Sunday, June 29, 2008

South Korea bans rallies against US beef imports

June 29, 2008, 1:07PM South Korea bans rallies against US beef imports

By HYUNG-JIN KIM Associated Press Writer © 2008 The Associated Press

SEOUL, South Korea — South Korean police refused Sunday to allow more candlelight protests against the resumption of American beef imports, just hours after thousands of demonstrators clashed with riot police in the streets of the capital.

The government said it would not tolerate violent, illegal rallies. Authorities used police buses to encircle a plaza in front of Seoul City Hall — the main site for weeks of evening rallies — to prevent protesters from gathering.

Nevertheless, about 1,700 people marched into nearby downtown streets chanting slogans demanding the government of President Lee Myung-bak cancel its decision to lift a ban on U.S. beef.

Thousands of riot police quickly chased them away. There were no immediate reports of serious injuries or clashes.

Jang Dae-hyun, a spokesman for the protest group, said police should cease harsh methods against demonstrators to prevent further violence. "We've been supporting peaceful rallies, but the police crackdown is too harsh," Jang said.

The hard-line stance came hours after about 15,000 people — some wielding steel pipes and hurling stones at police — demonstrated in the capital, leaving more than 200 protesters and riot police injured.

The rally turned violent after some protesters used ropes to try to drag away police buses used as barricades to prevent them from marching into the presidential Blue House.

Riot police immediately fired water cannons and sprayed fire extinguishers to repel them. Angry protesters attacked police, while police used clubs and shields against the crowd.

Rallies after sunset without police permission are officially illegal. Activists have nonetheless staged daily candlelight rallies to voice fears about the possible health risks of U.S. beef, such as mad cow disease.

Justice Minister Kim Kyung-han said authorities may have no choice but to use measures such as tear gas to prevent clashes between police and protesters. Tear gas has been banned since 1999.

He also said authorities would arrest those who instigate violent protests, which he said would aggravate national economic difficulties amid rising global oil prices.

As officials began inspecting U.S. beef Friday before it can reach markets, hundreds of labor activists blocked customs storage facilities.

"We are just here to express our opinions. I can't understand why this government tries to ban our rally," said Kim In-seok, 69, who runs a small construction company in Seoul. "Lee Myung-bak will face a serious public backlash."

U.S. beef has been banned for most of the time since late 2003, when the first case of mad cow disease in the U.S. was discovered.

In the wake of public outrage over plans to resume shipments of American beef, the South Korean Cabinet offered to resign and the president reshuffled top advisers.

Earlier rallies opposing the beef import deal drew up to 80,000 people, but have since dwindled.

This is very sad to see the Korean Government turn to violence against peaceful protesters. A true sign that shows the protesters are winning their fight. The Honorable people of Korea should be proud of these brave peaceful protesters. However, i am saddened that people are becoming hurt and injured fighting for the truth. there are other ways, just refuse to buy the stuff. let it rot, until they test it all, of all age groups, until the fda stops allowing loop holes in the feed ban, until the USDA fixes the failed BSE surveillance system, all livestock producing animals, must be tested for TSE. THE USDAs and the OIEs BSE MRR policy must be repealed, it was nothing more than a 'get out of jail free card' for the legal exporting of all strains of Transmissible Spongiform Encephalopathy globally. ...TSS

sad. they are wanting to throw the wrong people in jail. they should jail all the USA and Korean politicians that are lying about mad cow disease and the UKBSEnvCJD only theory. this is wrong, and both governments know this. the last two mad cow cases in the USA in Texas and Alabama were NOT UK BSE, but they were both atypical BSE, which is more virulent to humans than UK BSE. CJD is rising in the USA, with 'UNKNOWN PHENOTYPES' IN YOUNG AND OLD!

South Korea ... whom PD Diary portrayed as having probably died of variant Creutzfeldt-Jakob disease (vCJD), the human form of mad cow disease, there is a moment when ... See all stories on this topic


Portsmouth woman may have human form of Mad Cow Disease

06:38 PM EDT on Monday, April 7, 2008

Reported by: Wayne Carter PORTSMOUTH, Va. --

A 22-year-old Portsmouth woman is close to dying, and family says doctors believe the human equivalent of Mad Cow Disease could be the reason.

Creutzfeldt-Jakob Disease , or CJD, is so rare that there has only been one other possible case ever in the United States.

The Portsmouth Health Department is looking into the case because the variant form of the disease comes from eating infected meat, and Aretha Vincent's family says she's never left the United States.

please see full text ;

NOW, for the rest of the story. ...

Texas Firm Recalls Cattle Heads That Contain Prohibited Materials


Congressional and Public Affairs (202) 720-9113 Peggy Riek

WASHINGTON, June 26, 2008 - Beltex Corporation, doing business as Frontier Meats, a Fort Worth, Texas, establishment, is recalling approximately 2,850 pounds of fresh cattle heads which may contain specified risk materials (SRMs), the U.S. Department of Agriculture's Food Safety and Inspection Service announced today.

SRMs are tissues that are known to contain the infective agent in cattle infected with BSE, as well as materials that are closely associated with these potentially infective tissues. Therefore, FSIS prohibits SRMs from use as human food to minimize potential human exposure to the BSE agent.

The products subject to recall include: Cases of "BEEF WHOLE HEAD." Each shipping package bears the establishment number "EST. 7041B" inside the USDA mark of inspection, as well as a package code of "51904" or "63922."

The company is recalling all products packed between May 31, 2007, and June 24, 2008. These products were distributed to retail establishments and lunch carts in the Dallas-Ft. Worth, Texas, area.

The problem was discovered by the State of Texas officials during a routine inspection at a retail establishment.

Media and consumers with questions about the recall should contact the company Sales Department at (817) 624-1136.

Consumers with food safety questions can "Ask Karen," the FSIS virtual representative available 24 hours a day at The toll-free USDA Meat and Poultry Hotline 1-888-MPHotline (1-888-674-6854) is available in English and Spanish and can be reached from l0 a.m. to 4 p.m. (Eastern Time) Monday through Friday. Recorded food safety messages are available 24 hours a day.


