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From: TSS ()
© The Author (2007). Published by Oxford University Press on behalf of the Guarantors of Brain. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org 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: IngaZerr@med.uni-goettingen.de 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. http://brain.oxfordjournals.org/cgi/content/abstract/130/5/1350?maxtoshow=&HITS=10&hits=10&RESULTFORMAT=&fulltext=prion&searchid=1&FIRSTINDEX=0&volume=130&issue=5&resourcetype=HWCIT Copyright © 2006 Elsevier B.V. All rights reserved. Atypical BSE in Germany—Proof of transmissibility and biochemical characterization aFriedrich-Loeffler-Institut (FLI), Institute for Novel and Emerging Infectious Diseases, Boddenblick 5a, 17493 Greifswald, Insel Riems, Germany Received 11 January 2006; revised 23 May 2006; accepted 2 June 2006. Available online 17 August 2006. Abstract Keywords: BSE; Cattle; PrPSc; Biochemical differentiation Subject: BSE in Germany - Update Covering 2006 compared to USA Released: Feb 1 2007 Germany | BSE in Germany - Update Covering 2006 BSE tests cases were confirmed. Of the total, eight cases were discovered through routine testing at slaughter. http://www.fas.usda.gov/gainfiles/200701/146280051.pdf http://www.fas.usda.gov/gainfiles/200606/146198017.pdf GM6004 02/16/2006 Germany plans to adjust BSE testing age to EU level http://www.fas.usda.gov/gainfiles/200602/146176859.pdf GM6003 01/27/2006 BSE in Germany - Update Covering 2005 http://www.fas.usda.gov/gainfiles/200601/146176673.pdf GM3006 02/27/2003 German Cattle Identification and Beef Labeling http://www.fas.usda.gov/gainfiles/200302/145884797.pdf GM1033 11/27/2001 One year after the detection of BSE in Germany (Includes a detailed outline of the German risk management system) http://www.fas.usda.gov/gainfiles/200111/135682795.pdf DID THE U.K. START THE BASE EPIDEMIC AS WELL ??? STRICTLY CONFIDENTIAL http://www.bseinquiry.gov.uk/files/yb/1994/06/15005001.pdf http://www.bseinquiry.gov.uk/files/yb/1994/06/16010001.pdf http://www.bseinquiry.gov.uk/files/yb/1994/06/16012001.pdf http://www.bseinquiry.gov.uk/files/yb/1994/06/20002001.pdf http://www.bseinquiry.gov.uk/files/yb/1994/06/23007001.pdf http://www.bseinquiry.gov.uk/files/yb/1994/07/05005001.pdf 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. http://www.bseinquiry.gov.uk/files/yb/1994/06/29018001.pdf CONFIDENTIAL - POLICY AND COMMERCIAL BSE: LEGAL ACTIONS AGAINST GERMANY http://www.bseinquiry.gov.uk/files/yb/1994/07/20017001.pdf it's o.k. to poison 3rd world countries with BSE http://www.bseinquiry.gov.uk/files/yb/1994/05/20002001.pdf 64. A member noted that at the recent Neuroprion meeting, a study was Other work presented suggested that BSE and bovine amyloidotic spongiform http://www.seac.gov.uk/minutes/95.pdf Models Qingzhong Kong, Ph.D., Assistant Professor, Pathology, Case Western Reserve Bovine Amyloid Spongiform Encephalopathy (BASE) is an atypical BSE strain ***These results indicate that BASE is transmissible to humans and suggest that BASE is more virulent than There is a growing number of human CJD cases, and they were presented last He estimates that it may be up to 14 or 15 persons which display selectively 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 > 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: 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. * These two authors contributed equally to this work. Present address: Medical Biotechnology Center, University of Maryland Biotechnology Institute, Baltimore, MD 21201, USA. http://www.sciencemag.org/cgi/content/full/305/5684/673 An End to the Prion Debate? Don’t Count on It 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 disease. 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 injection. 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 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 ABSTRACT 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 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: stanley@ind.ucsf.edu . © 2005 by The National Academy of Sciences of the USA HUSH UP! GOVERNMENT TOLD GRAN: ''YOU MUST THINK OF THE ECONOMY'' http://www.bseinquiry.gov.uk/files/yb/1994/01/25009001.pdf http://www.bseinquiry.gov.uk/files/yb/1994/01/25010001.pdf Vickey Rimmer, 16, DID NOT DIE FROM nvCJD, she died from a form of sporadic SIMPLY PUT, the ukbsenvcjd only theory was wrong from day one. the elderly Science was dictated by 'big buisness' after the Vickey Rimmer case with the ATYPICAL TSE OF CATTLE AND SHEEP http://www.var.fgov.be/pdf/1100_TSEDAY.pdf AND HUMANS SEE STEADY INCREASE IN SPORADIC CJD IN THE USA FROM There is a growing number of human CJD cases, and they were presented last He estimates that it may be up to 14 or 15 persons which display selectively NOR98 CASE NOW DOCUMENTED IN USA??? ATYPICAL CJD IN HUMANS IN THE USA RISING??? USDA/FDA FAILING TERRIBLY IN SURVEILLANCE AND ERRADICATION??? TRIPLE SSS POLICY ALIVE AND WELL IN THE USA??? CJD SURVEILLANCE TERRIBLY WEAK, with very few questions on route and source being ask?
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