Vaccines and Transmissible Spongiform Encephalopathy the Prion Disease, what if ?

Vaccines and Transmissible Spongiform Encephalopathy the Prion Disease, what if ?



COMMERCIAL IN CONFIDENCE

3.2 Minute 5.3 - 5.4 Bovine Spongiform Encephalopathy

It was reported that some replies had been received from Companies using pituitary glands in their products. Copies of the BSE document had also been sent to DHSS and NIBSC.

and then another 3 + pages of blank space. ...TSS


http://collections.europarchive.org/tna/20080102164813/http://www.bseinquiry.gov.uk/files/yb/1988/09/06005001.pdf



COMMERCIAL IN CONFIDENCE

BSE - CURRENT POSITION WITH VETERINARY LICENCED PRODUCTS (MA.1968)

There are three areas of particular concern, vaccines (including emergency vaccines), pharmaceuticals which are covered by MA licences and unlicenses hormonal products produced under exemptions claimed under (Section 9(2) Medicines Act).

1) Vaccines


http://collections.europarchive.org/tna/20080103033809/http://www.bseinquiry.gov.uk/files/yb/1988/10/06005001.pdf



NOT FOR PUBLICATION

another 6 pages of blank space. ...TSS



http://collections.europarchive.org/tna/20080103032658/http://www.bseinquiry.gov.uk/files/yb/1988/11/01012001.pdf



http://collections.europarchive.org/tna/20080103032631/http://www.bseinquiry.gov.uk/files/yb/1988/11/04003001.pdf



http://collections.europarchive.org/tna/20080103033926/http://www.bseinquiry.gov.uk/files/yb/1988/04/00007001.pdf



COMMERCIAL IN CONFIDENCE


http://collections.europarchive.org/tna/20080103034137/http://www.bseinquiry.gov.uk/files/yb/1988/07/00007001.pdf



COMMERCIAL IN CONFIDENCE

Medicines Act - Veterinary Products Committee


http://collections.europarchive.org/tna/20080103034140/http://www.bseinquiry.gov.uk/files/yb/1988/09/00004001.pdf



COMMERCIAL IN CONFIDENCE

NOT FOR PUBLICATION

COMMITTEE ON SAFETY OF MEDICINES

another 6 pages or so that are blank. ...TSS


http://collections.europarchive.org/tna/20080102185137/http://www.bseinquiry.gov.uk/files/yb/1989/01/26007001.pdf



http://collections.europarchive.org/tna/20080102184613/http://www.bseinquiry.gov.uk/files/yb/1989/01/30001001.pdf



COMMERCIAL IN CONFIDENCE

NOT FOR PUBLICATION

COMMITTEE ON SAFETY OF MEDICINES

WORKING PARTY ON BOVINE SPONGIFORM ENCEPHALOPATHY

7.2.1. Products with bovine brain/lymphoid tissue as ingredients and administered by injection...[111]

7.2.2 Products with bovine ingredients (other than brain/lymphoid tissue) and administered by injection...[135]

7.2.3 Tissue implants, open wound dressings, surgical materials, dental and opthalmic products with bovine ingredients...[27]

7.2.4. Products with bovine ingredients and administered topically...[5]

7.2.5 Products with bovine ingredients and administered orally...[9]

7.2.6 Products with other animal/insect/bird ingredients and administered:

a. by injection a: 117

b. by topically b: 6

c. orally c: 8

7.2.7 Products with materials produced from animal material by chemical processes, eg stearic acid, gelatin and lanolin...[156]

With two exceptions, the replies to date have not given any immediate cause for concern, although 176 products do not conform to the CSM/VPC guidelines.

8. The first exception was from which gave very limited information about a very large number of homoepathic medicines with material obtained from cattle and a number with material from the brain. Of these, 53 were injectable products of which 20 were derived from cattle brain. A list of these products is attached as Appendix 1 to Annex D. The second exception relates to the product, 'Surgical Catgut', which is sourced from UK bovine intestines and will contain lymphoid material...

see full text ;


http://collections.europarchive.org/tna/20080102164420/http://www.bseinquiry.gov.uk/files/yb/1989/09/06011001.pdf



COMMERCIAL IN CONFIDENCE


http://collections.europarchive.org/tna/20080102164744/http://www.bseinquiry.gov.uk/files/yb/1988/10/00003001.pdf



MANAGEMENT IN CONFIDENCE


CERTIFIED BSE-FREE HERDS FOR SOURCE OF MATERIAL FOR BIOLOGICAL PRODUCTS

http://collections.europarchive.org/tna/20080102184729/http://www.bseinquiry.gov.uk/files/yb/1989/01/04001001.pdf




Subject: BSE--U.S. 50 STATE CONFERENCE CALL Jan. 9, 2001

Date: Tue, 9 Jan 2001 16:49:00 -0800

From: "Terry S. Singeltary Sr."

Reply-To: Bovine Spongiform Encephalopathy

To: BSE-L@uni-karlsruhe.de

[host Richard Barns] and now a question from Terry S. Singeltary of CJD Watch.

[TSS] yes, thank you, U.S. cattle, what kind of guarantee can you give for serum or tissue donor herds?

[no answer, you could hear in the back ground, mumbling and 'we can't. have him ask the question again.]

[host Richard] could you repeat the question?

[TSS] U.S. cattle, what kind of guarantee can you give for serum or tissue donor herds?

[not sure whom ask this] what group are you with?

[TSS] CJD Watch, my Mom died from hvCJD and we are tracking CJD world-wide.

[not sure who is speaking] could you please disconnect Mr. Singeltary

[TSS] you are not going to answer my question?

[not sure whom speaking] NO

from this point, i was still connected, got to listen and tape the whole conference. at one point someone came on, a woman, and ask again;

[unknown woman] what group are you with?

[TSS] CJD Watch and my Mom died from hvCJD we are trying to tract down CJD and other human TSE's world wide. i was invited to sit in on this from someone inside the USDA/APHIS and that is why i am here. do you intend on banning me from this conference now?

at this point the conference was turned back up, and i got to finish listening. They never answered or even addressed my one question, or even addressed the issue. BUT, i will try and give you a run-down for now, of the conference.

snip...full text ;


http://bse-atypical.blogspot.com/2010/01/14th-international-congress-on.html



The documents below were provided by Terry S. Singeltary Sr on 8 May 2000.

They are optically character read (scanned into computer) and so may contain typos and unreadable parts.

TIP740203/l 0424 CONFIDENTIAL

snip...

The responses by the companies were presented by Ms Turner and were categorised by MCA standards, the products that were discussed were all low volume usage products eg sutures, heart valves.

8. As the responses included some materials of human origin it was decided that more information should be sought about CJD. There had been 2 recent deaths reported associated with human growth hormone. These were being investigated.

snip...

http://www.mad-cow.org/00/may00_news.html#aaa



5.3.3 The greatest risk, in theory, would be from parenteral injection of material derived from bovine brain or lymphoid tissue. Medicinal products for injection or surgical implantation which are prepared from bovine tissues, or which utilise bovine serum albumin or similar agents in their manufacture, might also be capable of transmitting infectious agents. All medicinal products are licensed under the Medicines Act by the Licensing Authority following guidance, for example from the Committee on Safety of Medicines (CSM), the Committee on Dental and Surgical Materials (CDSM) and their subcommittees. The Licensing Authority have been alerted to potential concern about BSE in medicinal products and will ensure that scrutiny of source materials and manufacturing processes now takes account of BSE agent.

see all 76 pages ;


http://collections.europarchive.org/tna/20080102132706/http://www.bseinquiry.gov.uk/files/ib/ibd1/tab02.pdf



EXPORT OF BRITISH BIOLOGICAL PHARMACEUTICALS

1. Please see the attached note of a recent meeting in Brussels. For Dr. Purford should read Dr. Purves (I think). If the Germans get their way, and it looks as if they might, because of worries about BSE we could end up with a ban on certain bovine materials being exported from the UK for pharmaceutical manufacture. Thse materials include cell cultures of bovine origin (? and also any cultures which have been fed bovine nutrient material), bovine serum, and fetal calf serum.

2. Whilst export of these raw materials may be very limited, it is only a small step to include in this export ban any finished product made from such materials. This would include virtually all biologicals and vaccines. This could have very serious effects on the export trade of British Manufacturers of biologicals because even where they source their bovine ingredients outside the UK it might be impossible or at least very difficult to bypass any export ban.

3. Our own line is that we have not used regulations to restrict the use of British bovine material for non-food use, although certain offals cannot be used for human consumption. ...


http://collections.europarchive.org/tna/20080102220244/http://www.bseinquiry.gov.uk/files/yb/1990/03/13002001.pdf



Export of British 'Biological' Pharmaceuticals


http://collections.europarchive.org/tna/20080102220202/http://www.bseinquiry.gov.uk/files/yb/1990/03/13008001.pdf



http://collections.europarchive.org/tna/20080102215829/http://www.bseinquiry.gov.uk/files/yb/1990/03/13009001.pdf



No papers were presented by our American guests and none covered the subject of pharmaceuticals. ...


http://collections.europarchive.org/tna/20080102220453/http://www.bseinquiry.gov.uk/files/yb/1990/04/02002001.pdf



STANDING COMMITTEE MEETING ON BSE

Thanks for your note. I am disappointed not to have been informed about this meeting in advance and am surprised that Dr. Tyrrell was not involved either. I find it insulting to be told the proceedings were in confidence and find your excuse about only hosting the meeting unconvincing.


http://collections.europarchive.org/tna/20080102220555/http://www.bseinquiry.gov.uk/files/yb/1990/04/06002001.pdf



The documents below were provided by Terry S. Singeltary Sr on 8 May 2000.

They are optically character read (scanned into computer) and so may contain typos and unreadable parts.

TIP740203/l 0424 CONFIDENTIAL

Mr Cunningham CMP3 From: D O Hagger MBI Dr Salisbury MED/IMCD3 Mr Burton PD/STB/PG1B B/17/2 Date: 15.02.1989 Mr Dudley PD/AD4


snip...


89/06.19/8.1 BSE3/1 0191 Hr J Maslin (MAFF) Ref: Maslin3g

From: Dr H Pickles Med SEB/B Date: 3 July 1989

CATTLE BY-PRODUCTS AND BSE

I was interested to see the list of by-products sent to the HSE. Those of particular concern included:

* small intestines: sutures (I thought the source was ovine but you are checking this)

* spinal cord: pharmaceuticals

* thymus: pharmaceuticals

Are you able to give me more information on which UK manufacturers use these materials? Our proposed ban on bovine offal for human consumption would not affect these uses, I assume.

snip...see full text ;


http://www.mad-cow.org/00/may00_news.html



http://www.javno.com/en/world/clanak.php?id=32047



http://creutzfeldt-jakob-disease.blogspot.com/2007/12/risk-factors-for-sporadic-creutzfeldt.html



40,000 human heart valves a year from BSE herds Sun, 3 Sep 2000.