Thursday, June 26, 2008

Texas Firm Recalls Cattle Heads That Contain Prohibited Materials

Tuesday, May 27, 2008

FDA BSE/Ruminant Feed Inspections Firms Inventory Report Texas Legend Ranch OAI 05/10/2008

In 2007, in one weekly enforcement report, the fda recalled 10,000,000+ pounds of BANNED MAD COW FEED, 'in commerce', and i can tell you that most of it was fed out ;


Date: March 21, 2007 at 2:27 pm PST REASON Blood meal used to make cattle feed was recalled because it was cross-contaminated with prohibited bovine meat and bone meal that had been manufactured on common equipment and labeling did not bear cautionary BSE statement. VOLUME OF PRODUCT IN COMMERCE 42,090 lbs. DISTRIBUTION WI

REASON Products manufactured from bulk feed containing blood meal that was cross contaminated with prohibited meat and bone meal and the labeling did not bear cautionary BSE statement. VOLUME OF PRODUCT IN COMMERCE 9,997,976 lbs. DISTRIBUTION ID and NV


Subject: MAD COW FEED RECALL USA SEPT 6, 2006 1961.72 TONS IN COMMERCE AL, TN, AND WV Date: September 6, 2006 at 7:58 am PST

snip... see listings and references of enormous amounts of banned mad cow protein 'in commerce' in 2006 and 2005 ;

see full text ;

Friday, April 25, 2008

Substances Prohibited From Use in Animal Food or Feed [Docket No. 2002N-0273] (Formerly Docket No. 02N-0273) RIN 0910-AF46



Thursday, June 26, 2008

Texas Firm Recalls Cattle Heads That Contain Prohibited Materials


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

Please remember, the last two mad cows documented in the USA i.e. Alabama and Texas, both were of the 'atypical' BSE strain, and immediately after that, the USDA shut down the testing from 470,000 to 40,000 in the U.S. in 2007 out of about 35 million cattle slaughtered. also, science is showing that some of these atypical cases are more virulent to humans than the typical UK BSE strain ;

***Atypical forms of BSE have emerged which, although rare, appear to be more virulent than the classical BSE that causes vCJD.***

Progress Report from the National Prion Disease Pathology Surveillance Center

An Update from Stephen M. Sergay, MB, BCh & Pierluigi Gambetti, MD

April 3, 2008

In this context, a word is in order about the US testing program. After the discovery of the first (imported) cow in 2003, the magnitude of testing was much increased, reaching a level of >400,000 tests in 2005 (Figure 4). Neither of the 2 more recently indigenously infected older animals with nonspecific clinical features would have been detected without such testing, and neither would have been identified as atypical without confirmatory Western blots. Despite these facts, surveillance has now been decimated to 40,000 annual tests (USDA news release no. 0255.06, July 20, 2006) and invites the accusation that the United States will never know the true status of its involvement with BSE.

In short, a great deal of further work will need to be done before the phenotypic features and prevalence of atypical BSE are understood. More than a single strain may have been present from the beginning of the epidemic, but this possibility has been overlooked by virtue of the absence of widespread Western blot confirmatory testing of positive screening test results; or these new phenotypes may be found, at least in part, to result from infections at an older age by a typical BSE agent, rather than neonatal infections with new "strains" of BSE. Neither alternative has yet been investigated.

IF BSE is not in the USA (just not documented for many different reasons), and only atypical BSE is in the USA (plus CWD, plus, many strains of Scrapie, and Now the Nor-98 documented in 5 different states, plus TME, then why would human mad cow in the USA look like the UK nvCJD from UK BSE cows ? it was shown long ago in studies at Mission Texas that experimental transmission of USA Scrapie to USA Bovine, DID NOT LOOK LIKE UK BSE. so again, in short, why would human mad cow in the USA look like human mad cow in the UK i.e. the (nvCJD). however, I believe that BSE has been in the USA untested and undocumented for years. why on earth then does the USDA refuse to allow creekstone or anyone else test their product? simple, if you don't look/test, you don't find.


please see full text ;

A novel human disease with abnormal prion protein sensitive to protease (prionopathy)

HUMAN and ANIMAL TSE Classifications i.e. mad cow disease and the UKBSEnvCJD only theory JUNE 2008

Over the next 8-10 weeks, approximately 40% of all the adult mink on the farm died from TME. Since previous incidences of TME were associated with common or shared feeding practices, we obtained a careful history of feed ingredients used over the past 12-18 months. The rancher was a "dead stock" feeder using mostly (>95%) downer or dead dairy cattle and a few horses. Sheep had never been fed.

please note, dead stock downer cattle i.e. non-ambulatory, are the most likely to have mad cow disease.


What GAO Found

April 17, 2008


Public Reporting on Violations Can Identify Enforcement Challenges and Enhance Transparency

In January 2004, GAO reported that incomplete and inconsistent inspection records made it difficult to determine the frequency and scope of HMSA violations, inspectors did not always document violations of the act, and they did not consistently document the scope and severity of each incident. GAO also reported that enforcement actions to address noncompliance with the act were inconsistent, and that USDA was not using consistent criteria to determine when to suspend plant operations in cases of serious or repeated violations. The Congress has urged USDA to report annually on trends in compliance with humane slaughter methods. Such public reporting can enhance transparency, but USDA’s most recent report was in March 2003 and relied on incomplete data. For example, that report said very few infractions were for inhumane treatment, but GAO found that at least one-fourth of the infractions were for ineffective stunning which fails to meet humane standards. USDA has taken actions to address the recommendations GAO made in 2004 about oversight of HMSA. However, GAO has not evaluated the effectiveness of these actions. USDA faces resource challenges that may make it difficult for it to enforce HMSA and ensure the safety of the food supply. Although USDA’s budget for food safety-related activities has increased since 1988, staffing for these activities has declined from its highest level in 1995. Agency officials noted the overall decline is due, in part, to consolidation in the meat industry, resulting in fewer facilities. In 2004, GAO found that USDA lacked detailed information on how much time its inspectors spend on humane handling and slaughter activities, making it difficult to determine if the number of inspectors is adequate. USDA has taken actions to address most of GAO’s recommendationsfor assessing its resource needs for HMSA, but GAO has not evaluated these actions. Although not directly related to HMSA activities, the quantity of meat and poultry inspected and passed by USDA has grown, and the quantity of meat and poultry recalled has increased. USDA has oversight responsibility for ensuring the safety of meat, poultry, and processed eggs. For example, federal regulations prohibit companies from processing and selling meat from disabled cows—which have a higher probability of being infected with bovine spongiform encephalopathy—without explicit USDA inspector approval. However, USDA is only 1 of 15 agencies that collectively administer at least 30 laws related to food safety. This fragmentation is the key reason GAO added the federal oversight of food safety to its High-Risk Series in 2007 and called for a governmentwide reexamination of the food safety system. GAO has reported on problems with this system—including inconsistent oversight, ineffective coordination, and inefficient use of resources. Going forward, as GAO has recommended, a governmentwide, results-oriented performance plan and a reconvened President’s Council on Food Safety could build a sustained focus on the safety of the nation’s food supply.
Note: Data for 2008 are estimated. Although the number of recalls has declined in recent years, the quantity of meat and poultry recalled has increased sharply. Meat and poultry product recalls declined from 125 in 2002 to 58 in 2007. However, 2 of the 6 biggest meat recalls in U.S. history have occurred in the past 6 months. In October 2007, Topps Meat Company LLC announced the recall of 22 million pounds of ground beef used for frozen hamburgers due to E. coli contamination. At the time, the Topps recall was the fifth largest in U.S. history. The E. coli-contaminated meat sickened at least 32 people in eight states. On February 17, 2008, Westland/Hallmark Meat Company announced the recall of more than 143 million pounds of beef, the largest recall in U.S. history. The quantity of meat and poultry recalled has increased from 5 million pounds in 1994, the first year for which data were readily available, to 145 million in just the first quarter of March 2008.

