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From: TSS ()
Date: May 1, 2007 at 8:47 am PST

© The Author (2007). Published by Oxford University Press on behalf of the Guarantors of Brain. All rights reserved. For Permissions, please email:

Creutzfeldt–Jakob disease in Germany: a prospective 12-year surveillance
U. Heinemann1, A. Krasnianski1, B. Meissner1, D. Varges1, K. Kallenberg2, W. J. Schulz-Schaeffer3, B. J. Steinhoff4, E. M. Grasbon-Frodl5, H. A. Kretzschmar5 and I. Zerr1
1National TSE Reference Center at Department of Neurology, Georg-August University Göttingen, Germany, 2Department of Neuroradiology, Georg-August University Göttingen, Germany, 3Department of Neuropathology, Georg-August University Göttingen, Germany, 4Epilepsy Center Kork, Diakonie Kork, Germany and 5Department of Neuropathology, Ludwig-Maximilian University Munich, Germany

Correspondence to: Inga Zerr, MD, National Reference Center for TSE, Department of Neurology, Georg-August University Göttingen, Robert-Koch-Strasse 40, 37075 Göttingen, Germany E-mail:

Creutzfeldt–Jakob disease (CJD) is a rare and fatal neurodegenerative disorder with a worldwide incidence of 1–1.5 per million. As in other countries, a CJD surveillance unit with a clinical and neuropathological approach was established in Goettingen (Germany) in 1993. Here we report the epidemiological data from a prospective 12-year surveillance. Since 1993, there has been an increasing incidence of CJD, from 0.7 in 1993 to 1.6 in 2005 with a quite stable level since 1998. During this period, the proportion of patients with MV and VV codon 129 genotype rose, possibly because of better identification of atypical subtypes. Six percent of all patients had a PRNP mutation, mainly D178N-129M (FFI), E200K and V210I. Iatrogenic CJD was a rare phenomenon. No patient infected by cadaveric growth hormone extracts was reported. Furthermore, no variant CJD patient has yet been identified in Germany. Differential diagnoses revealed a variety of neurodegenerative diseases, with Alzheimer's disease in the lead. One-third of the non-CJD patients included in this study suffered from a potentially treatable disorder such as metabolic or inflammatory diseases. The incidence and mortality rates in Germany are similar to those in other European countries. In contrast, however, acquired forms, such as iatrogenic and variant CJD are still rare in Germany or have not yet been identified.

Key Words: CJD; dementia; epidemiology; diagnosis; CSF; MRI; codon 129 genotype; genetic CJD; reversible/treatable dementia

Copyright © 2006 Elsevier B.V. All rights reserved.

Atypical BSE in Germany—Proof of transmissibility and biochemical characterization

A. Buschmanna, A. Gretzschela, A.-G. Biacabeb, K. Schiebelc, C. Coronad, C. Hoffmanna, M. Eidena, T. Baronb, C. Casaloned and Martin H. Groschupa, ,

aFriedrich-Loeffler-Institut (FLI), Institute for Novel and Emerging Infectious Diseases, Boddenblick 5a, 17493 Greifswald, Insel Riems, Germany
bAFSSA-Lyon, Unite ATNC, Lyon, France
cInstitut für Biochemie, Universitity Erlangen-Nürnberg, Germany
dCEA, Instituto Zooprofilattico di Turino, Turin, Italy

Received 11 January 2006; revised 23 May 2006; accepted 2 June 2006. Available online 17 August 2006.

Intensive active surveillance has uncovered two atypical German BSE cases in older cattle which resemble the two different atypical BSE phenotypes that have recently been described in France (designated H-type) and Italy (designated L-type or BASE). The H-type is characterized by a significantly higher molecular size, but a conventional glycopattern of the proteinase K treated abnormal prion protein (PrPSc), while the L-type PrPSc has only a slightly lower molecular size and a distinctly different glycopattern. In this paper we describe the successful transmission of both German atypical BSE cases to transgenic mice overexpressing bovine PrPC. Upon challenge with the L-type, these mice developed BSE after a substantially shorter incubation period than any classical BSE transmission using these mice to date. In contrast, the incubation period was distinctly prolonged when these mice were challenged with the H-type. PrPSc accumulated in the brains of these mice were of the same atypical BSE type that had been used for the transmission. These atypical cases suggest the possible existence of sporadic BSE cases in bovines. It is thus feasible that the BSE epidemic in the UK could have also been initiated by an intraspecies transmission from a sporadic BSE case.

