countries with outbreaks of bovine spongiform
encephalopathy. This study describes the occurrence and epidemiology
of CJD and vCJD in the United States.

Methodology/Principal Findings: Analysis of CJD and vCJD deaths using
death certificates of US residents for 1979-2006, and those identified
through other surveillance mechanisms during 1996-2008: Since CJD is
invariably fatal, and illness duration is usually less than one year,
the CJD incidence is estimated as the death rate. During 1979 through
2006, an estimated 6917 deaths with CJD as a cause of death were
reported in the United States, an annual average of approximately 247
deaths (range 172-304 deaths). The average annual age-adjusted
incidence for CJD was 0.97 per 1 000 000 persons. Most (61.8 percent)
of the CJD deaths occurred among persons 65 years of age or older for
an average annual incidence of 4.8 per 1 000 000 persons in this
population. Most deaths were among whites (94.6 percent); the
age-adjusted incidence for whites was 2.7 times greater than that for
blacks (1.04 and 0.40, respectively).

****3 patients who died since 2004 were reported with vCJD;
epidemiologic evidence indicated that their infection was acquired
outside of the United States.

Conclusion/Significance: Surveillance continues to show an annual CJD
incidence rate of about 1 case per 1 000 000 persons and marked
differences in CJD rates by age and race in the United States. Ongoing
surveillance remains important for monitoring the stability of the CJD
incidence rates and detecting occurrences of vCJD and possibly other
novel prion diseases in the United States.

Communicated by:
Terry S. Singeltary Sr.

[The following is an extract from the Discussion section of the
foregoing paper. Interested readers should consult the original text
for the primary references. - Mod.CP:

"The US incidence of CJD during 1979 through 2006 remained relatively
stable at approximately 1 case per 1 000 000 persons; this incidence
is similar to that reported in many other countries. In the present
study, the large number of cases identified in ongoing US surveillance
provides insights into the incidence of CJD by sex. These data
demonstrate a majority (52.6 percent) of cases in females, largely
because of the higher number of women compared to men in the older age
populations that experienced the highest CJD incidence rates.
Incidence rates of CJD by sex were almost the same among persons
younger than 60 years of age and were higher among males relative to
females as the age of the population groups increased. These findings
are consistent with other studies that indicate a relative excess of
cases among females but a higher incidence of CJD among the male
population. The CJD incidence rates varied regionally, with the
highest rate in the Northeast region and the low!
est rates in the South and West regions. The low rate in the West is
of particular interest due to the longstanding presence of chronic
wasting disease (CWD) among cervids in parts of the region,
particularly in Colorado and Wyoming.

Ongoing US surveillance data continue to demonstrate marked
differences in CJD incidence by race and age. Similar to previous US
reports, the age-adjusted incidence remains more than 2.5 times higher
for whites than for blacks. Although the reasons for this disparity
are unknown, it is possible that genetic differences and/or
under-diagnosis among non-white patients could contribute. These
continuing differences in incidence by race in the United States raise
the possibility that the CJD incidence in countries where black
populations predominate might be significantly lower than in countries
where white populations predominate, an issue that deserves future

The incidence of CJD by age continues to show a pattern that is
strikingly different from that reported for vCJD. Almost all vCJD
cases, including all 3 US resident cases, died before 55 years of age.
The US surveillance analysis illustrates that only about 11 percent of
the CJD cases occurred in this younger US population. This relatively
low proportion, and incidence rate, of CJD cases in this younger age
group occurred despite an increased focus in US surveillance efforts
on suspected cases in this age group since 1996. Cases of CJD younger
than 30 years of age in the United States remain extremely rare, with
most of these cases being attributable to iatrogenic exposure or a
genetic mutation.

The incidence of CJD dramatically increased with increasing age until
it peaked in the 70-79 year age group. An explanation for the
subsequent drop in incidence of CJD among those 80 years of age and
older, a phenomenon consistently observed in earlier surveillance
studies of CJD, remains uncertain. The rarity of CJD, however, in
postmortem studies of possibly clinically unrecognized cases of CJD in
the elderly has led to the suggestion that the decline in incidence
among the elderly is real and unlikely an artifact of a varying
sensitivity, by age group, of surveillance.