Unpublished Inquiry documents obtained by CJD activist Terry S. Singeltary Sr. of Bacliff, Texas


http://www.mad-cow.org/00/sep00_news.html#hhh



USDA allows diseased animals into human food supply

Mon, 14 Aug 2000. Information provided by Terry S. Singeltary Sr.

In Confidence - Perceptions of unconventional slow virus diseases of animals in the USA - Report of a visit to the USA - April-May 1989 - G A H Wells [head of England's main veterinary lab -- webmaster]


2. Meeting with USDA, BSE Task Force



http://www.mad-cow.org/00/aug00_late_news.html#hhh




http://www.mad-cow.org/00/may00_news.html#aaa




http://www.mad-cow.org/00/01jan_news.html#aaa




Subject: Louping-ill vaccine documents from November 23rd, 1946

Date: Sat, 9 Sep 2000 17:44:57 -0700

From: "Terry S. Singeltary Sr."

Reply-To: Bovine Spongiform Encephalopathy

To: BSE-L@uni-karlsruhe.de


######### Bovine Spongiform Encephalopathy #########


THE VETERINARY RECORD 516 No 47. Vol. 58 November 23rd, 1946

NATIONAL VETERINARY MEDICAL ASSOCIATION OF GREAT BRITAIN AND IRELAND

ANNUAL CONGRESS, 1946

snip...

As a result of this experience a large-scale transmision experiment involving the ue of 788 sheep was commenced in 1938 on a farm specially taken for the purpose by the Animal Diseases Research Association with funds provided by the Agricultural Research Council. The experiment was designed to determine the nature of the infective agent and the pathogenesis of the disease. It is only possible here to give a summary of the result which showed that (1) saline suspensions of brain and spinal cord tissue of sheep affected with scrapie were infective to normal sheep when inoculatted intracerebrally or subcutaneously; (2) the incubation period after intracerebral inoculation was seven months and upwards and only 60 percent of the inoculated sheep developed scrapie during a period of four and a half years; (3) the incubation period after subcutaneous inoculation was 15 months and upwards and only about 30 percent of the inoculated sheep developed the disease during the four and a half years: (4) the infective agent was of small size and probably a filtrable virus.

The prolonged incubative period of the disease and the remarkable resistance of the causal agent to formalin are features of distinct interest. It still remains to determine if a biological test can be devised to detect infected animals so that they can be killed for food before they develop clinical symptoms and to explore the possibilities of producing an immunity to the disease.

==================================================================

Greetings List Members,

pretty disturbing document. now, what would stop this from happening with the vaccineCJD in children???

kind regards, Terry S. Singeltary Sr., Bacliff, Texas USA


http://www.whale.to/v/singeltary.html



MAD COW DISEASE BSE CJD CHILDREN VACCINES

Sunday, May 18, 2008

MAD COW DISEASE BSE CJD CHILDREN VACCINES

TIP740203/l 0424 CONFIDENTIAL


http://bseinquiry.blogspot.com/2008/05/mad-cow-disease-bse-cjd-children.html



Research Lead: Dr. David Westaway, University of Alberta

Project: "Extending the spectrum of Prionopathies to Amyotrophic Lateral Sclerosis and Autism"

This project proposes to link the chemistry of the prion protein to the new territory of other nervous system diseases, such as ALS (Lou Gehrig's disease) and the socialization disorder autism -diseases which are at least one thousand times more common than prion diseases. It is believed that a different type or prion protein may operate in other types of brain diseases, which could lead to new ways of thinking about incurable disorders. The project will create changes in the amounts of the various forms of the new membrane protein, and then perform an array of analyses on the behavior and nervous system transmission of laboratory mice. Nervous transmission by electrical impulse can be measured in isolated brain cells, a system that is also convenient to study the effect of stress by adding small amounts of toxins to the fluids bathing the cultures. By these means, the project aims to extend the boundaries of what is considered "prion disease."

Funding: $520,500

http://www.prioninstitute.ca/index.php?page=webpages&menucat=42&id=26&action=displaypage&side=1


Unfolding the Prion Mystery Building and Growing Research Expertise in Alberta Year 4 2008-2009 Annual Report

Dr. David Westaway, University of Alberta Extending the spectrum of prionopathies to amyotrophic lateral sclerosis (ALS) and autism Dr. Westaway’s study aims to extend the boundaries of what is considered prion disease. His project takes the chemistry of the prion protein into the territory of nervous system diseases such as ALS (Lou Gehrig’s disease) and socialization disorder diseases such as autism. These brain diseases are at least 1,000 times more common than diseases currently accepted as prion related. Dr. Westaway hypothesizes that a different type of protein misfolding may operate in brain diseases such as Lou Gehrig’s and autism. This type of protein misfolding may occur in response to stresses in the brain. Unlike misfolded prions, other misfolded proteins may be noninfectious and not viable outside of the affected animal. Dr. Westaway’s research team will investigate these hypotheses by inducing changes in the brain cells of laboratory mice, measuring the resulting electrical impulses in the animals’ nervous systems and analyzing the effect on behaviour. Because nervous transmission by electrical impulse can be measured in isolated brain cells, adding small amounts of toxins to the fluids bathing the cell cultures will make it possible to study the effect of stress. The results could lead to new ways of thinking about nervous system disorders.

http://www.prioninstitute.ca/forms/WEBSITE%20AR.pdf




102

Causes of Death and Neuropathology in Autism Spectrum Disorder: A Medical Examiner Perspective

Kenneth Hutchins1, Mariana Nunez2, Carol Petito2. 1Miami Dade County Medical Examiner Department; 2University of Miami Miller School of Medicine, Department of Pathology

Autism Spectrum Disorder (ASD) is characterized by abnormalities in how patients relate to and communicate with others and their environment . It develops in as many as 1 in 150 children and may be associated with co-morbid disorders including seizures and mental retardation. Because ASD reduces life expectancies, we reviewed autopsy records of 22 consecutive cases from two south Florida Medical Examiner Departments over a 10 year period and correlated cause of death (COD) with clinical history and neuropathology. Patient ages averaged 18±11 yrs and ranged from 3-51 years; 16 were male and 11 were children

http://journals.lww.com/


53

Acute Disseminated Encephalomyelitis in a 16-Year Old Patient After Receiving HPV-Vaccination: A Case Report Xianyuan Song, Francis DiMario Jr., Thomas Ciesielski, Dean Uphoff. Hartford Hospital

Acute acquired demyelination of the central nervous system (CNS) in pediatric patients may lead to a variety of clinical phenotypes depending on the site of demyelination, including optic neuritis, transverse myelitis, neuromyelitis optica, acute disseminated encephalomyelitis (ADEM), and acute multiple sclerosis. Broader definition of ADEM is applied to patients with multiple foci of white matter demyelination. About 50% of cases of ADEM follow viral exanthemata, respiratory and other infections or vaccinations. The clinical course is variable, ranging from a slow progression over weeks to a fulminant course over hours to days. HPV vaccine is only recently developed (approved in 2006), and we have not found any reports documenting the association of administration of HPV vaccine and CNS demyelinating disease (ADEM). We now report a 16-year-old female who presented with acute asymmetric, right greater than left, vision loss. MRI scan and CT showed edema with white matter changes in the right parieto-occipital, parietal junction, and an intrinsic lesion in the optic chiasm and the left optic nerve. No lesions were seen in the spinal cord. She was afebrile and alert. Right parietal biopsy showed acute inflammatory demyelination in the white matter. CSF was negative for oligoclonal bands and anti-NMO antibody, a specific marker for neuromyelitis optica. Other laboratory studies including antinuclear antibody, CMV titer, toxoplasmosis titer, double-stranded DNA, Sjogren antibody, angiotensin-converting enzyme, and antiphospholipid antibody were all normal. The patient's history included 2 injections of HPV vaccine, 2 month and 10 days before her neurological presentation. The clinical, MRI and pathological findings suggest a diagnosis of ADEM. The patient was treated with high dose steroid and IVIG. On discharge, she had some improvement in the right visual fields. ADEM after HPV vaccination is a new occurrence. Here, we report that HPV vaccine may be correlated with the occurrence of ADEM.

http://journals.lww.com/jneuropath/Fulltext/2010/05000/American_Association_of_Neuropathologists,_Inc__.9.aspx




see full text ;


http://bseinquiry.blogspot.com/2008/05/mad-cow-disease-bse-cjd-children.html




Terry S. Singeltary Sr. [flounder@wt.net ]

Monday, January 08,200l 3:03 PM


freas@CBS5055530.CBER.FDA.GOV


CJD/BSE (aka madcow) Human/Animal TSE’s--U.S.--Submission



To Scientific Advisors and Consultants Staff January 2001 Meeting (short version)


Greetings again Dr. Freas and Committee Members,


http://www.fda.gov/ohrms/dockets/ac/01/slides/3681s2_09.pdf





BELOW, PAGE 1 ACTUALLY STARTS ON PAGE 13, then when you get to the bottom, part 3 starts at the top.........TSS


From: Terry S. Singeltary Sr.

To: FREAS@CBER.FDA.GOV

Cc: william.freas@fda.hhs.gov ; rosanna.harvey@fda.hhs.gov

Sent: Friday, December 01, 2006 2:59 PM

Subject: Re: TSE advisory committee for the meeting December 15, 2006 [TSS SUBMISSION

snip...

ONE FINAL COMMENT PLEASE, (i know this is long Dr. Freas but please bear with me)

THE USA is in a most unique situation, one of unknown circumstances with human and animal TSE. THE USA has the most documented TSE in different species to date, with substrains growing in those species (BSE/BASE in cattle and CWD in deer and elk, there is evidence here with different strains), and we know that sheep scrapie has over 20 strains of the typical scrapie with atypical scrapie documented and also BSE is very likely to have passed to sheep. all of which have been rendered and fed back to animals for human and animal consumption, a frightening scenario. WE do not know the outcome, and to play with human life around the globe with the very likely TSE tainted blood from the USA, in my opinion is like playing Russian roulette, of long duration, with potential long and enduring consequences, of which once done, cannot be undone.

These are the facts as i have come to know through daily and extensive research of TSE over 9 years, since 12/14/97. I do not pretend to have all the answers, but i do know to continue to believe in the ukbsenvcjd only theory of transmission to humans of only this one strain from only this one TSE from only this one part of the globe, will only lead to further failures, and needless exposure to humans from all strains of TSE, and possibly many more needless deaths from TSE via a multitude of proven routes and sources via many studies with primates and rodents and other species. ...