Keywords: BSE; Cattle; PrPSc; Biochemical differentiation

Subject: BSE in Germany - Update Covering 2006 compared to USA
Date: February 1, 2007 at 3:09 pm PST

Released: Feb 1 2007 Germany | BSE in Germany - Update Covering 2006
GM7004 Highlight: In 2006, 16 cases of BSE were confirmed in Germany, compared to 32 in 2005. This brings the total number of BSE cases to 405, since it was first detected in Germany in November 2000. In June 2006, Germany abolished its stricter BSE testing requirements and replaced it with the standard EU testing regime. Beef consumption is still below the pre-BSE level, primarily because of healthier consumer eating habits rather than fears of BSE.


BSE tests

In 2006, a total of 1,888,053 animals were tested for BSE in Germany, of which 16 BSE

cases were confirmed. Of the total, eight cases were discovered through routine testing at


GM6020 06/19/2006 Germany Raises BSE Testing Age to EU Level

GM6004 02/16/2006 Germany plans to adjust BSE testing age to EU level

GM6003 01/27/2006 BSE in Germany - Update Covering 2005

GM3006 02/27/2003 German Cattle Identification and Beef Labeling

GM1033 11/27/2001 One year after the detection of BSE in Germany

(Includes a detailed outline of the German risk management




e) one way for the industry to take the damages action would be for it to send a consignment of beef to Germany after the regulation came into affect, and to have it turned back at the German border.



it's o.k. to poison 3rd world countries with BSE

18 January 2007 - Draft minutes of the SEAC 95 meeting (426 KB) held on 7
December 2006 are now available.


64. A member noted that at the recent Neuroprion meeting, a study was
presented showing that in transgenic mice BSE passaged in sheep may be more
virulent and infectious to a wider range of species than bovine derived BSE.

Other work presented suggested that BSE and bovine amyloidotic spongiform
encephalopathy (BASE) MAY BE RELATED. A mutation had been identified in the


3:30 Transmission of the Italian Atypical BSE (BASE) in Humanized Mouse

Models Qingzhong Kong, Ph.D., Assistant Professor, Pathology, Case Western Reserve

Bovine Amyloid Spongiform Encephalopathy (BASE) is an atypical BSE strain
discovered recently in Italy, and similar or different atypical BSE cases
were also reported in other countries. The infectivity and phenotypes of
these atypical BSE strains in humans are unknown. In collaboration with
Pierluigi Gambetti, as well as Maria Caramelli and her co-workers, we have
inoculated transgenic mice expressing human prion protein with brain
homogenates from BASE or BSE infected cattle. Our data shows that about half
of the BASE-inoculated mice became infected with an average incubation time
of about 19 months; in contrast, none of the BSE-inoculated mice appear to
be infected after more than 2 years.

***These results indicate that BASE is transmissible to humans and suggest that BASE is more virulent than
classical BSE in humans.***

6:30 Close of Day One

1997 TO 2006. SPORADIC CJD CASES TRIPLED, with phenotype
of 'UNKNOWN' strain growing. ...

There is a growing number of human CJD cases, and they were presented last
week in San Francisco by Luigi Gambatti(?) from his CJD surveillance

He estimates that it may be up to 14 or 15 persons which display selectively
SPRPSC and practically no detected RPRPSC proteins.

THE myth of atypical BSE i.e. BASE or any other strain of TSE being that of a spontaneous event, is nothing more than wishful thinking, with absolutely no science to back it up. THE most plausible route of exposure and transmission are through tainted feed with atypical MBM, unless of course they had been segregating the different mbm i.e. bse from the base all along. WE all know this did not take place, they have been feeding now only BSE tainted feed over the years, but atypical BSE i.e. BASE as well. ALSO, vertical and or lateral exposure and transmission has not been ruled in or out with these new phenotypes to date. TO claim that only BSE can transmit orally and the BASE cannot, without any sort of transmission studies, is like believing in the ukbsenvcjd only theory. it just aint so. ...TSS

Subject: Atypical BSE in Germany—Proof of transmissibility and biochemical characterization
Date: August 20, 2006 at 3:33 pm PST

> These atypical cases suggest the possible existence of sporadic BSE cases in bovines. It is thus

> feasible that the BSE epidemic in the UK could have also been initiated by an intraspecies

> transmission from a sporadic BSE case.