see full text 18 pages ;

Thu Dec 6, 2007 11:38


[Docket No. 03-025IFA] FSIS Prohibition of the Use of Specified Risk Materials for Human Food and Requirement for the Disposition of Non-Ambulatory Disabled Cattle 9/13/2005

3. Prof. A. Robertson gave a brief account of BSE. The US approach was to accord it a _very low profile indeed_. Dr. A Thiermann showed the picture in the ''Independent'' with cattle being incinerated and thought this was a fanatical incident to be _avoided_ in the US _at all costs_ $

Attachment to Singeltary comment
January 28, 2007

Greetings APHIS,

I would kindly like to submit the following to ;

[Federal Register: January 9, 2007 (Volume 72, Number 5)] [Proposed Rules] [Page 1101-1129] From the Federal Register Online via GPO Access [] [DOCID:fr09ja07-21]


[Docket No. FSIS-2006-0011] FSIS Harvard Risk Assessment of Bovine Spongiform Encephalopathy (BSE)

APHIS-2006-0041-0006 TSE advisory committee for the meeting December 15, 2006

U.S. slams door on revising S. Korea beef import pact

June 11, 2008, 10:14PM

Wednesday, June 11, 2008

OIE Recognition of the BSE Status of Members RESOLUTION No. XXI (Adopted by the International Committee of the OIE on 27 May 2008)

Saturday, June 7, 2008

Export Requirements for the Republic of Korea IMPORT HEALTH REQUIREMENTS FOR U.S. BEEF AND BEEF PRODUCTS

Why Americans, As Well as Koreans, Should Be Worried About Mad Cow Tainted USA Beef

By Terry S. Singeltary Sr. May 15, 2008

Straight to the Source

Web Note: This is an important commentary by Terry S. Singeltary Sr., on a recent Business Week story on the controversy in South Korea over their government's lifting on the ban on conventional (non-organic) beef, despite the fact that the USDA is still allowing slaughterhouse waste and blood and manure to be fed to cows, and refusing to test all cows at slaughter. See the Mad Cow section of the OCA website for in-depth information. Terry is a regular blogger on the OCA website on Mad Cow issues.

Ronnie Cummins

One Korean official says the probability of a human being catching a mad cow disease by eating U.S. beef is like the one of a golf player scoring a hole-in-one and then being killed by lightning.

this is typical BSe. you here industry groups comment 'your more likely to get hit by a car than die from CJD'. well, maybe so, but my mother and many more did not die from getting hit by a car, they died from CJD, my mothers being the hvCJD (confirmed), and my neighbors mother died from CJD (confirmed). the UKBSEnvCJD _only_ theory is incorrect. there are more strains of mad cow than the UK BSE in beef to nvCJD in humans in the UK. The deception by the USDA, FDA, and the Bush administration about mad cow disease, CJD, and all Transmissible Spongiform Encephalopathy over the past 8 years have been outrageous, to a point of being criminal. I am vested in nothing, but the truth.

snip...see full text ;

Tuesday, May 13, 2008

Concerned Americans against Mad Cow Disease STATEMENT OF SOLIDARITY with Koreans May 13, 2008


Friday, June 20, 2008


Wednesday, June 11, 2008

OIE Recognition of the BSE Status of Members RESOLUTION No. XXI (Adopted by the International Committee of the OIE on 27 May 2008)


U.S. slams door on revising S. Korea beef import pact

June 11, 2008, 10:14PM

Saturday, June 7, 2008

Export Requirements for the Republic of Korea IMPORT HEALTH REQUIREMENTS FOR U.S. BEEF AND BEEF PRODUCTS

Monday, June 23, 2008


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


8. Human susceptibility to CWD

Millions of North Americans hunt deer and elk (U.S. Department of the Interior, Census Bureau), and there is no doubt that people have been exposed to CWD through venison consumption, particularly in light of recent data showing CWD prions in muscle [2]. Human susceptibility to CWD or to other newly emerging animal TSE [9, 14] is still unclear, although we can be somewhat reassured in that there have been no large scale outbreaks of human TSE cases in Colorado and Wyoming, where CWD has existed for decades [51]. Up until approximately 10 years ago, autopsies were not performed on suspect human TSE cases in many states due to biosafety concerns, therefore the diagnosis of potential new TSE strains has been hampered. This indicates that clinical TSE diagnoses in humans were not confirmed, nor was any strain typing done to look for the appearance of potentially subtle or unusual pathological or biochemical phenotypes of a new TSE strain. Fortunately, the autopsy rate for suspect cases is improving. At the National Prion Disease Pathology Surveillance Center at Case Western Reserve University (Cleveland, Ohio), Creutzfeldt-Jakob disease (CJD) suspect cases are studied and classified by CJD subtype. Thus far,