Since vCJD was initially recognized in the United Kingdom in 1996, CDC
received reports of 3 subsequently confirmed cases of vCJD among US
residents. The epidemiological data indicated that each of these cases
was most likely infected in the United Kingdom (2 cases) and in Saudi
Arabia (1 case).

Through mid-2009, 20 cases of BSE (bovine spongiform encephalopathy)
were identified among cattle in North America, including 3 that were
identified in the United States. In comparison, the United Kingdom
reported more than 184 000 BSE cases as of 28 Sep 2008 and 168 cases
of vCJD as of 2 Mar 2009. These BSE/vCJD data suggest that the
greatest risk of vCJD in US residents will continue to be among
persons who as a child or young adult consumed UK beef products during
1980-1996, the years when such products were most subject to BSE
contamination. Such US residents would include those who were born and
raised either in the United Kingdom or in another country where
potentially BSE contaminated UK beef products were available for
consumption. These persons would also include those who consumed such
UK beef products as a child or young adult during visits abroad. The
United States historically has imported few or no live cattle, beef
products, or livestock nutritional supplements from the United
Kingdom, and throughout the 1990s had banned the import of live
ruminants and most ruminant products from known BSE countries. Because
indigenous BSE cases in North America were initially documented in
2003 and have continued to occur through 2008, albeit in relatively
low numbers, the results of ongoing US vCJD surveillance receives
considerable attention, particularly among those concerned about the
emergence of indigenous vCJD cases in the United States.

Limitations of using the US national multiple cause-of-death data
include possible coding and reporting discrepancies, and misdiagnosis
of CJD as a cause of death. However, the use of national death
certificate data has been found to be a reasonably sensitive (=80
percent) method compared to more active methods of CJD case
ascertainment. Furthermore, the US prion disease surveillance includes
activities carried out by the NPDPSC (National Prion Disease Pathology
Surveillance Center -- see part [3] above). The NPDPSC, established by
CDC in collaboration with the American Association of
Neuropathologists, makes prion disease testing available
free-of-charge to US physicians, which can help to improve the
accuracy of prion disease diagnoses. This center can confirm or refute
the presence of vCJD, and also detect other unusual or new prion
diseases. The prion surveillance efforts further utilize the
laboratory test results in the investigation and identification of CJD
among persons younger than 55 years of age. Finally, the use of the
SuperMICAR procedure beginning in 1999 (fully in 2003) enables
detection of deaths with prion disease even if cause of death on the
death certificate is miscoded (e.g., an inappropriate coding rule, a
misinterpretation or a misreading of the certificate).

The occurrence of CJD and vCJD continues to be an international and
national concern. Ongoing CJD and vCJD surveillance in many countries
of the world, including the United States, remains critical for
determining the extent to which the agents of classic and possibly
atypical BSE may cause disease in humans. Physicians and health care
workers in the United States are encouraged to indicate CJD, as
appropriate, on death certificates for all their patients who die with
CJD or vCJD. In addition, health care workers who provide care to
patients with suspected or clinically diagnosed CJD or vCJD should
discuss possible options for autopsy with their local and state health
department and the NPDPSC. Brain tissue specimens obtained by autopsy
from these patients may be submitted to the NPDPSC for further
analysis and confirmation of the CJD diagnosis. The ongoing prion
disease surveillance and diagnostic testing is important for
monitoring the stability of the CJD incidence rates, a!
nd detecting possible occurrences of vCJD and other new prion diseases
in the United States." - Mod.CP]

[5] Prions from recombinant protein
Date: Thu 28 Jan 2010
Source: Genetic Engineering and Biotechnology News [edited]