OVER 20 strains of typical scrapie documented, who knows how many atypical strains, all rendered and fed back to other species for human and animal consumption for decades, yet they wish us to believe the one strain only theory in the bovine and human i.e. BSE to nvCJD, and then want us to believe in magic i.e. the spontaneous myth with all other TSE in the bovine to human? IF atypical BSE i.e. BASE is so similar to some sporadic CJD's, then how in the hell did they all of a sudden become spontaneous? could it not be so simple as an atypical BSE i.e. BASE was transmitted the same way most of all of the other BSE cattle were i.e. feed of just an atypical source? why would these animals not develop an atypical BSE i.e. BASE from the same oral route? and or possibly even some lateral/horizontal transmission. However, the spontaneous TSE theory in any species in the field has never been proven. The in vitro BSE/TSE that Soto and Prusiner claim to have developed looks like no other natural field TSE ever seen before, and as the infectious aspect of the study is questionable to say the least. Also, please explain to me how a distinct synthetic prion, of a strain that is supposedly unlike any other we have ever seen, how can this explain 6 different documented phenotypes of sporadic CJD to date? OR, if you render an atypical TSE of what ever phenotype, in what ever species, of the atypical strain and feed it to another whatever species, nothing happens right x 1 x 2 x 3 x 4 etc passage? This has been proven, correct? please show me these transmission studies? ALL other TSE only happens spontaneously, right? NOT in my wildest dreams. but what a dream it is to wish something away with junk science. odd, how the USDA et al never really believed in this spontaneous theory for some time, and now it's gone International, along with the OIEs GW BSE MRR policy, the legal trading of all strains of all TSE. Literally thousands and thousands of TONS of potential mad cow protein IN COMMERCE STILL IN THE USA, and what about that BSE MRR policy and all the supposedly BSE FREE products in the USA that is going to other Countries??? ITs like the last 30 years of the attempt to eradicate this disease globally went down the tubes over night. Good luck Switzerland, you better seal your borders and keep them that way. ...TSS

Science 30 July 2004:
Vol. 305. no. 5684, pp. 673 - 676
DOI: 10.1126/science.1100195

Synthetic Mammalian Prions
Giuseppe Legname,1,2* Ilia V. Baskakov,1,2* Hoang-Oanh B. Nguyen,1 Detlev Riesner,6 Fred E. Cohen,1,3,4 Stephen J. DeArmond,1,5 Stanley B. Prusiner1,2,4

Recombinant mouse prion protein (recMoPrP) produced in Escherichia coli was polymerized into amyloid fibrils that represent a subset of ß sheet–rich structures. Fibrils consisting of recMoPrP(89–230) were inoculated intracerebrally into transgenic (Tg) mice expressing MoPrP(89–231). The mice developed neurologic dysfunction between 380 and 660 days after inoculation. Brain extracts showed protease-resistant PrP by Western blotting; these extracts transmitted disease to wild-type FVB mice and Tg mice overexpressing PrP, with incubation times of 150 and 90 days, respectively. Neuropathological findings suggest that a novel prion strain was created. Our results provide compelling evidence that prions are infectious proteins.

1 Institute for Neurodegenerative Diseases, University of California, San Francisco, CA 94143, USA.
2 Department of Neurology, University of California, San Francisco, CA 94143, USA.
3 Department of Cellular and Molecular Pharmacology, University of California, San Francisco, CA 94143, USA.
4 Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA.
5 Department of Pathology, University of California, San Francisco, CA 94143, USA.
6 Institut für Physikalische Biologie, Heinrich-Heine-Universität, 40225 Düsseldorf, Germany.

* These two authors contributed equally to this work.

Present address: Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD 21201, USA.

To whom correspondence should be addressed. E-mail:

An End to the Prion Debate?

Don’t Count on It

A bold set of prion experiments in mice

may have proven that the misshapen proteins

are, by themselves, infectious. If the

work holds up, it will be a watershed in

prion biology, validating the belief that

these proteins alone are the culprits in

“mad cow disease” and similar illnesses.

As is typical for the controversy-laden

field, however, many scientists express reservations

about the study on page 673. It was

led by Stanley Prusiner of the University of

California, San Francisco, who won the

Nobel Prize in 1997 for discovering prions.

“It’s really a striking result that seems to

fill in one more piece of the infectivity puzzle,”

says Byron Caughey, a biochemist at

the National Institutes of Health’s Rocky

Mountain Laboratories in Hamilton, Montana.