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


snip... 48 pages...




http://www.regulations.gov/fdmspublic/ContentViewer?objectId=09000064801f3413&disposition=attachment&contentType=msw8




Saturday, January 29, 2011

Atypical L-Type Bovine Spongiform Encephalopathy (L-BSE) Transmission to Cynomolgus Macaques, a Non-Human Primate

Jpn. J. Infect. Dis., 64 (1), 81-84, 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/atypical-l-type-bovine-spongiform.html




Tuesday, January 25, 2011

Generation of a new form of human PrPSc in vitro by inter-species transmission from cervids prions

http://chronic-wasting-disease.blogspot.com/2011/01/generation-of-new-form-of-human-prpsc.html




Friday, January 21, 2011

Strain-Specific Barriers against Bovine Prions in Hamsters

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/strain-specific-barriers-against-bovine.html





Wednesday, January 19, 2011

EFSA BIOHAZ Scientific Opinion on the revision of the quantitative risk assessment (QRA) of the BSE risk posed by processed animal proteins (PAPs)

EFSA Journal 2011;9(1):1947

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-biohaz-scientific-opinion-on.html





Wednesday, January 19, 2011

EFSA and ECDC review scientific evidence on possible links between TSEs in animals and humans Webnachricht 19 Januar 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-and-ecdc-review-scientific.html




Tuesday, January 18, 2011

Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/agent-strain-variation-in-human-prion.html




Tuesday, December 14, 2010

Infection control of CJD, vCJD and other human prion diseases in healthcare and community settings part 4, Annex A1, Annex J, UPDATE DECEMBER 2010

http://creutzfeldt-jakob-disease.blogspot.com/2010/12/infection-control-of-cjd-vcjd-and-other.html




strictly NOT private and confidential $$$


Saturday, January 22, 2011

Alzheimer's, Prion, and Neurological disease, and the misdiagnosis there of, a review 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/alzheimers-prion-and-neurological.html




Wednesday, January 5, 2011

ENLARGING SPECTRUM OF PRION-LIKE DISEASES Prusiner Colby et al 2011

Prions

David W. Colby1,* and Stanley B. Prusiner1,2

http://betaamyloidcjd.blogspot.com/2011/01/enlarging-spectrum-of-prion-like.html



*** Thursday, December 23, 2010

Alimentary prion infections: Touch-down in the intestine, Alzheimer, Parkinson disease and TSE mad cow diseases $ The Center for Consumer Freedom

http://betaamyloidcjd.blogspot.com/2010/12/alimentary-prion-infections-touch-down.html



Friday, September 3, 2010

Alzheimer's, Autism, Amyotrophic Lateral Sclerosis, Parkinson's, Prionoids, Prionpathy, Prionopathy, TSE


http://betaamyloidcjd.blogspot.com/2010/09/alzheimers-autism-amyotrophic-lateral.html




http://betaamyloidcjd.blogspot.com/




DID EVERYONE THAT LOST A LOVED ONE FILL OUT THEIR CJD QUESTIONNAIRE FROM THE CDC AND OR THE CJD FOUNDATION ???


Friday, November 30, 2007

CJD QUESTIONNAIRE USA CWRU AND CJD FOUNDATION

http://cjdquestionnaire.blogspot.com/





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

Atypical L-Type Bovine Spongiform Encephalopathy (L-BSE) Transmission to Cynomolgus Macaques, a Non-Human Primate

Jpn. J. Infect. Dis., 64 (1), 81-84, 2011

To see a printable version of the article in the Adobe file format, click this [PDF] link.

Short Communication

Atypical L-Type Bovine Spongiform Encephalopathy (L-BSE) Transmission to Cynomolgus Macaques, a Non-Human Primate

Fumiko Ono, Naomi Tase1, Asuka Kurosawa3, Akio Hiyaoka, Atsushi Ohyama, Yukio Tezuka, Naomi Wada2, Yuko Sato3, Minoru Tobiume3, Ken'ichi Hagiwara4, Yoshio Yamakawa4*, Keiji Terao1, and Tetsutaro Sata3

The Corporation for Production and Research of Laboratory Primates, Tsukuba 305-0843; 1Tsukuba Primate Research Center, National Institute of Biomedical Innovation, Tsukuba 305-0843; 2Department of Veterinary Medicine, Yamaguchi University, Yamaguchi 753-8515; and 3Department of Pathology and 4Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Tokyo 162-8640, Japan

(Received December 9, 2010. Accepted December 22, 2010)

--------------------------------------------------------------------------------

*Corresponding author: Mailing address: Department of Biochemistry and Cell Biology, National Institute of Infectious Diseases, Toyama 1-23-1, Shinjuku-ku, Tokyo 162-8640, Japan. Tel: +81-3-5285-1111 ext. 2127, Fax: +81-3-5285-1157, E-mail: yamakawa@nih.go.jp

--------------------------------------------------------------------------------

SUMMARY: A low molecular weight type of atypical bovine spongiform encephalopathy (L-BSE) was transmitted to two cynomolgus macaques by intracerebral inoculation of a brain homogenate of cattle with atypical BSE detected in Japan. They developed neurological signs and symptoms at 19 or 20 months post-inoculation and were euthanized 6 months after the onset of total paralysis. Both the incubation period and duration of the disease were shorter than those for experimental transmission of classical BSE (C-BSE) into macaques. Although the clinical manifestations, such as tremor, myoclonic jerking, and paralysis, were similar to those induced upon C-BSE transmission, no premonitory symptoms, such as hyperekplexia and depression, were evident. Most of the abnormal prion protein (PrPSc) was confined to the tissues of the central nervous system, as determined by immunohistochemistry and Western blotting. The PrPSc glycoform that accumulated in the monkey brain showed a similar profile to that of L-BSE and consistent with that in the cattle brain used as the inoculant. PrPSc staining in the cerebral cortex showed a diffuse synaptic pattern by immunohistochemistry, whereas it accumulated as fine and coarse granules and/or small plaques in the cerebellar cortex and brain stem. Severe spongiosis spread widely in the cerebral cortex, whereas florid plaques, a hallmark of variant Creutzfeldt-Jakob disease in humans, were observed in macaques inoculated with C-BSE but not in those inoculated with L-BSE.

snip...

To date, 27 cases of L-BSE and 24 cases of H-BSE have been report­ed worldwide (16), thus meaning that the prevalence of atypical BSE is considerably lower than that of C-BSE. However, recent studies showed that L-BSE is easily transmissible to transgenic mice expressing human (17,18) or bovine (19,20) prion protein, as well as to non-human primates (21), with shorter incubation periods than for the transmission of C-BSE to these animals. The virulent nature of L-BSE has stimulated new concern for human public health since the transmis­sion of C-BSE to humans resulted in variant Creutz­feldt-Jakob disease (vCJD) (4-7), a new emergent prion disease.

snip...

Two macaques simultaneously developed neurologi­cal signs and symptoms 19-20 months post-inoculation (mpi) with the brain homogenate of BSEI JP24. The monkeys entered the terminal stage of the disease (total paralysis) at 24-25 mpi, Both the onset and duration of the disease were shorter than those reported for the transmission of C-BSE to macaques by us and other groups (27,28). The clinical manifestations such as tremor, myoclonic jerking, and paralysis were similar to those observed during the transmission of C-BSE to ma- caques, whereas the premonitory abnormal behaviors, such as hyperekplexia and depression, seen upon trans­mission of C-BSE to macaques were not evident (27).

Histopathological analysis and IHC, performed as described previously (29), showed that severe spon­giform changes and the accumulation of Prpsc with various patterns were detectable in the brains of both monkeys (Fig. 1). Vacuolization was profound throughout the cerebral cortex, from the frontal to the occipital lobes (Fig. la). Likewise, synaptic-type Prpsc precipitation (30) was observed in the whole cerebral cortex and basal ganglia by IHC (Figs. Ib and c). Dense precipitates and plaques of Prpsc, which had been ob­served in cattle (JP24) brain (13), were not detected in the cerebrum of the monkeys. Prpsc, in the form of small plaques or coarse granules, was, however, detect­ed in the molecular layer of the cerebellum (Fig. Ie). Despite the severe spongiosis in the cerebral cortex, florid plaques, which are large Prpsc plaques surround­ed by vacuoles, a hallmark ofvCJD (4-7,30) and C-BSE transmission to macaques (27,28), were not observed. The histopathology of the brain was therefore similar to that reported for the brain of L-BSE (BASE)-transmit­ted macaques (21).

snip...

see full text ;

http://www.nih.go.jp/JJID/64/81.pdf


Monday, September 13, 2010

atypical BSE strains and sporadic CJD strains, is there a connection and why shouldn't there be $

http://bse-atypical.blogspot.com/2010/09/atypical-bse-strains-and-sporadic-cjd.html


Monday, September 13, 2010

atypical BSE strains and sporadic CJD strains, is there a connection and why shouldn't there be $ A Surprisingly High Number of the Plaque-Like VV sCJD Subtype Among the Polish sCJD-is There a Connection with BASE?

PPo4-15:

A Surprisingly High Number of the Plaque-Like VV sCJD Subtype Among the Polish sCJD—is There a Connection with BASE?

Beata Sikorska and Pawel P. Liberski Department of Molecular Pathology and Neuropathology; Medical University of Lodz; Lodz, Poland

Recently described bovine amyloidotic spongiform encephalopathy (BASE) or L type BSE—was is overrepresented in Poland (15% of all cases of BSE). Moreover, the number of BASE cases in Poland per million bovines is the highest in Europe. A potential human risk from BASE is evident from experimental transmission to “humanized” transgenic animals and primates. Taking into consideration that non-human primate inoculated with BASE had a shorter incubation period than monkeys infected with classical BSE, and that humanized Tg mice have been found to be highly susceptible to infection with atypical form of BSE, it seems probable that BASE may be more pathogenic for humans than BSE, but the transmitted disease may differ from BSE-derived vCJD. Among 47 cases which have been diagnosed as definite in our laboratory, in 19 cases complete histopathological examination and codon 129 status were available. On the basis of the histological pattern and codon 129 status the cases of sCJD were divided into subtypes according to the Parchi&Gambetti classification. The results are as follows: type 1 (MMorMV)- 42%, type 2 (VV)-32%, type 3 (MV)-10.5%, type 4c (MM)- 10.5% and type 5 (VV)-5 %. Although the number of cases is too low to conclude a significantly different distribution of sCJD subtypes in Polish population those data show surprisingly high number of the plaque-like VV sCJD subtype. Interestingly, it was shown before that Tg mice inoculated with BASE showed granular and plaque-like aggregates or PrPSc in brains resembling those observed in VV2 subtype of sCJD.

PPo2-26:

Transmission of Classical and Atypical (L-type) Bovine Spongiform Encephalopathy (BSE) Prions to Cynomolgus macaques

Fumiko Ono,1 Yoshio Yamakawa,2 Minoru Tobiume,3 Yuko Sato,3 Harutaka Katano,3 Kenichi Hagiwara,2 Iori Itagaki,1 Akio Hiyaoka,1 Katuhiko Komatuzaki,1 Yasunori Emoto,1 Hiroaki Shibata,4 Yuichi Murayama,5 Keiji Terao,4 Yasuhiro Yasutomi4 and Tetsutaro Sata3

1The Corporation for Production and Research of Laboratory Primates; Tsukuba City, Japan; 2Departments of Cell Biology and Biochemistry; and 3Pathology; National Institute of Infectious Diseases; Tokyo, Japan; 4Tsukuba Primate Research Center; National Institute of Biomedical Innovation; Tsukuba City, Japan; 5Prion Disease Research Team; National Institute of Animal Health; Tsukuba City, Japan

Key words: L-type BSE, cBSE, cynomolgus macaques, transmission

BSE prion derived from classical BSE (cBSE) or L-type BSE was characterized by inoculation into the brain of cynomolgus macaques. The neurologic manifestation was developed in all cynomolgus macaques at 27–43 months after intracerebral inoculation of brain homogenate from cBSE-affected cattle (BSE JP/6). Second transmission of cBSE from macaque to macaque shortened incubation period to 13–18 months. cBSE-affected macaques showed the similar clinical signs including hyperekplexia, tremor and paralysis in both primary and second transmission.