*** twenty-seven CJD patients who regularly consumed venison were reported to the Surveillance Center***,

however there have been no unusual or novel prion subtypes that might indicate the appearance of a new prion strain [7, 41]. Other indirect studies of human susceptibility to CWD also suggest that the risk is low. In biochemical conversion studies, Raymond et al. [68] showed that the efficiency of CWD to convert recombinant human PrP into amyloid fibrils was low, but similar to that of both BSE and scrapie fibrils to do the same. These results suggest that there is a molecular incompatibility in the conversion of human PrPC by CWD, sheep scrapie, or BSE, and that cross species infections in humans may be rare events. To determine whether common PrPSc strain features may link CWD and CJD, histopathology and the PrPSc biochemical characteristics from deer and elk were compared with that of humans with sporadic CJD (sCJD) cases that are methionine homozygous at codon 129 of the Prnp gene by Xie et al. [96], although strain features including histologic profile, target organs, and glycoform patterns will not necessarily remain the same upon crossing species barriers [6, 5, 8, 57]. The PrPSc form is cleaved by proteinase-K (PK) at different sites depending on the conformation of the protein and may aid determination of whether the PrPSc conformation is similar. By western blot (SDS-PAGE) of elk CWD, the unglycosylated PK-resistant PrPSc migrated at 21 kDa, similar to sCJD (MM1 subtype) and the PK cleavage site was the same, occurring at residues 78 and 82 as assessed by N-terminal sequencing. Conformational stability was evaluated by measuring the PrPSc stability under partially denaturing conditions and also showed no significant difference between elk CWD and sCJD MM1 PrPSc. However, elk CWD and human sCJD MM1 strains exhibited distinct glycoform patterns by two dimensional gel electrophoresis, suggesting that the strains differed. Future studies may utilize luminescent conjugated polymers, which were recently shown to distinguish naturally- and experimentally-derived prion strains [79]. To study elk-human prion species barriers, Kong et al. inoculated elk CWD into transgenic mice expressing either human PrP or elk PrP. Whereas the elk PrP expressing mice developed disease after only 118-142 days post-inoculation, human PrP expressing mice (129M) did not develop any features of TSE after more than 657 or more than 756 days [41]. In accordance with these results, Tamgüney et al. also reported that human PrP overexpressing mice were not susceptible to 9 CWD isolates from mule deer, white-tailed deer, and elk [84]. However, mice have a limited lifespan and further passages may be necessary to detect low levels of prion infectivity that may be present subclinically. Although indi rect evidence is accumulating that there may be a robust species barrier for CWD transmission to humans, one report indicates nonhuman primate susceptibility to CWD. Intracerebral inoculation of squirrel monkeys (Saimiri sciureus) demonstrated a positive CWD transmission [49]. Among non-human primates, however, the Prnp sequence of the new world monkeys are the most distant from humans [72], and therefore may not indicate that human prion conversion would occur by CWD.


11. Disease control challenges posed by CWD

Evidence is building that indicates efficient horizontal transmission occurs in CWD, indeed a complicating aspect in disease control [91]. Potential transmission mechanisms range from spread via direct contact among animals to environmental exposure through grazing in areas contaminated by prion-infected secretions, excretions (saliva, urine, feces), tissues (placenta), or decomposed carcasses. Recently, in a breakthrough finding, saliva from CWD infected deer was shown to transmit prion disease [50]. An additional experiment by Miller and colleagues showed that CWD-infected carcasses allowed to decay naturally in confined pastures can lead to CWD infections in captive deer, demonstrating the potential for environmental contamination to spread infection [55]. Modelling studies have provided further


support that environmental contamination is likely playing a significant role in transmitting CWD [56, 53]. Additionally, infectious prions have been demonstrated to bind soil particles and remain infectious to animals by both intracerebral and oral exposure routes [38, 37]. Prion infectivity has been recovered from soil more than two years after experimental exposure to prions, suggesting the soil may serve as a reservoir for CWD prions [75]. Taken together, these results indicate that there may even be multiple sources for CWD exposure, perhaps through direct contact and environmental routes. Significant challenges to CWD eradication exist in free-ranging cervids. Infected deer and elk range over a broad geographic region, and even previously surmised geographic barriers such as the Continental Divide have proven passable by infected animals. Ridding the environment of CWD-contaminated soil or even CWD-infected carcasses is not possible. Moreover, the available ante-mortem diagnostic tests for surveillance are laborious and impractical for large numbers of free-ranging animals [74, 88, 95]. Therefore for a wildlife manager, this disease is costly to survey and difficult to control.

12. Conclusion

***CWD in cervids is efficiently transmitted, likely more than any other TSE in animals or humans. Therefore, it is unlikely that this TSE can be eradicated, but perhaps through an improved understanding of transmission routes, biological factors influencing pathogenesis, and the molecular basis of CWD prion conversion, a targeted strategy for interrupting disease spread may be developed.


I thank Drs. Michael Miller, Jason Bartz and Mathias Heikenwalder for critical review of the manuscript.

snip...see full text 19 pages ;

Subject: Species barriers for chronic wasting disease by in vitro conversion of prion protein Date: November 3, 2007 at 10:57 am PST

Species barriers for chronic wasting disease by in vitro conversion of prion protein

Li Li a, Michael B. Coulthart b, Aru Balachandran c, Avi Chakrabartty d, Neil R. Cashman a,* a Brain Research Centre, Division of Neurology, Department of Medicine, University of British Columbia and Vancouver Coastal Health, UBC Hospital, 2211 Wesbrook Mall, Vancouver, BC, Canada V6T 2B5 b Prion Diseases Program, National Microbiology Laboratory, Public Health Agency of Canada, Winnipeg, Man., Canada R3E 3R2 Q1 c National Reference Laboratory for Scrapie and CWD, Animal Diseases Research Institute, Canadian Food Inspection Agency, 3851 Fallowfield Road, Nepean, Ont., Canada K2H 8P9 d University Health Network, Department of Medical Biophysics, University of Toronto, Toronto, Ont., Canada M5G 1L7 Received 6 October 2007


Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy that can affect North American cervids (deer, elk, and moose). Using a novel in vitro conversion system based on incubation of prions with normal brain homogenates, we now report that PrPCWD of elk can readily induce the conversion of normal cervid PrP (PrPC) molecules to a protease-resistant form, but is less efficient in converting the PrPC of other species, such as human, bovine, hamster, and mouse. However, when substrate brain homogenates are partially denatured by acidic conditions (pH 3.5), PrPCWD-induced conversion can be greatly enhanced in all species. Our results dem- onstrate that PrPC from cervids (including moose) can be efficiently converted to a protease-resistant form by incubation with elk CWD prions, presumably due to sequence and structural similarities between these species. Moreover, partial denaturation of substrate PrPC can apparently overcome the structural barriers between more distant species.


Although Syrian hamsters were initially deemed resistant to CWD [19], a recent publication demonstrates that CWD can be transmitted and adapted to hamster [20].


Substrate denaturation and human health

We confirm with multiple species that acid/GdnHCl- treated brain PrPC is a superior substrate for in vitro con- version than untreated PrPC, possibly by overcoming con- formational barriers in partial denaturation of substrate PrPC. PrP conversion in scrapie-infected neuroblastoma cells is believed to occur in endosomes, a low-pH and reducing environment [26]. The non-ruminant stomach possesses a low pH lumen, and PrPC is expressed in this organ [27]. Such acidic (denaturing) organ or cellular organellar environments might also promote CWD trans- mission to non-cervid species, including humans.


This work was supported by the Canadian Institutes of Health Research (Institute of Infection and Immunity, Safe Food and Water program) and PrioNet Canada.