“But,” he adds, “it’s worth pointing out

some significant caveats.”

For years, biologists have tried to prove

that a protein called PrP can misfold and

become an infectious prion by purifying

protein clumps from diseased brains and

injecting them into healthy animals. But it

hasn’t been clear that PrP alone was what

was being injected; using synthetic misfolded

PrP, meanwhile, hasn’t reliably triggered


In their tests, Prusiner and colleagues used

transgenic mice making 16 times the normal

amount of PrP. These mice express a truncated

PrP that may more readily make up prion

clumps. This, the group reasoned, might sensitize

the animals to introduced PrP.

To obtain PrP free of brain tissue, Prusiner’s

team genetically altered Escherichia coli

bacteria into producing PrP fragments that

they misfolded to form amyloid fibrils, which

have been implicated in various brain diseases.

Prusiner’s team injected those prion

fibrils into the brains of the mice.

Almost a year later, with no animals

sick, the researchers were ready to declare

the study a failure. But then, 380 days after

being inoculated, one of the mice showed

symptoms of a prionlike disease. Eventually,

all seven inoculated mice showed neurological

disease, the last one 660 days after


Prusiner’s team also inoculated a batch of

normal animals with brain tissue from one of

the sick ones. These rodents took about 150

days to sicken.

“It is a spectacular breakthrough,” says

Neil Cashman, a neuroscientist at the University

of Toronto. “This is the beginning

of the end of all the objections about the

prion hypothesis.”

Not so fast, say some experts. Do

Prusiner’s mice with excess PrP get sick normally?

wonders John Collinge, director of

the Medical Research Council Prion Unit at

University College London. His team had

relied on rodents with 10 times the normal

level of PrP but abandoned them after finding

prion disease–like pathology in animals

that hadn’t been inoculated with anything.

Prusiner’s mice, says Collinge, may be

“poised” to become infectious even without

the inoculation; giving them a shot of synthetic,

misfolded PrP may push them over

the edge, but so might other stresses.

The long latency time between inoculation

and disease also worries prion experts.

Some wonder if the experiments were contaminated

by other prion strains in the lab.

Yale University neuropathologist Laura

Manuelidis, who has long criticized the prion

hypothesis, says the brain samples from

some of Prusiner’s mice resemble RML

scrapie, a common strain. Prusiner counters

that with contamination, the control animals

inoculated with saline should have gotten

sick as well.

Another explanation for long latency is

that infecting animals with synthetic PrP is

inefficient. The first inoculations may have

contained few prions, says Prusiner. This

might also explain why no one has yet accomplished

the gold-standard experiment:

infecting normal mice, not transgenic ones,

with pure prion proteins. Until then, one of

biomedicine’s longest-running controversies

is likely to continue. –JENNIFER COUZIN

Journal of Virology, July 2003, p. 7611-7622, Vol. 77, No. 13
0022-538X/03/$08.00+0 DOI: 10.1128/JVI.77.13.7611-7622.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

Molecular Distinction between Pathogenic and Infectious Properties of the Prion Protein
Roberto Chiesa,1,2 Pedro Piccardo,3 Elena Quaglio,1, Bettina Drisaldi,1, San Ling Si-Hoe,1 Masaki Takao,3, Bernardino Ghetti,3 and David A. Harris1*

Department of Cell Biology and Physiology, Washington University School of Medicine, St. Louis, Missouri 63110,1 Dulbecco Telethon Institute and Department of Neuroscience, Istituto di Ricerche Farmacologiche "Mario Negri," Milan 20157, Italy,2 Division of Neuropathology, Indiana University School of Medicine, Indianapolis, Indiana 462023

Received 8 January 2003/ Accepted 2 April 2003


Tg(PG14) mice express a prion protein (PrP) with a nine-octapeptide insertion associated with a human familial prion disease. These animals spontaneously develop a fatal neurodegenerative disorder characterized by ataxia, neuronal apoptosis, and accumulation in the brain of an aggregated and weakly protease-resistant form of mutant PrP (designated PG14spon). Brain homogenates from Tg(PG14) mice fail to transmit disease after intracerebral inoculation into recipient mice, indicating that PG14spon, although pathogenic, is distinct from PrPSc, the infectious form of PrP. In contrast, inoculation of Tg(PG14) mice with exogenous prions of the RML strain induces accumulation of PG14RML, a PrPSc form of the mutant protein that is infectious and highly protease resistant. Like PrPSc, both PG14spon and PG14RML display conformationally masked epitopes in the central and octapeptide repeat regions. However, these two forms differ profoundly in their oligomeric states, with PG14RML aggregates being much larger and more resistant to dissociation. Our analysis provides new molecular insight into an emerging puzzle in prion biology, the discrepancy between the infectious and neurotoxic properties of PrP.