Two macaques were intracerebrally inoculated brain homogenate from the L-type BSE-affected cattle (BSE JP/24). The incubation periods were 19–20 months in primary transmission.

The clinical course of the L-type BSE-affected macaques differed from that in cBSE-affected macaques in the points of severe myoclonus without hyperekplexia. The glycoform profile of PrPSc detected in macaque CNS was consistent with original pattern of either cBSE or L-typeBSE PrPSc, respectively. Although severe spongiform change in the brain was remarkable in all BSE-affected macaques, severe spongiform spread widely in cerebral cortex in L-type BSE-affected macaques. Heavy accumulation of PrPSc surrounded by vacuola formed florid plaques in cerebral cortex of cBSE-affected macaques. Deposit of PrPSc in L-type BSE-affected macaque was weak and diffuse synaptic pattern in cerebrum, but large PrPSc plaques were evident at cerebellum. MRI analysis, T2, T1, DW and flair sequences, at the time of autopsy revealed that brain atrophy and dilatation of cerebral ventricles were significantly severe in L-type BSE-affected macaques. These results suggest that L-type BSE is more virulent strain to primates comparing to cBSE.

SP1-4:

Evidence from Molecular Strain Typing

Gianluigi Zanusso Department of Neurological and Visual Sciences; Section of Clinical Neurology; University of Verona; Verona, Italy

Key words: molecular analysis, strain typing, atypical BSE, CJD

In 2001, active surveillance for bovine spongiform encephalopathy (BSE) led to the discovery of atypical BSE phenotypes in aged cattle distinct from classical BSE (C-type). These atypical BSE cases had been classified as low L-type (BASE) or high H-type BSE based on the molecular mass and the degree of glycosylation of of the pathological prion protein (PrPSc). Transmission studies in TgBov mice showed that H-type BSE, C-type BSE and BASE behave as distinct prion strains with different incubation periods, PrPSc molecular patterns and pathological phenotypes. A still unclear issue concerns the potential transmissibility and phenotypes of atypical BSEs in humans. We previously indicated that BASE was similar to a distinct subgroup of sporadic form of Creutzfeldt-Jakob disease (sCJD) MV2, based on molecular similarities and on neuropathological pattern of PrP deposition. To investigate a possible link between BASE and sCJD, Kong et al. and Comoy et al. experimentally inoculated TgHu mice (129MM) and a non-human primate respectively, showing in both models that BASE was more virulent compare to BSE. Further, non-human primate reproduced a clinical phenotype resembling to that of sCJD subtype MM2. Here, we presented a comparative analysis of the biochemical fingerprints of PrPSc between the different sCJD subtypes and animal TSEs and after experimental transmission to animals.

http://www.prion2010.org/bilder/prion_2010_program_latest_w_posters_4_.pdf?139&PHPSESSID=a30a38202cfec579000b77af81be3099


Opinion of the Scientific Steering Committee on the GEOGRAPHICAL RISK OF BOVINE SPONGIFORM ENCEPHALOPATHY (GBR) in POLAND Adopted on 30/03/2001

It is concluded that it is likely but not confirmed that one or several cattle that are (pre-clinically or clinically) infected with the BSE agent are currently present in the domestic herd of Poland (GBR III).

http://ec.europa.eu/food/fs/sc/ssc/out185_en.pdf



http://bse-atypical.blogspot.com/2010/09/atypical-bse-strains-and-sporadic-cjd.html



Atypical BSE (BASE) Transmitted from Asymptomatic Aging Cattle to a Primate

Emmanuel E. Comoy1*, Cristina Casalone2, Nathalie Lescoutra-Etchegaray1, Gianluigi Zanusso3, Sophie Freire1, Dominique Marcé1, Frédéric Auvré1, Marie-Magdeleine Ruchoux1, Sergio Ferrari3, Salvatore Monaco3, Nicole Salès4, Maria Caramelli2, Philippe Leboulch1,5, Paul Brown1, Corinne I. Lasmézas4, Jean-Philippe Deslys1

1 Institute of Emerging Diseases and Innovative Therapies, CEA, Fontenay-aux-Roses, France, 2 Istituto Zooprofilattico Sperimentale del Piemonte, Turin, Italy, 3 Policlinico G.B. Rossi, Verona, Italy, 4 Scripps Florida, Jupiter, Florida, United States of America, 5 Genetics Division, Brigham & Women's Hospital, Harvard Medical School, Boston, Massachusetts, United States of America

Abstract Top Background Human variant Creutzfeldt-Jakob Disease (vCJD) results from foodborne transmission of prions from slaughtered cattle with classical Bovine Spongiform Encephalopathy (cBSE). Atypical forms of BSE, which remain mostly asymptomatic in aging cattle, were recently identified at slaughterhouses throughout Europe and North America, raising a question about human susceptibility to these new prion strains.

Methodology/Principal Findings Brain homogenates from cattle with classical BSE and atypical (BASE) infections were inoculated intracerebrally into cynomolgus monkeys (Macacca fascicularis), a non-human primate model previously demonstrated to be susceptible to the original strain of cBSE. The resulting diseases were compared in terms of clinical signs, histology and biochemistry of the abnormal prion protein (PrPres). The single monkey infected with BASE had a shorter survival, and a different clinical evolution, histopathology, and prion protein (PrPres) pattern than was observed for either classical BSE or vCJD-inoculated animals. Also, the biochemical signature of PrPres in the BASE-inoculated animal was found to have a higher proteinase K sensitivity of the octa-repeat region. We found the same biochemical signature in three of four human patients with sporadic CJD and an MM type 2 PrP genotype who lived in the same country as the infected bovine.

Conclusion/Significance Our results point to a possibly higher degree of pathogenicity of BASE than classical BSE in primates and also raise a question about a possible link to one uncommon subset of cases of apparently sporadic CJD. Thus, despite the waning epidemic of classical BSE, the occurrence of atypical strains should temper the urge to relax measures currently in place to protect public health from accidental contamination by BSE-contaminated products.

Citation: Comoy EE, Casalone C, Lescoutra-Etchegaray N, Zanusso G, Freire S, et al. (2008) Atypical BSE (BASE) Transmitted from Asymptomatic Aging Cattle to a Primate. PLoS ONE 3(8): e3017. doi:10.1371/journal.pone.0003017

Editor: Neil Mabbott, University of Edinburgh, United Kingdom

Received: April 24, 2008; Accepted: August 1, 2008; Published: August 20, 2008

Copyright: © 2008 Comoy et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.

Funding: This work has been supported by the Network of Excellence NeuroPrion.

Competing interests: CEA owns a patent covering the BSE diagnostic tests commercialized by the company Bio-Rad.

* E-mail: emmanuel.comoy@cea.fr

http://www.plosone.org/article/info:doi/10.1371/journal.pone.0003017


Session I - Prions: Structure, Strain and Detection (II)

Searching for BASE Strain Signature in Sporadic Creutzfedlt-Jakob Disease

Gianluigi Zanusso

Department of Neurological and Visual Sciences, Section of Clinical Neurology University of Verona, Verona, Italy.

Bovine amyloidotic spongiform encephalopathy (BASE) is a newly recognized form of bovine prion disease, which was originally detected in Italy in 2004 as an effect of active surveillance. BASE or BSE L-type (L is referred to the lower electrophoretic PrPSc migration than classical BSE) has now been reported in several countries, including Japan. All field cases of BASE were older than 8 years and neurologically normal at the time of slaughtered. By experimental transmission, we defined the disease phenotype of cattle BASE, which is quite distinct from that seen in typical BSE and characterized by mental dullness and amyotrophy. Surprisingly, following intraspecies and interspecies transmission the incubation period of BASE was shorter than BSE. The relatively easy transmission of BASE isolate as well as the molecular similarity with sporadic Creutzfeldt-Jakob disease (sCJD) have raised concern regarding its potential passage to humans. Tg humanized mice Met/Met at codon 129 challenged with both BSE and BASE isolates, showed a resistance to BSE but a susceptibility to BASE at a 60% rate; in addition, BASE-inoculated Cynomolgus (129 Met/Met) had shorter incubation periods than BSE-inoculated primates. In this study we compared the biochemical properties of PrPSc in Cynomolgus and in TgHu Met/Met mice challenged with BSE and BASE strains, by conventional SDS-PAGE analysis and 2D separation. The results obtained disclose distinct conformational changes in PrPSc, which are dependent on the inoculated host but not on the codon 129 genotype.

This work was supported by Neuroprion contract n. FOOD CT 2004 -506579 (NOE)

http://www.istitutoveneto.it/prion_09/Abstracts_09.pdf


P02.35

Molecular Features of the Protease-resistant Prion Protein (PrPres) in H-type BSE

Biacabe, A-G1; Jacobs, JG2; Gavier-Widén, D3; Vulin, J1; Langeveld, JPM2; Baron, TGM1 1AFSSA, France; 2CIDC-Lelystad, Netherlands; 3SVA, Sweden

Western blot analyses of PrPres accumulating in the brain of BSE-infected cattle have demonstrated 3 different molecular phenotypes regarding to the apparent molecular masses and glycoform ratios of PrPres bands. We initially described isolates (H-type BSE) essentially characterized by higher PrPres molecular mass and decreased levels of the diglycosylated PrPres band, in contrast to the classical type of BSE. This type is also distinct from another BSE phenotype named L-type BSE, or also BASE (for Bovine Amyloid Spongiform Encephalopathy), mainly characterized by a low representation of the diglycosylated PrPres band as well as a lower PrPres molecular mass. Retrospective molecular studies in France of all available BSE cases older than 8 years old and of part of the other cases identified since the beginning of the exhaustive surveillance of the disease in 20001 allowed to identify 7 H-type BSE cases, among 594 BSE cases that could be classified as classical, L- or H-type BSE. By Western blot analysis of H-type PrPres, we described a remarkable specific feature with antibodies raised against the C-terminal region of PrP that demonstrated the existence of a more C-terminal cleaved form of PrPres (named PrPres#2 ), in addition to the usual PrPres form (PrPres #1). In the unglycosylated form, PrPres #2 migrates at about 14 kDa, compared to 20 kDa for PrPres #1. The proportion of the PrPres#2 in cattle seems to by higher compared to the PrPres#1. Furthermore another PK-resistant fragment at about 7 kDa was detected by some more N-terminal antibodies and presumed to be the result of cleavages of both N- and C-terminal parts of PrP. These singular features were maintained after transmission of the disease to C57Bl/6 mice. The identification of these two additional PrPres fragments (PrPres #2 and 7kDa band) reminds features reported respectively in sporadic Creutzfeldt-Jakob disease and in Gerstmann-Sträussler-Scheinker (GSS) syndrome in humans.