Scientists have determined how a normal protein can be converted into
a prion, an infectious agent that causes fatal brain diseases in
humans and mammals. The finding, in mice, is expected to advance the
understanding of transmissible spongiform encephalopathies, or TSEs, a
family of neuro-degenerative diseases that include Creutzfeldt-Jakob
Disease (CJD), kuru and fatal familial insomnia in humans, scrapie in
sheep, and bovine spongiform encephalopathy (BSE) in cattle, also
known as "mad cow disease." "This study provides the strongest
evidence yet to prove the prion hypothesis," said Jiyan Ma, associate
professor of molecular and cellular biochemistry at Ohio State
University and senior author of the study. "It also offers important
insights into the molecular mechanism and potential therapeutic
targets for these diseases." The study is in press in the journal
Science and appears online as a Science Express report on 28 Jan 2010
[and a commentary in ScienceNow, see below].

In 1982, the concept of a prion was introduced as an improperly folded
protein that is able to recruit other normal proteins to take on those
same characteristics, leading to widespread damage in the brain.
However, lingering doubt remained among some investigators that a
protein, instead of pathogens like viruses, is actually the infectious
agent for these brain diseases. The skepticism related to
unsatisfactory results of creating an infectious prion with
recombinant prion protein, a protein created artificially in bacterial
cells, which many consider the "holy grail" of the prion field. With
this work, Ma and his colleagues were successful in using recombinant
protein to generate a prion.

Using a recombinant mouse prion protein, known as PrP, the team
discovered that the protein's interaction with lipids, the main
structural component of a cell membrane, leads to its change in
conformation, or misfolding of the protein. The newly formed
recombinant prion made mice sick within 130 days after injection into
the brain, and those brain tissues from the sick mice infected a 2nd
group of mice as well, thus proving the recombinant prion's serial
transmissibility. "The major thing we showed in this study is that the
infectious agent in these diseases is truly a misfolded protein. We
folded recombinant mouse prion protein into its normal shape, then
converted it into a different conformation and showed that when it
infected an animal, it caused full-blown prion disease, with all of
the characteristics," Ma said.

Previous studies have shown that the PrP protein is situated on cell
membranes, [which are] composed primarily of lipids. Because of the
location, the lipids became a target for investigation, Ma said. After
creating [i.e. synthesizing] the recombinant prion protein in
bacterial cells, the team tested various conditions mimicking the
protein's interactions with lipids, introducing additional compounds
that Ma called "helper molecules" that could promote the conversion.
After many attempts, they found the condition that was able to convert
normal recombinant prion protein into an infectious prion, which
requires the presence of lipids and polyanions. They determined that
the converted protein was a prion based on 3 characteristics: The
misfolded prion protein molecules clumped together, resisted the
effects of an enzyme that processes normal prion protein, and
recruited surrounding normal proteins to misfold along with them.

To demonstrate that it was able to cause disease in an animal, the
team injected the recombinant prion into the brains of a group of
normal mice. These mice showed a host of symptoms of TSEs 130 days
after the injection, including clasping of their limbs, rigid tails
and severe weight loss. Most survived only 20 days after symptoms
appeared. The brains of these mice had classic signs of prion disease,
including microscopic holes, called spongiosis, throughout the brain.
Three control samples were used for comparison and did not produce any
clinical symptoms or structural brain changes in mice. Brain tissues
from diseased mice were then injected into the brains of a group of
additional mice to test for transmission of the illness. These mice
also developed prion disease.

This finding should significantly advance prion research, Ma said.
"For example, we still don't know what actually makes prions
infectious or how their propagation causes damage in the brain," he
said. "We can use this in-vitro system to apply to studies of why it
is infectious. We can also use it to develop methods to stop that
infectivity or disrupt the infectious conformation. This information
can be potentially developed as therapeutic strategies against these
fatal diseases."

Co-authors of the work are Fei Wang and Xinhe Wang of Ohio State's
Department of Molecular and Cellular Biochemistry, and Chong-Gang Yuan
of the ECNU School of Life Science.