[20] G.J. Raymond, L.D. Raymond, K.D. Meade-White, A.G. Hughson, C. Favara, D. Gardner, E.S. Williams, M.W. Miller, R.E. Race, B. Caughey, Transmission and adaptation of chronic wasting disease to hamsters and transgenic mice: evidence for strains, J. Virol. 81 (2007) 4305?4314.

2007 Elsevier Inc. All rights reserved.

Please cite this article in press as: L. Li et al., Species barriers for chronic wasting disease by in vitro..., Biochem. Biophys. Res. Commun. (2007), doi:10.1016/j.bbrc.2007.10.087

Transmission and adaptation of chronic wasting disease to hamsters and transgenic mice: evidence for strains

Gregory J. Raymond1, Lynne D. Raymond1, Kimberly D. Meade-White1, Andrew G. Hughson1, Cynthia Favara1, Donald Gardner2, Elizabeth S. Williams3§, Michael W. Miller4, Richard E. Race1*, and Byron Caughey1*

Running title: CWD transmission to rodent species

Laboratory of Persistent Viral Diseases1, and Rocky Mountain Veterinary Branch2, NIAID, NIH, Rocky Mountain Laboratories, Hamilton, MT 59840; Department of Veterinary Sciences, University of Wyoming, Laramie, WY 820703; Colorado Division of Wildlife, Wildlife Research Center, Fort Collins, CO 80526-20974. §deceased *corresponding authors: Byron Caughey, Rocky Mountain Labs, 903 S. 4th St, Hamilton, MT 59840, USA;; Tel: (406) 363-9264; FAX: (406) 363-9286 Richard Race, Rocky Mountain Labs, 903 S. 4th St, Hamilton, MT 59840, USA;; Tel: (406) 363-9358; FAX: (406) 363-9286

In vitro screening using the cell-free prion protein conversion system indicated that certain rodents may be susceptible to chronic wasting disease (CWD). Therefore, CWD isolates from mule deer, white-tailed deer and elk were inoculated intracerebrally into various rodent species to assess their susceptibility and to develop new rodent models of CWD. The species inoculated were Syrian golden, Djungarian, Chinese, Siberian, and Armenian hamsters; transgenic mice expressing the Syrian golden hamster prion protein; and, RML Swiss and C57 BL10 wild-type mice. The transgenic mice and the Syrian golden, Chinese, Siberian and Armenian hamsters had limited susceptibility to certain of the CWD inocula as evidenced by incomplete attack rates and long incubation periods. With serial passages of CWD isolates in Syrian golden hamsters, incubation periods rapidly stabilized as isolates with either short (85-89 days) or long (408-544 days) mean incubation periods and distinct neuropathological patterns. In contrast, wild-type mouse strains and Djungarian hamsters were not susceptible to CWD. These results show that CWD can be transmitted and adapted to some species of rodents and suggest that the cervid-derived CWD inocula may have contained, or diverged into, at least two distinct transmissible spongiform encephalopathy strains.


Differences in PrP-res glycoform patterns analyzed from several CWD- affected deer and elk have also suggested that CWD in mule deer may be more heterogeneous than in elk (19). Curiously, however, this apparent strain difference was not manifested when the identical mule deer CWD inoculum was serially passaged through only one recipient species. Serial passage in Sg hamsters yielded only the fast isolate (Table 1 and Figure 3), while passage first through the Tg (haPrP) mice then into Sg hamsters yielded only the slow isolate (Table 2 and Figure 3). With this in mind, it is important to consider other possible explanations for these results. One possibility is that CWD might be able to undergo a stochastic change into a more rapid and aggressive strain in Sg hamsters, and that this happened to occur after the mule deer CWD inoculations. A similar emergence of both fast and slow strains has been observed upon inoculation of TME into Sg hamsters (5). These strains developed even when a clonal isolate of the TME inoculum was used, suggesting that they arose in the recipient Sg hamsters rather than in the mink source (1). Finally, although extensive precautions were taken, we cannot formally prove that inadvertent contamination of the mule deer CWD inoculum with hamster-derived 263K strain did not occur which potentially could yield short- incubation-period passages in Sg hamsters (Table 1). However, the incubation period observed with the CWD passages (85-89 d) were significantly longer than 263K incubation periods observed in our lab (70-75 d) and no mock-infected

controls became sick during their lifespan. Also, we saw no 263K-like infectivity develop in the highly susceptible Tg (haPrP) mice even though we used the identical primary inoculum for both recipient species. Interestingly, the similarity of the Sg hamster-adapted CWD fast isolate and 263K might be due to a common origin since there is circumstantial evidence that CWD arose from cervid exposure to sheep scrapie, which was also the origin of the 263K strain in hamsters (14). Furthermore, the Hyper strain derived from TME inoculations has 263K-like strain characteristics in Sg hamsters (5). Thus, it would appear that both CWD and TME transmissions into Sg hamsters can result in divergent fast and slow strains.


Subject: Re: Colorado Surveillance Program for Chronic Wasting Disease Transmission to Humans (TWO SUSPECT CASES) From: "Terry S. Singeltary Sr." <[log in to unmask]> Reply-To: Sustainable Agriculture Network Discussion Group <[log in to unmask]> Date: Wed, 4 Apr 2007 16:22:22 -0500 Content-Type: multipart/alternative Parts/Attachments: text/plain (3340 lines) , text/html (2782 lines)

Subject: Re: Transmission and adaptation of chronic wasting disease to hamsters and transgenic mice: evidence for strains Date: April 1, 2007 at 7:30 pm PST