http://www.neuroprion.com/pdf_docs/conferences/prion2007/abstract_book.pdf


Thursday, October 07, 2010

Experimental Transmission of H-type Bovine Spongiform Encephalopathy to Bovinized Transgenic Mice

Thursday, October 07, 2010 Experimental Transmission of H-type Bovine Spongiform Encephalopathy to Bovinized Transgenic Mice

Vet Pathol 0300985810382672, first published on October 4, 2010

Experimental Transmission of H-type Bovine Spongiform Encephalopathy to Bovinized Transgenic Mice

H. Okada okadahi@affrc.go.jp Prion Disease Research Center, National Institute of Animal Health, Tsukuba, K. Masujin Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Y. Imamaru Prion Disease Research Center, National Institute of Animal Health, Tsukuba, M. Imamura Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Y. Matsuura Prion Disease Research Center, National Institute of Animal Health, Tsukuba, S. Mohri Prion Disease Research Center, National Institute of Animal Health, Tsukuba, S. Czub Animal Disease Research Institute, Canadian Food Inspection Agency, T. Yokoyama Prion Disease Research Center, National Institute of Animal Health, Tsukuba,

Abstract

To characterize the biological and biochemical properties of H-type bovine spongiform encephalopathy (BSE), a transmission study with a Canadian H-type isolate was performed with bovinized transgenic mice (TgBoPrP), which were inoculated intracerebrally with brain homogenate from cattle with H-type BSE. All mice exhibited characteristic neurologic signs, and the subsequent passage showed a shortened incubation period. The distribution of disease-associated prion protein (PrPSc) was determined by immunohistochemistry, Western blot, and paraffin-embedded tissue (PET) blot. Biochemical properties and higher molecular weight of the glycoform pattern were well conserved within mice. Immunolabeled granular PrPSc, aggregates, and/or plaque-like deposits were mainly detected in the following brain locations: septal nuclei, subcallosal regions, hypothalamus, paraventricular nucleus of the thalamus, interstitial nucleus of the stria terminalis, and the reticular formation of the midbrain. Weak reactivity was detected by immunohistochemistry and PET blot in the cerebral cortex, most thalamic nuclei, the hippocampus, medulla oblongata, and cerebellum. These findings indicate that the H-type BSE prion has biological and biochemical properties distinct from those of C-type and L-type BSE in TgBoPrP mice, which suggests that TgBoPrP mice constitute a useful animal model to distinguish isolates from BSE-infected cattle.

© 2010 Sage Publications, Inc.

http://vet.sagepub.com/content/early/2010/10/02/0300985810382672.abstract



let's take a closer look at this new prionpathy or prionopathy, and then let's look at the g-h-BSEalabama mad cow.



This new prionopathy in humans? the genetic makeup is IDENTICAL to the g-h-BSEalabama mad cow, the only _documented_ mad cow in the world to date like this, ......wait, it get's better. this new prionpathy is killing young and old humans, with LONG DURATION from onset of symptoms to death, and the symptoms are very similar to nvCJD victims, OH, and the plaques are very similar in some cases too, bbbut, it's not related to the g-h-BSEalabama cow, WAIT NOW, it gets even better, the new human prionpathy that they claim is a genetic TSE, has no relation to any gene mutation in that family. daaa, ya think it could be related to that mad cow with the same genetic make-up ??? there were literally tons and tons of banned mad cow protein in Alabama in commerce, and none of it transmitted to cows, and the cows to humans there from ??? r i g h t $$$

ALABAMA MAD COW g-h-BSEalabama

In this study, we identified a novel mutation in the bovine prion protein gene (Prnp), called E211K, of a confirmed BSE positive cow from Alabama, United States of America. This mutation is identical to the E200K pathogenic mutation found in humans with a genetic form of CJD. This finding represents the first report of a confirmed case of BSE with a potential pathogenic mutation within the bovine Prnp gene. We hypothesize that the bovine Prnp E211K mutation most likely has caused BSE in "the approximately 10-year-old cow" carrying the E221K mutation.

http://www.plospathogens.org/article/info%3Adoi%2F10.1371%2Fjournal.ppat.1000156


http://www.plospathogens.org/article/fetchObjectAttachment.action?uri=info%3Adoi%2F10.1371%2Fjournal.ppat.1000156&representation=PDF


Saturday, August 14, 2010

BSE Case Associated with Prion Protein Gene Mutation (g-h-BSEalabama) and VPSPr PRIONPATHY

(see mad cow feed in COMMERCE IN ALABAMA...TSS)

http://prionpathy.blogspot.com/2010/08/bse-case-associated-with-prion-protein.html


Tuesday, August 03, 2010

Variably protease-sensitive prionopathy: A new sporadic disease of the prion protein

http://creutzfeldt-jakob-disease.blogspot.com/2010/08/variably-protease-sensitive-prionopathy.html


Monday, August 9, 2010

Variably protease-sensitive prionopathy: A new sporadic disease of the prion protein or just more PRIONBALONEY ?

http://prionunitusaupdate2008.blogspot.com/2010/08/variably-protease-sensitive-prionopathy.html


***+++***

Thursday, July 10, 2008

A Novel Human Disease with Abnormal Prion Protein Sensitive to Protease update July 10, 2008 Friday, June 20, 2008

http://cjdmadcowbaseoct2007.blogspot.com/2008/07/novel-human-disease-with-abnormal-prion.html


TSE

http://transmissiblespongiformencephalopathy.blogspot.com/


Wednesday, July 28, 2010

Atypical prion proteins and IBNC in cattle DEFRA project code SE1796 FOIA Final report

http://bse-atypical.blogspot.com/2010/07/atypical-prion-proteins-and-ibnc-in.html


IBNC

"All of the 15 cattle tested showed that the brains had abnormally accumulated prion protein."

Saturday, February 28, 2009

NEW RESULTS ON IDIOPATHIC BRAINSTEM NEURONAL CHROMATOLYSIS "All of the 15 cattle tested showed that the brains had abnormally accumulated PrP" 2009

SEAC 102/2

http://bse-atypical.blogspot.com/2009/02/new-results-on-idiopathic-brainstem.html



Seven main threats for the future linked to prions

The NeuroPrion network has identified seven main threats for the future linked to prions.

First threat

The TSE road map defining the evolution of European policy for protection against prion diseases is based on a certain numbers of hypotheses some of which may turn out to be erroneous. In particular, a form of BSE (called atypical Bovine Spongiform Encephalopathy), recently identified by systematic testing in aged cattle without clinical signs, may be the origin of classical BSE and thus potentially constitute a reservoir, which may be impossible to eradicate if a sporadic origin is confirmed. Also, a link is suspected between atypical BSE and some apparently sporadic cases of Creutzfeldt-Jakob disease in humans. These atypical BSE cases constitute an unforeseen first threat that could sharply modify the European approach to prion diseases.

Second threat

snip...

http://www.neuroprion.org/en/np-neuroprion.html


Wednesday, March 31, 2010

Atypical BSE in Cattle

To date the OIE/WAHO assumes that the human and animal health standards set out in the BSE chapter for classical BSE (C-Type) applies to all forms of BSE which include the H-type and L-type atypical forms. This assumption is scientifically not completely justified and accumulating evidence suggests that this may in fact not be the case. Molecular characterization and the spatial distribution pattern of histopathologic lesions and immunohistochemistry (IHC) signals are used to identify and characterize atypical BSE. Both the L-type and H-type atypical cases display significant differences in the conformation and spatial accumulation of the disease associated prion protein (PrPSc) in brains of afflicted cattle. Transmission studies in bovine transgenic and wild type mouse models support that the atypical BSE types might be unique strains because they have different incubation times and lesion profiles when compared to C-type BSE. When L-type BSE was inoculated into ovine transgenic mice and Syrian hamster the resulting molecular fingerprint had changed, either in the first or a subsequent passage, from L-type into C-type BSE. In addition, non-human primates are specifically susceptible for atypical BSE as demonstrated by an approximately 50% shortened incubation time for L-type BSE as compared to C-type. Considering the current scientific information available, it cannot be assumed that these different BSE types pose the same human health risks as C-type BSE or that these risks are mitigated by the same protective measures.

This study will contribute to a correct definition of specified risk material (SRM) in atypical BSE. The incumbent of this position will develop new and transfer existing, ultra-sensitive methods for the detection of atypical BSE in tissue of experimentally infected cattle.

http://www.prionetcanada.ca/detail.aspx?menu=5&dt=293380&app=93&cat1=387&tp=20&lk=no&cat2


snip...

please see all seven threats listed in the USA, and more...FULL TEXT ;


Thursday, August 12, 2010

Seven main threats for the future linked to prions

http://prionpathy.blogspot.com/2010/08/seven-main-threats-for-future-linked-to.html


http://prionpathy.blogspot.com/



Evaluation of the Human Transmission Risk of an Atypical Bovine Spongiform Encephalopathy Prion Strain

Qingzhong Kong,1* Mengjie Zheng,1 Cristina Casalone,2 Liuting Qing,1 Shenghai Huang,1? Bikram Chakraborty,1 Ping Wang,1 Fusong Chen,1 Ignazio Cali,1 Cristiano Corona,2 Francesca Martucci,2 Barbara Iulini,2 Pierluigi Acutis,2 Lan Wang,1 Jingjing Liang,1 Meiling Wang,1 Xinyi Li,1 Salvatore Monaco,3 Gianluigi Zanusso,3 Wen-Quan Zou,1 Maria Caramelli,2 and Pierluigi Gambetti1* Department of Pathology, Case Western Reserve University, Cleveland, Ohio 44106,1 CEA, Istituto Zooprofilattico Sperimentale, 10154 Torino, Italy,2 Department of Neurological and Visual Sciences, University of Verona, 37134 Verona, Italy3 *Corresponding author. Mailing address: Department of Pathology, Case Western Reserve University, Cleveland, OH 44106. Phone for Pierluigi Gambetti: (216) 368-0586. Fax: (216) 368-2546. E-mail: pxg13@case.edu . Phone for Qingzhong Kong: (216) 368-1756. Fax: (216) 368-2546. E-mail: qxk2@case.edu ?Present address: Department of Patient Education and Health Information, Cleveland Clinic Foundation, Cleveland, OH 44195. Received November 30, 2007; Accepted January 16, 2008.