Strain-specified characteristics of mouse synthetic prions

Giuseppe Legname *, , Hoang-Oanh B. Nguyen *, Ilia V. Baskakov * , Fred E. Cohen *, ¶, ||, Stephen J. DeArmond * , **, and Stanley B. Prusiner *, , ||,

*Institute for Neurodegenerative Diseases and Departments of Neurology, ¶Cellular and Molecular Pharmacology, ||Biochemistry and Biophysics, and **Pathology, University of California, San Francisco, CA 94143

Contributed by Stanley B. Prusiner, December 6, 2004

Synthetic prions were produced in our laboratory by using recombinant mouse prion protein (MoPrP) composed of residues 89-230. The first mouse synthetic prion strain (MoSP1) was inoculated into transgenic (Tg) 9949 mice expressing N-terminally truncated MoPrP(23-88) and WT FVB mice expressing full-length MoPrP. On first and second passage in Tg9949 mice, MoSP1 prions caused disease in 516 ± 27 and 258 ± 25 days, respectively; numerous, large vacuoles were found in the brainstem and gray matter of the cerebellum. MoSP1 prions passaged in Tg9949 mice were inoculated into FVB mice; on first and second passage, the FVB mice exhibited incubation times of 154 ± 4 and 130 ± 3 days, respectively. In FVB mice, vacuolation was less intense but more widely distributed, with numerous lesions in the hippocampus and cerebellar white matter. This constellation of widespread neuropatho-logic changes was similar to that found in FVB mice inoculated with Rocky Mountain Laboratory (RML) prions, a strain derived from a sheep with scrapie. Conformational stability studies showed that the half-maximal GdnHCl (Gdn1/2) concentration for denaturation of MoSP1 prions passaged in Tg9949 mice was 4.2 M; passage in FVB mice reduced the Gdn1/2 value to 1.7 M. RML prions passaged in either Tg9949 or FVB mice exhibited Gdn1/2 values of 1.8 M. The incubation times, neuropathological lesion profiles, and Gdn1/2 values indicate that MoSP1 prions differ from RML and many other prion strains derived from sheep with scrapie and cattle with bovine spongiform encephalopathy.



Author contributions: G.L., I.V.B., F.E.C., and S.B.P. designed research; H.-O.B.N. and S.J.D. performed research; G.L., S.J.D., and S.B.P. analyzed data; S.B.P. contributed new reagents/analytic tools; and G.L., S.J.D., and S.B.P. wrote the paper.

Abbreviations: PrP, prion protein; MoPrP, mouse PrP; PrPSc, disease-causing isoform of PrP; MoSP1, mouse synthetic prion1; rec, recombinant; Tg, transgenic; RML, Rocky Mountain Laboratory; Gdn1/2, half-maximal GdnHCl; HuM, human-mouse; PK, proteinase K.

G.L., S.J.D., and S.B.P. have a financial interest in InPro Biotechnology, Inc.

Present address: Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD 21201.

To whom correspondence should be addressed. E-mail: .

© 2005 by The National Academy of Sciences of the USA



Vickey Rimmer, 16, DID NOT DIE FROM nvCJD, she died from a form of sporadic
CJD, whatever the hell that is.
and there have been 16 year old die from sporadic CJD in the USA as well.

SIMPLY PUT, the ukbsenvcjd only theory was wrong from day one. the elderly
are expendable, pets and kids are not.

Science was dictated by 'big buisness' after the Vickey Rimmer case with the
ukbsenvcjd only myth.



1997 TO 2006. SPORADIC CJD CASES TRIPLED, with phenotype
of 'UNKNOWN' strain growing. ...

There is a growing number of human CJD cases, and they were presented last
week in San Francisco by Luigi Gambatti(?) from his CJD surveillance

He estimates that it may be up to 14 or 15 persons which display selectively
SPRPSC and practically no detected RPRPSC proteins.






CJD SURVEILLANCE TERRIBLY WEAK, with very few questions on route and source being ask?

to be continued....


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