Communicated by:
ProMED-mail Rapporteur Mary Marshall

[The abstract and reference for the Science paper published online of
28 Jan 2010 described above are reproduced below for the convenience
of readers

Title: Generating a Prion with Bacterially Expressed Recombinant Prion Protein

By: Fei Wang,1,* Xinhe Wang,1,* Chong-Gang Yuan,2 Jiyan Ma1,2

At: 1 Department of Molecular and Cellular Biochemistry, Ohio State
University, Columbus, OH 43210, USA. 2 School of Life Science, East
China Normal University, Shanghai 200062, China.

Abstract: "The prion hypothesis posits that a misfolded form of prion
protein (PrP) is responsible for the infectivity of prion disease.
Using recombinant murine PrP purified from _Escherichia coli_, we
created a recombinant prion with the hallmarks of the pathogenic PrP
isoform: aggregated, protease-resistant, and self-perpetuating. After
intracerebral injection of the recombinant prion, wild-type mice
developed neurological signs in around 130 days and reached the
terminal stage of disease in around 150 days. Characterization of
diseased mice revealed classic neuropathology of prion disease, the
presence of protease-resistant PrP, and the capability of serially
transmitting the disease, confirming that these mice succumbed to
prion disease. Thus, as postulated by the prion hypothesis, the
infectivity in mammalian prion disease results from an altered
conformation of PrP. This research provides an insight into the
conditions required to convert the normal PrP to the pathogenic form."

A commentary by Jennifer Couzin-Frankel, entitled "Prion disease - no
accomplice required" has appeared in ScienceNow at:
which is abbreviated below:

"Jiyan Ma, a biochemist at Ohio State University in Columbus, along
with colleagues there and in China, has solved these 2 problems by
coaxing prions to misfold much like he believes they do naturally.
Instead of misfolding the healthy prion protein, PrP, into amyloid
fibrils, which have been linked to disease, the team combined the PrP
with various blends of lipids, fatty molecules believed to misfold it
in the cell. "This is like cooking," Ma says, getting the right
combination of ingredients. Eventually, Ma's group came up with a
recipe that looked promising and injected it into the brains of 15
normal mice. Within about 130 days, all of the animals developed what
looked like prion disease: their heads twitched, they lost muscle
tissue, and they became lethargic. The animals died several months
later. Control animals injected with a "harmless" solution stayed

To make sure it was prions that were making the mice sick, Ma
performed a series of tests to prove infectious disease. Dissecting
the animals' brains, he and his colleagues extracted tissue and
injected it into the brains of healthy animals. Those animals then
fell ill just like the previous group, and all showed evidence of

This is something "that we and others have been trying to do for some
time," says Claudio Soto, a neuroscientist at the University of Texas
Medical School in Houston. "This is the evidence for the protein only

For those who were already convinced, the paper still "changes the
rules of the game," says Adriano Aguzzi, a neuropathologist at the
University of Zurich in Switzerland. That's because Ma and his
colleagues managed to create large quantities of synthetic prion,
which, Aguzzi believes, will make it possible to study prion structure
in more detail than was previously possible.

But will it convince the skeptics? "On the face of it, it looks like
they've turned tin into gold," says Laura Manuelidis, a
neuropathologist at Yale University who has long doubted that prions
cause disease all by themselves. (She believes that viruses are
involved.) But Manuelidis worries that what Ma claims as a success --
the speed with which the animals got sick -- instead suggests that
something went wrong. She wonders if the animals actually contracted
scrapie, another prion disease, because of lab contamination. Ma
wholeheartedly rejects this possibility: "There's no way" the mice
could have contracted a natural prion disease like scrapie, he says,
because his lab has not worked with naturally occurring prions."

The experiments conducted by Professor Ma's group reinforce the
concept that prions are otherwise normal proteins converted to an
infectious form responsible for neurological diseases in humans and
animals. To some extent, Prof. Ma's work defines the conditions that
convert the normal protein (PrP) into the infectious form. However,
they do not yet shed much light on the greater problem of how the
pathogenic PrP, once formed, converts its normal homologues to the
pathogenic form and is propagated as an infectious agent. - Mod.CP]

[see also:
Prion disease update 2010 20100107.0076
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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