Bovine spongiform encephalopathy (BSE), the prion disease in cattle, was widely believed to be caused by only one strain, BSE-C. BSE-C causes the fatal prion disease named new variant Creutzfeldt-Jacob disease in humans. Two atypical BSE strains, bovine amyloidotic spongiform encephalopathy (BASE, also named BSE-L) and BSE-H, have been discovered in several countries since 2004; their transmissibility and phenotypes in humans are unknown. We investigated the infectivity and human phenotype of BASE strains by inoculating transgenic (Tg) mice expressing the human prion protein with brain homogenates from two BASE strain-infected cattle. Sixty percent of the inoculated Tg mice became infected after 20 to 22 months of incubation, a transmission rate higher than those reported for BSE-C. A quarter of BASE strain-infected Tg mice, but none of the Tg mice infected with prions causing a sporadic human prion disease, showed the presence of pathogenic prion protein isoforms in the spleen, indicating that the BASE prion is intrinsically lymphotropic. The pathological prion protein isoforms in BASE strain-infected humanized Tg mouse brains are different from those from the original cattle BASE or sporadic human prion disease. Minimal brain spongiosis and long incubation times are observed for the BASE strain-infected Tg mice. These results suggest that in humans, the BASE strain is a more virulent BSE strain and likely lymphotropic.

http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2268471



P26 TRANSMISSION OF ATYPICAL BOVINE SPONGIFORM ENCEPHALOPATHY (BSE) IN HUMANIZED MOUSE MODELS

Liuting Qing1, Fusong Chen1, Michael Payne1, Wenquan Zou1, Cristina Casalone2, Martin Groschup3, Miroslaw Polak4, Maria Caramelli2, Pierluigi Gambetti1, Juergen Richt5*, and Qingzhong Kong1 1Department of Pathology, Case Western Reserve University, Cleveland, OH 44106, USA; 2CEA, Istituto Zooprofilattico Sperimentale, Italy; 3Friedrich-Loeffler-Institut, Germany; 4National Veterinary Research Institute, Poland; 5Kansas State University, Diagnostic Medicine/Pathobiology Department, Manhattan, KS 66506, USA. *Previous address: USDA National Animal Disease Center, Ames, IA 50010, USA

Classical BSE is a world-wide prion disease in cattle, and the classical BSE strain (BSE-C) has led to over 200 cases of clinical human infection (variant CJD). Two atypical BSE strains, BSE-L (also named BASE) and BSE-H, have been discovered in three continents since 2004. The first case of naturally occurring BSE with mutated bovine PrP gene (termed BSE-M) was also found in 2006 in the USA. The transmissibility and phenotypes of these atypical BSE strains/isolates in humans were unknown. We have inoculated humanized transgenic mice with classical and atypical BSE strains (BSE-C, BSE-L, BSE-H) and the BSE-M isolate. We have found that the atypical BSE-L strain is much more virulent than the classical BSE-C. The atypical BSE-H strain is also transmissible in the humanized transgenic mice with distinct phenotype, but no transmission has been observed for the BSE-M isolate so far.

III International Symposium on THE NEW PRION BIOLOGY: BASIC SCIENCE, DIAGNOSIS AND THERAPY 2 - 4 APRIL 2009, VENEZIA (ITALY)

http://www.istitutoveneto.it/prion_09/Abstracts_09.pdf



Monday, October 19, 2009

Atypical BSE, BSE, and other human and animal TSE in North America Update October 19, 2009

snip...

I ask Professor Kong ;

Thursday, December 04, 2008 3:37 PM Subject: RE: re--Chronic Wating Disease (CWD) and Bovine Spongiform Encephalopathies (BSE): Public Health Risk Assessment


''IS the h-BSE more virulent than typical BSE as well, or the same as cBSE, or less virulent than cBSE? just curious.....''


Professor Kong reply ;


.....snip


''As to the H-BSE, we do not have sufficient data to say one way or another, but we have found that H-BSE can infect humans. I hope we could publish these data once the study is complete.


Thanks for your interest.''


Best regards,


Qingzhong Kong, PhD Associate Professor Department of Pathology Case Western Reserve University Cleveland, OH 44106 USA



Rare BSE mutation raises concerns over risks to public health

SIR — Atypical forms (known as H- and L-type) of bovine spongiform encephalopathy (BSE) have recently appeared in several European countries as well as in Japan, Canada and the United States. This raises the unwelcome possibility that variant Creutzfeldt–Jakob disease (vCJD) could increase in the human population. Of the atypical BSE cases tested so far, a mutation in the prion protein gene (PRNP) has been detected in just one, a cow in Alabama with BSE; her healthy calf also carried the mutation (J. A. Richt and S. M. Hall PLoS Pathog. 4, e1000156; 2008). This raises the possibility that the disease could occasionally be genetic in origin. Indeed, the report of the UK BSE Inquiry in 2000 suggested that the UK epidemic had most likely originated from such a mutation and argued against the scrapierelated assumption. Such rare potential pathogenic PRNP mutations could occur in countries at present considered to be free of BSE, such as Australia and New Zealand. So it is important to maintain strict surveillance for BSE in cattle, with rigorous enforcement of the ruminant feed ban (many countries still feed ruminant proteins to pigs). Removal of specified risk material, such as brain and spinal cord, from cattle at slaughter prevents infected material from entering the human food chain. Routine genetic screening of cattle for PRNP mutations, which is now available, could provide additional data on the risk to the public. Because the point mutation identified in the Alabama animals is identical to that responsible for the commonest type of familial (genetic) CJD in humans, it is possible that the resulting infective prion protein might cross the bovine–human species barrier more easily. Patients with vCJD continue to be identified. The fact that this is happening less often should not lead to relaxation of the controls necessary to prevent future outbreaks. Malcolm A. Ferguson-Smith Cambridge University Department of Veterinary Medicine, Madingley Road, Cambridge CB3 0ES, UK e-mail: maf12@cam.ac.uk Jürgen A. Richt College of Veterinary Medicine, Kansas State University, K224B Mosier Hall, Manhattan, Kansas 66506-5601, USA

NATUREVol 45726 February 2009

http://www.nature.com/nature/journal/v457/n7233/full/4571079b.html


Our findings demonstrate that cervid PrPSc, upon strain adaptation by serial passages in vitro or in cervid transgenic mice, is capable of converting human PrPC to produce PrPSc with unique biochemical properties, likely representing a new human prion strain. The newly generated CWD-huPrPSc material has been inoculated into transgenic mice expressing human PrP to study infectivity and disease phenotype and this data will be published elsewhere.

http://www.jbc.org/content/early/2011/01/04/jbc.M110.198465.long


Tuesday, January 25, 2011

Generation of a new form of human PrPSc in vitro by inter-species transmission from cervids prions

http://chronic-wasting-disease.blogspot.com/2011/01/generation-of-new-form-of-human-prpsc.html


WHAT ABOUT CWD AND LIVESTOCK, especially, second passage ;


Title: Experimental Second Passage of Chronic Wasting Disease (Cwd(mule Deer)) Agent to Cattle

Authors

Hamir, Amirali Kunkle, Robert Miller, Janice - ARS RETIRED Greenlee, Justin Richt, Juergen

Submitted to: Journal of Comparative Pathology Publication Type: Peer Reviewed Journal Publication Acceptance Date: July 25, 2005 Publication Date: January 1, 2006 Citation: Hamir, A.N., Kunkle, R.A., Miller, J.M., Greenlee, J.J., Richt, J.A. 2006. Experimental second passage of chronic wasting disease (CWD(mule deer)) agent to cattle. Journal of Comparative Pathology. 134(1):63-69.

Interpretive Summary: To compare the findings of experimental first and second passage of chronic wasting disease (CWD) in cattle, 6 calves were inoculated into the brain with CWD-mule deer agent previously (first) passaged in cattle. Two other uninoculated calves served as controls. Beginning 10-12 months post inoculation (PI), all inoculates lost appetite and weight. Five animals subsequently developed clinical signs of central nervous system (CNS) abnormality. By 16.5 months PI, all cattle had been euthanized because of poor prognosis. None of the animals showed microscopic lesions of spongiform encephalopathy (SE) but the CWD agent was detected in their CNS tissues by 2 laboratory techniques (IHC and WB). These findings demonstrate that inoculated cattle amplify CWD agent but also develop clinical CNS signs without manifestation of microscopic lesions of SE. This situation has also been shown to occur following inoculation of cattle with another TSE agent, namely, sheep scrapie. The current study confirms previous work that indicates that the diagnostic tests currently used for confirmation of bovine spongiform encephalopathy (BSE) in the U.S. would detect CWD in cattle, should it occur naturally. Furthermore, it raises the possibility of distinguishing CWD from BSE in cattle due to the absence of microscopic lesions and a unique multifocal distribution of PrPres, as demonstrated by IHC, which in this study, appears to be more sensitive than the WB. Technical Abstract: To compare clinicopathological findings of first and second passage of chronic wasting disease (CWD) in cattle, a group of calves (n=6) were intracerebrally inoculated with CWD-mule deer agent previously (first) passaged in cattle. Two other uninoculated calves served as controls. Beginning 10-12 months post inoculation (PI), all inoculates lost appetite and lost weight. Five animals subsequently developed clinical signs of central nervous system (CNS) abnormality. By 16.5 months PI, all cattle had been euthanized because of poor prognosis. None of the animals showed microscopic lesions of spongiform encephalopathy (SE) but PrPres was detected in their CNS tissues by immunohistochemistry (IHC) and Western blot (WB) techniques. These findings demonstrate that intracerebrally inoculated cattle not only amplify CWD PrPres but also develop clinical CNS signs without manifestation of morphologic lesions of SE. This situation has also been shown to occur following inoculation of cattle with another TSE agent, scrapie. The current study confirms previous work that indicates the diagnostic techniques currently used for confirmation of bovine spongiform encephalopathy (BSE) in the U.S. would detect CWD in cattle, should it occur naturally. Furthermore, it raises the possibility of distinguishing CWD from BSE in cattle due to the absence of neuropathologic lesions and a unique multifocal distribution of PrPres, as demonstrated by IHC, which in this study, appears to be more sensitive than the WB.

http://www.ars.usda.gov/research/publications/publications.htm?SEQ_NO_115=178318


Wednesday, January 19, 2011

EFSA BIOHAZ Scientific Opinion on the revision of the quantitative risk assessment (QRA) of the BSE risk posed by processed animal proteins (PAPs)

EFSA Journal 2011;9(1):1947

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-biohaz-scientific-opinion-on.html


Monday, January 17, 2011

MAD COW Update on Feed Enforcement Activities to Limit the Spread of BSE January 13, 2011

January 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/mad-cow-update-on-feed-enforcement.html


Thursday, November 18, 2010

Increased susceptibility of human-PrP transgenic mice to bovine spongiform encephalopathy following passage in sheep

http://bse-atypical.blogspot.com/2010/11/increased-susceptibility-of-human-prp.html


Tuesday, January 18, 2011

Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/agent-strain-variation-in-human-prion.html


Thursday, December 23, 2010

Molecular Typing of Protease-Resistant Prion Protein in Transmissible Spongiform Encephalopathies of Small Ruminants, France, 2002–2009 Volume 17, Number 1–January 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2010/12/molecular-typing-of-protease-resistant.html


Wednesday, January 19, 2011

EFSA and ECDC review scientific evidence on possible links between TSEs in animals and humans Webnachricht 19 Januar 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-and-ecdc-review-scientific.html


Friday, January 21, 2011

Strain-Specific Barriers against Bovine Prions in Hamsters

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/strain-specific-barriers-against-bovine.html


Saturday, December 18, 2010

OIE Global Conference on Wildlife Animal Health and Biodiversity - Preparing for the Future (TSE AND PRIONS) Paris (France), 23-25 February 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2010/12/oie-global-conference-on-wildlife.html


Monday, November 30, 2009


USDA AND OIE COLLABORATE TO EXCLUDE ATYPICAL SCRAPIE NOR-98 ANIMAL HEALTH CODE


http://nor-98.blogspot.com/2009/11/usda-and-oie-collaborate-to-exclude.html


http://bseusa.blogspot.com/2010/04/usda-and-oie-out-of-touch-with-risk.html



Tuesday, November 02, 2010

BSE - ATYPICAL LESION DISTRIBUTION (RBSE 92-21367) statutory (obex only) diagnostic criteria CVL 1992

http://bse-atypical.blogspot.com/2010/11/bse-atypical-lesion-distribution-rbse.html


USA

5 Includes 16 cases in which the diagnosis is pending, and 18 inconclusive cases;

6 Includes 21 (19 from 2010) cases with type determination pending in which the diagnosis of vCJD has been excluded.

2010

PLEASE NOTE REFERENCE LINES 5. AND 6.