Nonetheless, the rodent-adapted CWD models we have developed may be useful to experimentally analyze TSE species and strain differences. Despite the low initial attack rate on the first passage of CWD into Sg hamsters, CWD derived initially from elk and mule deer readily adapted to hamsters as evidenced by the 100% infection rate on second and third passages. The average incubation periods were similar for the second and third passages, but considerably shorter than the first passage in the Sg hamsters, suggesting that any species barrier to infection (formally, the shortening of incubation period between the first and subsequent passages in a new species) was overcome quickly.<<< very disturbing considering the potential for iatrogenic CJD via silent human CWD carriers. ...TSS Chronic Wasting Disease and Potential Transmission to Humans Ermias D. Belay,* Ryan A. Maddox,* Elizabeth S. Williams,† Michael W. Miller,‡ Pierluigi Gambetti,§ and Lawrence B. Schonberger* *Centers for Disease Control and Prevention, Atlanta, Georgia, USA; †University of Wyoming, Laramie, Wyoming, USA; ‡Colorado Division of Wildlife, Fort Collins, Colorado, USA; and §Case Western Reserve University, Cleveland, Ohio, USA Suggested citation for this article: Belay ED, Maddox RA, Williams ES, Miller MW, Gambetti P, Schonberger LB. Chronic wasting disease and potential transmission to humans. Emerg Infect Dis [serial on the Internet]. 2004 Jun [date cited]. Available from: ---------------------------------------------------------------------------- ---- Chronic wasting disease (CWD) of deer and elk is endemic in a tri-corner area of Colorado, Wyoming, and Nebraska, and new foci of CWD have been detected in other parts of the United States. Although detection in some areas may be related to increased surveillance, introduction of CWD due to translocation or natural migration of animals may account for some new foci of infection. Increasing spread of CWD has raised concerns about the potential for increasing human exposure to the CWD agent. The foodborne transmission of bovine spongiform encephalopathy to humans indicates that the species barrier may not completely protect humans from animal prion diseases. Conversion of human prion protein by CWD-associated prions has been demonstrated in an in vitro cell-free experiment, but limited investigations have not identified strong evidence for CWD transmission to humans. More epidemiologic and laboratory studies are needed to monitor the possibility of such transmissions. snip... Conclusions The lack of evidence of a link between CWD transmission and unusual cases of CJD, despite several epidemiologic investigations, and the absence of an increase in CJD incidence in Colorado and Wyoming suggest that the risk, if any, of transmission of CWD to humans is low. Although the in vitro studies indicating inefficient conversion of human prion protein by CWD-associated prions raise the possibility of low-level transmission of CWD to humans, no human cases of prion disease with strong evidence of a link with CWD have been identified. However, the transmission of BSE to humans and the resulting vCJD indicate that, provided sufficient exposure, the species barrier may not completely protect humans from animal prion diseases. Because CWD has occurred in a limited geographic area for decades, an adequate number of people may not have been exposed to the CWD agent to result in a clinically recognizable human disease. The level and frequency of human exposure to the CWD agent may increase with the spread of CWD in the United States. Because the number of studies seeking evidence for CWD transmission to humans is limited, more epidemiologic and laboratory studies should be conducted to monitor the possibility of such transmissions. Studies involving transgenic mice expressing human and cervid prion protein are in progress to further assess the potential for the CWD agent to cause human disease. Epidemiologic studies have also been initiated to identify human cases of prion disease among persons with an increased risk for exposure to potentially CWD-infected deer or elk meat (47). If such cases are identified, laboratory data showing similarities of the etiologic agent to that of the CWD agent would strengthen the conclusion for a causal link. Surveillance for human prion diseases, particularly in areas where CWD has been detected, remains important to effectively monitor the possible transmission of CWD to humans. Because of the long incubation period associated with prion diseases, convincing negative results from epidemiologic and experimental laboratory studies would likely require years of follow-up. In the meantime, to minimize the risk for exposure to the CWD agent, hunters should consult with their state wildlife agencies to identify areas where CWD occurs and continue to follow advice provided by public health and wildlife agencies. Hunters should avoid eating meat from deer and elk that look sick or test positive for CWD. They should wear gloves when field-dressing carcasses, bone-out the meat from the animal, and minimize handling of brain and spinal cord tissues. As a precaution, hunters should avoid eating deer and elk tissues known to harbor the CWD agent (e.g., brain, spinal cord, eyes, spleen, tonsils, lymph nodes) from areas where CWD has been identified.

From: TSS (
Date: September 30, 2002 at 7:06 am PST
From: "Belay, Ermias"
To: Cc: "Race, Richard (NIH)" ; ; "Belay, Ermias"
Sent: Monday, September 30, 2002 9:22 AM

Dear Sir/Madam,

In the Archives of Neurology you quoted (the abstract of which was attached to your email), we did not say CWD in humans will present like variant CJD. That assumption would be wrong. I encourage you to read the whole article and call me if you have questions or need more clarification (phone: 404-639-3091). Also, we do not claim that "no-one has ever been infected with prion disease from eating venison." Our conclusion stating that we found no strong evidence of CWD transmission to humans in the article you quoted or in any other forum is limited to the patients we investigated. Ermias Belay, M.D. Centers for Disease Control and Prevention -----Original Message----- From: Sent: Sunday, September 29, 2002 10:15 AM To: [log in to unmask]">[log in to unmask]; [log in to unmask]">[log in to unmask]; [log in to unmask]">[log in to unmask] Subject: TO CDC AND NIH - PUB MED- 3 MORE DEATHS - CWD - YOUNG HUNTERS

Sunday, November 10, 2002 6:26 PM ......snip........end..............TSS


A. Aguzzi - Chronic Wasting Disease (CWD) also needs to be addressed. Most serious because of rapid horizontal spread and higher prevalence than BSE in UK, up to 15% in some populations. Also may be a risk to humans - evidence that it is not dangerous to humans is thin.

JOURNAL OURNAL OF VIROLOGY IROLOGY, Nov. 2005, p. 13794–13796 Vol. 79, No. 21 0022-538X/05/$08.00 !0 doi:10.1128/JVI.79.21.13794–13796.2005 Copyright © 2005, American Society for Microbiology. All Rights Reserved.


Interspecies Transmission of Chronic Wasting Disease Prions to Squirrel Monkeys (Saimiri sciureus sciureus)

Richard F. Marsh, 1† Anthony nthony E. Kincaid, 2 Richard A. Bessen, 3 and Jason C. Bartz Bartz4* Department of Animal Health and Biomedical Sciences, University of Wisconsin, Madison 53706 537061; Department of Physical Therapy Therapy2 and Department of Medical Microbiology and Immunology, 4 Creighton University, Omaha, Nebraska 68178; and Department of Veterinary Molecular Biology, Montana State University, Bozeman, Montana 59718 597183 Received 3 May 2005/Accepted 10 August 2005

Chronic wasting disease (CWD) is an emerging prion disease of deer and elk. The risk of CWD transmission to humans following exposure to CWD-infected tissues is unknown. To assess the susceptibility of nonhuman primates to CWD, two squirrel monkeys were inoculated with brain tissue from a CWD-infected mule deer. The CWD-inoculated squirrel monkeys developed a progressive neurodegenerative disease and were euthanized at 31 and 34 months postinfection. Brain tissue from the CWD-infected squirrel monkeys contained the abnormal isoform of the prion protein, PrP-res, and displayed spongiform degeneration. This is the first reported transmission of CWD to primates. ...snip...end

Full Text

Diagnosis and Reporting of Creutzfeldt-Jakob Disease

Singeltary, Sr et al. JAMA.2001; 285: 733-734.

full text ;