Monday, August 9, 2010

National Prion Disease Pathology Surveillance Center Cases Examined (July 31, 2010) Year Total Referrals2 Prion Disease Sporadic Familial Iatrogenic vCJD

1996 & earlier 51 33 28 5 0 0

1997 114 68 59 9 0 0

1998 88 52 44 7 1 0

1999 120 72 64 8 0 0

2000 146 103 89 14 0 0

2001 209 119 109 10 0 0

2002 248 149 125 22 2 0

2003 274 176 137 39 0 0

2004 325 186 164 21 0 1(3)

2005 344 194 157 36 1 0

2006 383 197 166 29 0 2(4)

2007 377 214 187 27 0 0

2008 394 231 204 25 0 0

2009 425 259 216 43 0 0

2010 204 124 85 20 0 0

TOTAL 3702(5) 2177(6) 1834 315 4 3

1 Listed based on the year of death or, if not available, on year of referral;

2 Cases with suspected prion disease for which brain tissue and/or blood (in familial cases) were submitted;

3 Disease acquired in the United Kingdom;

4 Disease was acquired in the United Kingdom in one case and in Saudi Arabia in the other case;

5 Includes 16 cases in which the diagnosis is pending, and 18 inconclusive cases;

6 Includes 21 (19 from 2010) cases with type determination pending in which the diagnosis of vCJD has been excluded.

http://www.cjdsurveillance.com/pdf/case-table.pdf


Monday, August 9, 2010

National Prion Disease Pathology Surveillance Center Cases Examined (July 31, 2010)

(please watch and listen to the video and the scientist speaking about atypical BSE and sporadic CJD and listen to Professor Aguzzi)

http://prionunitusaupdate2008.blogspot.com/2010/08/national-prion-disease-pathology.html


Tuesday, December 14, 2010

Infection control of CJD, vCJD and other human prion diseases in healthcare and community settings part 4, Annex A1, Annex J, UPDATE DECEMBER 2010

http://creutzfeldt-jakob-disease.blogspot.com/2010/12/infection-control-of-cjd-vcjd-and-other.html


Saturday, June 13, 2009

Monitoring the occurrence of emerging forms of Creutzfeldt-Jakob disease in the United States 2003 revisited 2009

http://cjdusa.blogspot.com/2009/06/monitoring-occurrence-of-emerging-forms.html


Saturday, January 2, 2010

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

http://prionunitusaupdate2008.blogspot.com/2010/01/human-prion-diseases-in-united-states.html



my comments to PLosone here ;


http://www.plosone.org/annotation/listThread.action?inReplyTo=info%3Adoi%2F10.1371%2Fannotation%2F04ce2b24-613d-46e6-9802-4131e2bfa6fd&root=info%3Adoi%2F10.1371%2Fannotation%2F04ce2b24-613d-46e6-9802-4131e2bfa6fd



14th ICID International Scientific Exchange Brochure -

Final Abstract Number: ISE.114

Session: International Scientific Exchange

Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America

update October 2009

T. Singeltary

Bacliff, TX, USA

Background:

An update on atypical BSE and other TSE in North America. Please remember, the typical U.K. c-BSE, the atypical l-BSE (BASE), and h-BSE have all been documented in North America, along with the typical scrapie's, and atypical Nor-98 Scrapie, and to date, 2 different strains of CWD, and also TME. All these TSE in different species have been rendered and fed to food producing animals for humans and animals in North America (TSE in cats and dogs ?), and that the trading of these TSEs via animals and products via the USA and Canada has been immense over the years, decades.

Methods:

12 years independent research of available data

Results:

I propose that the current diagnostic criteria for human TSEs only enhances and helps the spreading of human TSE from the continued belief of the UKBSEnvCJD only theory in 2009. With all the science to date refuting it, to continue to validate this old myth, will only spread this TSE agent through a multitude of potential routes and sources i.e. consumption, medical i.e., surgical, blood, dental, endoscopy, optical, nutritional supplements, cosmetics etc.

Conclusion:

I would like to submit a review of past CJD surveillance in the USA, and the urgent need to make all human TSE in the USA a reportable disease, in every state, of every age group, and to make this mandatory immediately without further delay. The ramifications of not doing so will only allow this agent to spread further in the medical, dental, surgical arena's. Restricting the reporting of CJD and or any human TSE is NOT scientific. Iatrogenic CJD knows NO age group, TSE knows no boundaries. I propose as with Aguzzi, Asante, Collinge, Caughey, Deslys, Dormont, Gibbs, Gajdusek, Ironside, Manuelidis, Marsh, et al and many more, that the world of TSE Transmissible Spongiform Encephalopathy is far from an exact science, but there is enough proven science to date that this myth should be put to rest once and for all, and that we move forward with a new classification for human and animal TSE that would properly identify the infected species, the source species, and then the route.

http://ww2.isid.org/Downloads/14th_ICID_ISE_Abstracts.pdf



Tuesday, December 14, 2010

Infection control of CJD, vCJD and other human prion diseases in healthcare and community settings part 4, Annex A1, Annex J, UPDATE DECEMBER 2010

http://creutzfeldt-jakob-disease.blogspot.com/2010/12/infection-control-of-cjd-vcjd-and-other.html



HOW many of you recieved a written CJD Questionnaire asking real questions pertaining to route and source (and there are many here in North America) ?


IS every case getting a cjd questionnaire asking real questions ???


Friday, November 30, 2007

CJD QUESTIONNAIRE USA CWRU AND CJD FOUNDATION USA PRION UNIT


http://cjdquestionnaire.blogspot.com/2007/11/cjd-questionnaire.html


TSS

Terry S. Singeltary Sr. P.O. Box 42 Bacliff, Texas USA 77518 flounder9@verizon.net

Declaration of Prion as a Pest Under FIFRA and Amendment of EPA's Regulatory Definition of Pests To Include Prion EPA-HQ-OPP-2010-0427

EPA-HQ-OPP-2010-0427

[Federal Register: January 26, 2011 (Volume 76, Number 17)] [Proposed Rules] [Page 4602-4608] From the Federal Register Online via GPO Access [wais.access.gpo.gov] [DOCID:fr26ja11-30]

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ENVIRONMENTAL PROTECTION AGENCY

40 CFR Part 152

[EPA-HQ-OPP-2010-0427; FRL-8850-4] RIN 2070-AJ26

Declaration of Prion as a Pest Under FIFRA and Amendment of EPA's Regulatory Definition of Pests To Include Prion

AGENCY: Environmental Protection Agency (EPA).

ACTION: Proposed rule.

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SUMMARY: EPA proposes to declare a prion (i.e., proteinaceous infectious particle) a ``pest'' under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA), and to amend its regulations to expressly include prion within the regulatory definition of pest. EPA currently considers a prion to be a pest under FIFRA, so a product intended to reduce the infectivity of any prion on inanimate surfaces (i.e., a ``prion-related product'') is considered to be a pesticide and regulated as such. Any company seeking to distribute or sell a pesticide product regulated under FIFRA must obtain a section 3 registration, section 24(c) registration, or a section 18 emergency exemption before it can be distributed or sold in the United States. This proposed rule would codify the Agency's current interpretation of FIFRA, and provides interested parties the opportunity to comment about how it is adding prion to the list of pests in the regulatory definition of pest. This amendment, together with the formal declaration that a prion is a pest, will eliminate any confusion about the status of prion-related products under FIFRA. Codifying the Agency's current interpretation of FIFRA will not change the manner in which EPA currently regulates prion-related products under FIFRA sections 3, 24(c) and 18. Regulating prion-related products under FIFRA is appropriate for protecting human health and the environment against unreasonable adverse effects and ensuring that such products are effective.

DATES: Comments must be received on or before March 28, 2011.

ADDRESSES: Submit your comments, identified by docket identification (ID) number EPA-HQ-OPP-2010-0427, by one of the following methods: Federal eRulemaking Portal: http://www.regulations.gov. Follow the on-line instructions for submitting comments. Mail: Office of Pesticide Programs (OPP) Regulatory Public Docket (7502P), Environmental Protection Agency, 1200 Pennsylvania Ave., NW., Washington, DC 20460-0001. Delivery: OPP Regulatory Public Docket (7502P), Environmental Protection Agency, Rm. S-4400, One Potomac Yard (South Bldg.), 2777 S. Crystal Dr., Arlington, VA. Deliveries are only accepted during the Docket Facility's normal hours of operation (8:30 a.m. to 4 p.m., Monday through Friday, excluding legal holidays). Special arrangements should be made for deliveries of boxed information. The Docket Facility telephone number is (703) 305-5805. Instructions: Direct your comments to docket ID number EPA-HQ-OPP- 2010-0427. EPA's policy is that all comments received will be included in the docket without change and may be made available on-line at http://www.regulations.gov, including any personal information provided, unless the comment includes information claimed to be Confidential Business Information (CBI) or other information whose disclosure is restricted by statute. Do not submit information that you consider to be CBI or otherwise protected through regulations.gov or e- mail. The regulations.gov website is an ``anonymous access'' system, which means EPA will not know your identity or contact information unless you provide it in the body of your comment. If you send an e- mail comment directly to EPA without going through regulations.gov, your e-mail address will be automatically captured and included as part of the comment that is placed in the docket and made available on the Internet. If you submit an electronic comment, EPA recommends

[[Page 4603]]

that you include your name and other contact information in the body of your comment and with any disk or CD-ROM you submit. If EPA cannot read your comment due to technical difficulties and cannot contact you for clarification, EPA may not be able to consider your comment. Electronic files should avoid the use of special characters, any form of encryption, and be free of any defects or viruses. Docket: All documents in the docket are listed in the docket index available at http://www.regulations.gov. Although listed in the index, some information is not publicly available, e.g., CBI or other information whose disclosure is restricted by statute. Certain other material, such as copyrighted material, is not placed on the Internet and will be publicly available only in hard copy form. Publicly available docket materials are available either in the electronic docket at http://www.regulations.gov, or, if only available in hard copy, at the OPP Regulatory Public Docket in Rm. S-4400, One Potomac Yard (South Bldg.), 2777 S. Crystal Dr., Arlington, VA. The hours of operation of this Docket Facility are from 8:30 a.m. to 4 p.m., Monday through Friday, excluding legal holidays. The Docket Facility telephone number is (703) 305-5805.