Tuesday, June 3, 2008


NOR-98 ATYPICAL SCRAPIE 5 cases documented in USA in 5 different states USA 2007


Aspects of the Cerebellar Neuropathology in Nor98

Gavier-Widén, D1; Benestad, SL2; Ottander, L1; Westergren, E1 1National Veterinary Insitute, Sweden; 2National Veterinary Institute, Norway

Nor98 is a prion disease of old sheep and goats. This atypical form of scrapie was first described in Norway in 1998. Several features of Nor98 were shown to be different from classical scrapie including the distribution of disease associated prion protein (PrPd) accumulation in the brain. The cerebellum is generally the most affected brain area in Nor98. The study here presented aimed at adding information on the neuropathology in the cerebellum of Nor98 naturally affected sheep of various genotypes in Sweden and Norway. A panel of histochemical and immunohistochemical (IHC) stainings such as IHC for PrPd, synaptophysin, glial fibrillary acidic protein, amyloid, and cell markers for phagocytic cells were conducted. The type of histological lesions and tissue reactions were evaluated. The types of PrPd deposition were characterized. The cerebellar cortex was regularly affected, even though there was a variation in the severity of the lesions from case to case. Neuropil vacuolation was more marked in the molecular layer, but affected also the granular cell layer. There was a loss of granule cells. Punctate deposition of PrPd was characteristic. It was morphologically and in distribution identical with that of synaptophysin, suggesting that PrPd accumulates in the synaptic structures. PrPd was also observed in the granule cell layer and in the white matter. ***The pathology features of Nor98 in the cerebellum of the affected sheep showed similarities with those of sporadic Creutzfeldt-Jakob disease in humans.

Published online before print October 20, 2005

Proc. Natl. Acad. Sci. USA, 10.1073/pnas.0502296102 Medical Sciences

A newly identified type of scrapie agent can naturally infect sheep with resistant PrP genotypes

( sheep prion transgenic mice )

Annick Le Dur *, Vincent Béringue *, Olivier Andréoletti , Fabienne Reine *, Thanh Lan Laï *, Thierry Baron , Bjørn Bratberg ¶, Jean-Luc Vilotte , Pierre Sarradin **, Sylvie L. Benestad ¶, and Hubert Laude * *Virologie Immunologie Moléculaires and Génétique Biochimique et Cytogénétique, Institut National de la Recherche Agronomique, 78350 Jouy-en-Josas, France; Unité Mixte de Recherche, Institut National de la Recherche Agronomique-Ecole Nationale Vétérinaire de Toulouse, Interactions Hôte Agent Pathogène, 31066 Toulouse, France; Agence Française de Sécurité Sanitaire des Aliments, Unité Agents Transmissibles Non Conventionnels, 69364 Lyon, France; **Pathologie Infectieuse et Immunologie, Institut National de la Recherche Agronomique, 37380 Nouzilly, France; and ¶Department of Pathology, National Veterinary Institute, 0033 Oslo, Norway

Edited by Stanley B. Prusiner, University of California, San Francisco, CA, and approved September 12, 2005 (received for review March 21, 2005)

Scrapie in small ruminants belongs to transmissible spongiform encephalopathies (TSEs), or prion diseases, a family of fatal neurodegenerative disorders that affect humans and animals and can transmit within and between species by ingestion or inoculation. Conversion of the host-encoded prion protein (PrP), normal cellular PrP (PrPc), into a misfolded form, abnormal PrP (PrPSc), plays a key role in TSE transmission and pathogenesis. The intensified surveillance of scrapie in the European Union, together with the improvement of PrPSc detection techniques, has led to the discovery of a growing number of so-called atypical scrapie cases. These include clinical Nor98 cases first identified in Norwegian sheep on the basis of unusual pathological and PrPSc molecular features and "cases" that produced discordant responses in the rapid tests currently applied to the large-scale random screening of slaughtered or fallen animals. Worryingly, a substantial proportion of such cases involved sheep with PrP genotypes known until now to confer natural resistance to conventional scrapie. Here we report that both Nor98 and discordant cases, including three sheep homozygous for the resistant PrPARR allele (A136R154R171), efficiently transmitted the disease to transgenic mice expressing ovine PrP, and that they shared unique biological and biochemical features upon propagation in mice. These observations support the view that a truly infectious TSE agent, unrecognized until recently, infects sheep and goat flocks and may have important implications in terms of scrapie control and public health.

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

A.L.D. and V.B. contributed equally to this work.

To whom correspondence should be addressed.

Hubert Laude, E-mail:

Like lambs to the slaughter

31 March 2001

Debora MacKenzie

Magazine issue 2284

What if you can catch old-fashioned CJD by eating meat from a sheep infected with scrapie?

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

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

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

The complete article is 889 words long.

full text;


Adaptation of the bovine spongiform encephalopathy agent to primates and comparison with Creutzfeldt- Jakob disease: Implications for human health Corinne Ida Lasmézas*,, Jean-Guy Fournier*, Virginie Nouvel*, Hermann Boe*, Domíníque Marcé*, François Lamoury*, Nicolas Kopp, Jean-Jacques Hauw§, James Ironside¶, Moira Bruce, Dominique Dormont*, and Jean-Philippe Deslys* * Commissariat à l'Energie Atomique, Service de Neurovirologie, Direction des Sciences du Vivant/Département de Recherche Medicale, Centre de Recherches du Service de Santé des Armées 60-68, Avenue du Général Leclerc, BP 6, 92 265 Fontenay-aux-Roses Cedex, France; Hôpital Neurologique Pierre Wertheimer, 59, Boulevard Pinel, 69003 Lyon, France; § Laboratoire de Neuropathologie, Hôpital de la Salpêtrière, 83, Boulevard de l'Hôpital, 75013 Paris, France; ¶ Creutzfeldt-Jakob Disease Surveillance Unit, Western General Hospital, Crewe Road, Edinburgh EH4 2XU, United Kingdom; and Institute for Animal Health, Neuropathogenesis Unit, West Mains Road, Edinburgh EH9 3JF, United Kingdom

Edited by D. Carleton Gajdusek, Centre National de la Recherche Scientifique, Gif-sur-Yvette, France, and approved December 7, 2000 (received for review October 16, 2000)


There is substantial scientific evidence to support the notion that bovine spongiform encephalopathy (BSE) has contaminated human beings, causing variant Creutzfeldt-Jakob disease (vCJD). This disease has raised concerns about the possibility of an iatrogenic secondary transmission to humans, because the biological properties of the primate-adapted BSE agent are unknown. We show that (i) BSE can be transmitted from primate to primate by intravenous route in 25 months, and (ii) an iatrogenic transmission of vCJD to humans could be readily recognized pathologically, whether it occurs by the central or peripheral route. Strain typing in mice demonstrates that the BSE agent adapts to macaques in the same way as it does to humans and confirms that the BSE agent is responsible for vCJD not only in the United Kingdom but also in France. The agent responsible for French iatrogenic growth hormone-linked CJD taken as a control is very different from vCJD but is similar to that found in one case of sporadic CJD and one sheep scrapie isolate. These data will be key in identifying the origin of human cases of prion disease, including accidental vCJD transmission, and could provide bases for vCJD risk assessment.

typical scrapie transmits to primates by there NON-FORCED ORAL CONSUMPTION ;


snip...full text ;


Friday, March 21, 2008

Association between Deposition of Beta-Amyloid and Pathological Prion Protein in Sporadic Creutzfeldt-Jakob Disease

Friday, March 21, 2008 Association between Deposition of Beta-Amyloid and Pathological Prion Protein in Sporadic Creutzfeldt-Jakob Disease

Original Paper

Association between Deposition of Beta-Amyloid and Pathological Prion Protein in Sporadic Creutzfeldt-Jakob Disease

Laura Debatina, Johannes Strefferb, Markus Geissenc, Jakob Matschkec, Adriano Aguzzia, Markus Glatzela, c

aInstitute of Neuropathology, and bDivision of Psychiatry Research, University Hospital Zurich, Zurich, Switzerland; cInstitute of Neuropathology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany

Address of Corresponding Author

Neurodegenerative Dis (DOI: 10.1159/000121389)

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Key Words

Sporadic Creutzfeldt-Jakob disease Alzheimer's disease Deposition of -amyloid Prion protein

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Background: Alzheimer's disease (AD) and prion diseases such as sporadic Creutzfeldt-Jakob disease (sCJD) share common features concerning their molecular pathogenesis and neuropathological presentation and the coexistence of AD and CJD in patients suggest an association between the deposition of the proteolytically processed form of the amyloid precursor protein, -amyloid (A), which deposits in AD, and the abnormal form of the prion protein, PrPSc, which deposits in sCJD. Methods: We have characterized sCJD patients (n = 14), AD patients (n = 5) and nondemented controls (n = 5) with respect to the deposition of PrPSc and A morphologically, biochemically and genetically and correlated these findings to clinical data. Results: sCJD-diseased individuals with abundant deposits of A present with a specific clinicopathological profile, defined by higher age at disease onset, long disease duration, a genetic profile and only minimal amounts of PrPSc in the cerebellum. Conclusion: The co-occurrence of pathological changes typical for sCJD and AD in combination with the inverse association between accumulation of A and PrPSc in a subgroup of sCJD patients is indicative of common pathways involved in the generation or clearance of A and PrPSc in a subgroup of sCJD patients.

Copyright © 2008 S. Karger AG, Basel

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Author Contacts

Markus Glatzel Institute of Neuropathology, University Medical Center Hamburg-Eppendorf Martinistrasse 52, DE-20246 Hamburg (Germany) Tel. +49 40 42 803 2218, Fax +49 40 42 803 4929 E-Mail

please see full text ;

Alzheimer's and CJD

Saturday, March 22, 2008

10 Million Baby Boomers to have Alzheimer's in the coming decades 2008 Alzheimer's disease facts and figures

re-Association between Deposition of Beta-Amyloid and Pathological Prion Protein in Sporadic Creutzfeldt-Jakob Disease

Aguzzi A. Unraveling prion strains with cell biology and organic chemistry. Proc Natl Acad Sci U S A. 2008 Jan 2; [Epub ahead of print] No abstract available.

Institute of Neuropathology, UniversitätsSpital Zürich, Schmelzbergstrasse 12, CH-8091 Zürich, Switzerland

Prions are the infectious agents causing transmissible spongiform encephalopathies (TSEs), which comprise human Creutzfeldt-Jakob disease (CJD), scrapie of sheep, bovine spongiform encephalopathy (BSE), and several other rare ailments of various species. According to the protein-only hypothesis (1), prions are composed solely of PrPSc, a misfolded form of the cellular protein PrPC. PrPSc typically forms highly ordered fibrillary aggregates, also termed "amyloid." The term "prion strain" denotes individual prion isolates sharing the same PrP sequence but giving rise to distinct, stable disease traits with different incubation periods and lesion profiles upon serial transmission in congenic hosts. The propagation of different strains in mice congenic with respect to their Prnp allelotypes is difficult to explain by the protein-only hypothesis because the epigenetic strain characteristics of prions appear to dominate over the primary prion protein sequence of the infected host (2, 3).

Circumstantial evidence suggests that strain phenotypes are encoded by distinct conformations of PrPSc (Fig. 1). This was first implied by experiments showing that distinct strains of transmissible mink encephalopathy went along with different protease-exposed sites within PrPSc (4). Great strides have been made since then, yet the final proof that conformational variants of PrPSc represent the biological basis of mammalian prion strains is still elusive. Distinct prion strains may bear highly divergent risks of transmission to humans: Sheep scrapie-derived strains may be mostly innocuous, whereas BSE-derived strains appear to induce variant CJD (vCJD) in humans. Also, two subtypes . . . [Full Text of this Article]


snip... significance than prions. Strain-like amyloid

conformational variants may occur

in Alzheimer's disease (AD) (22), suggesting

that the pathogenetic mechanisms

operating in AD and prion to

diseases have more in common than

typically appreciated (23). Ordered aggregation

of proteins was also found to

occur in most instances of type II diabetes,

chronic inflammatory conditions,

and many disorders of skeletal muscle.

Therefore, a full understanding of the

prion strain phenomenon may help with

devising a sensitive diagnostic procedure,

and possibly also rational therapies, of

many aggregation proteinopathies. Some

of the latter diseases rank among the

most prevalent chronic ailments of


The statistical incidence of CJD cases in the United States has been revised to reflect that there is one case per 9000 in adults age 55 and older. Eighty-five percent of the cases are sporadic, meaning there is no known cause at present.

Communicated by: Terry S. Singeltary Sr. <>

[In submitting these data, Terry S. Singeltary Sr. draws attention to the steady increase in the "type unknown" category, which, according to their definition, comprises cases in which vCJD could be excluded. The total of 26 cases for the current year (2007) is disturbing, possibly symptomatic of the circulation of novel agents. Characterization of these agents should be given a high priority. - Mod.CP],F2400_P1001_PUB_MAIL_ID:1010,39963

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 collection.

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

Hardcover, 304 pages plus photos and illustrations. ISBN 0-387-95508-9
June 2003

BY Philip Yam


Answering critics like Terry Singeltary, who feels that the U.S. under-counts CJD, Schonberger conceded that the current surveillance system has errors but stated that most of the errors will be confined to the older population.

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

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