FOR FURTHER INFORMATION CONTACT: Jeff Kempter, Antimicrobials Division, Office of Pesticide Programs, Environmental Protection Agency, 1200 Pennsylvania Ave., NW., Washington, DC 20460-0001; telephone number: (703) 305-5448; fax number: (703) 308-6467; e-mail address: kempter.carlton@epa.gov.

SUPPLEMENTARY INFORMATION:

I. General Information

A. Does this action apply to me?

You may be potentially affected by this action if you apply for or own pesticide registrations. Potentially affected entities may include, but are not limited to: Producers of pesticide products (NAICS code 32532). Producers of antimicrobial pesticides (NAICS code 32561). Veterinary testing laboratories (NAICS code 541940). Medical pathology laboratories (NAICS code 621511). Taxidermists, independent (NAICS code 711510). Surgeons (NAICS code 621111). Dental surgeons (NAICS code 621210). Mortician services (NAICS code 812210). Manufacturers of medical tissue devices of human and animal origin (NAICS code undetermined). Manufacturers of other human cellular and tissue products (NAICS code undetermined). Organ banks, body (NAICS code 621991). Plasma, blood, merchant wholesalers (NAICS code 424210). This listing is not intended to be exhaustive, but rather provides a guide for readers regarding entities likely to be affected by this action. Other types of entities not listed in this unit could also be affected. The North American Industrial Classification System (NAICS) codes have been provided to assist you and others in determining whether this action might apply to certain entities. If you have any questions regarding the applicability of this action to a particular entity, consult the person listed under FOR FURTHER INFORMATION CONTACT.

B. What should I consider as I prepare my comments for EPA?

1. Submitting CBI. Do not submit this information to EPA through regulations.gov or e-mail. Clearly mark the part or all of the information that you claim to be CBI. For CBI information in a disk or CD-ROM that you mail to EPA, mark the outside of the disk or CD-ROM as CBI and then identify electronically within the disk or CD-ROM the specific information that is claimed as CBI. In addition to one complete version of the comment that includes information claimed as CBI, a copy of the comment that does not contain the information claimed as CBI must be submitted for inclusion in the public docket. Information so marked will not be disclosed except in accordance with procedures set forth in 40 CFR part 2. 2. Tips for preparing your comments. When submitting comments, remember to: i. Identify the document by docket ID number and other identifying information (subject heading, Federal Register date and page number). ii. Follow directions. The Agency may ask you to respond to specific questions or organize comments by referencing a Code of Federal Regulations (CFR) part or section number. iii. Explain why you agree or disagree; suggest alternatives and substitute language for your requested changes. iv. Describe any assumptions and provide any technical information and/or data that you used. v. If you estimate potential costs or burdens, explain how you arrived at your estimate in sufficient detail to allow for it to be reproduced. vi. Provide specific examples to illustrate your concerns and suggest alternatives. vii. Explain your views as clearly as possible, avoiding the use of profanity or personal threats. viii. Make sure to submit your comments by the comment period deadline identified.

II. Background

A. What action is the Agency taking?

EPA has decided that under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA) a prion is considered to be a pest, and proposes to declare a prion to be a pest and to explicitly include it in the lists of pests in 40 CFR 152.5. These actions would affirm the Agency's authority to regulate products distributed or sold for the purpose of reducing the infectivity of prions on inanimate surfaces (i.e., prion-related products). Prion-related products are currently regulated under FIFRA and subject to all requirements and provisions of the Act based on EPA's September 10, 2003 decision that prions share enough characteristics of an ``other micro-organism'' or ``form of life'' (as those terms are used in FIFRA) to fall within the scope of FIFRA section 2(t) and 40 CFR 152.5(d). This proposal ensures that the regulatory definition reflects the Agency's authority to regulate products distributed or sold for the purpose of reducing the infectivity of prions on inanimate surfaces (i.e., prion-related products). The primary impact of declaring that a prion is a pest and including ``prion'' in the regulatory definition of ``pest'' is to provide regulatory clarity that prion-related products must be registered or exempted under FIFRA sections 3, 24(c), or 18 before such products may be distributed or sold in the United States. Note that not all prions and prion-related products are affected by the proposed rule. Firstly, EPA's regulations at 40 CFR 152.5(d) exclude pests ``* * * in or on living man or other living animals and those on or in processed food or processed animal feed, beverages, drugs * * * and cosmetics.'' Therefore, the proposed rule would not apply to those uses of prion-related products. Secondly, the definition of ``pesticide'' in FIFRA section 2(u) excludes new animal drugs and liquid chemical sterilants intended for use on a critical or semi- critical device. Accordingly, products which fall into those categories would not be covered by the proposed rule.

[[Page 4604]]

B. What is the Agency's authority for taking this action?

This action is issued under the authority of sections 2 through 34 of FIFRA (7 U.S.C. 136-136y).

III. Prion as a Pest Under FIFRA

A. What is a prion?

snip...see full text ;

http://edocket.access.gpo.gov/2011/2011-1636.htm


Friday, August 29, 2008

CREEKSTONE VS USDA COURT OF APPEALS, BUSH SAYS, NO WAY, NO HOW

http://madcowtesting.blogspot.com/2008/08/creekstone-vs-usda-court-of-appeals.html



Creekstone Farms Premium Beef v. USDA Civ. Action No. 06-544 (JR) Plaintiff’s Summary Judgment Reply and Opposition

http://www.cwd.cc/061103_CFPB_Exh_8_Brown_declaration.pdf


Tuesday, November 02, 2010

BSE - ATYPICAL LESION DISTRIBUTION (RBSE 92-21367) statutory (obex only) diagnostic criteria CVL 1992

http://bse-atypical.blogspot.com/2010/11/bse-atypical-lesion-distribution-rbse.html


Scientific Issues Associated with Designating a Prion as a “Pest” under the Federal Insecticide, Fungicide, and Rodenticide Act

Posted Apr 09 2009 7:13pm March 31 - April 1, 2009

Panel Member List FIFRA Scientific Advisory Panel Open Meeting, March 31 - April 1, 2009

Scientific Issues Associated with Designating a Prion as a “Pest” under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA), and Related Efficacy Test Methods

Environmental Protection Agency Conference Center Lobby Level, One Potomac Yard (South Bldg.), 2777 Crystal Dr., Arlington, VA 22202

FIFRA SAP Website: http://www.epa.gov/scipoly/sap/ Docket Number EPA-HQ-OPP-2008-0859 OPP Docket Telephone: 703-305-5805

FIFRA SAP Session Chair

Steven G. Heeringa, Ph.D. Research Scientist & Director for Statistical Design University of Michigan Institute for Social Research Ann Arbor, MI

Designated Federal Official

Myrta R. Christian, M.S. US Environmental Protection Agency Office of Science Coordination & Policy FIFRA Scientific Advisory Panel EPA East Building, MC 7201M 1200 Pennsylvania Avenue, NW Washington, DC 20460 Tel: 202-564-8450, Fax: 202-564-8382, mhtml:%7B33B38F65-8D2E-434D-8F9B-8BDCD77D3066%7Dmid://00000202/!x-usc:mailto:Chr

FIFRA Scientific Advisory Panel Members

John R. Bucher, Ph.D., DABT Associate Director Environmental Toxicology Program National Institute of Environmental Health Sciences Research Triangle Park, NC

Janice E. Chambers, Ph.D., DABT, ATS William L. Giles Distinguished Professor Director, Center for Environmental Health Sciences College of Veterinary Medicine Mississippi State University Mississippi State, MS

Kirby C. Donnelly, Ph.D. Professor and Head Department of Environmental and Occupational Health School of Rural Public Health Texas A&M University System Health Science Center College Station, TX

Carey N. Pope, Ph.D. Professor, Head & Sitlington Chair of Toxicology Department of Physiological Sciences Oklahoma State University College of Veterinary Medicine Stillwater, OK

Kenneth M. Portier, Ph.D. Program Director, Statistics American Cancer Society National Home Office Atlanta, GA

Daniel Schlenk, Ph.D. Professor of Aquatic Ecotoxicology & Environmental Toxicology Department of Environmental Sciences University of California, Riverside Riverside, CA

FQPA Science Review Board Members

Jason C. Bartz, Ph.D. Assistant Professor Department of Medical Microbiology & Immunology Creighton University School of Medicine Omaha, Nebraska

Dr. Jason C. Bartz is an Assistant Professor in the Department of Medical Microbiology and Immunology in the School of Medicine at Creighton University where he conducts research on prion diseases. Dr. Bartz received a Ph.D. in veterinary science from the University of Wisconsin where he focused on interspecies transmission and adaptation of prions to new host species. Dr. Bartz has over 15 years of experience in prion disease research and is currently investigating the biology of prion strains. Specifically, Dr. Bartz is interested in the mechanisms of strain-specific routes of neuroinvasion, prion strain targeting in the central nervous system and prion strain interference. Dr. Bartz has been an advisor to panels of the National Institutes of Health and the Department of Defense.

Byron Caughey, Ph.D. Senior Investigator & Chief - TSE/Prion Biochemistry Section Laboratory of Persistent Viral Diseases NIH/NIAID Rocky Mountain Laboratories Hamilton, Montana

Dr. Byron Caughey is a Senior Investigator and Chief of the TSE/prion Biochemistry Section of the Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute for Allergy and Infectious Diseases, National Institutes of Health in Hamilton, Montana. Dr. Caughey got his Ph.D. in Biochemistry from the University of Wisconsin-Madison in 1985. In 1986, after post-doctoral studies in neurochemistry at Duke University, he began TSE/prion research at Rocky Mountain Laboratories. Dr. Caughey has published extensively in the TSE/prion field on biochemical, biophysical, cell biological, diagnostic and therapeutic aspects of TSE/prion diseases. He has served on journal editorial boards and is currently a senior editor for the Journal of Virology. He has been a member of institutional scientific review committees for the Institute for Animal Health (UK) and the NIDDK (NIH), and chaired the TSEs Review Panel for the 2006 USDA Scientific Quality Review. He has been an ad hoc reviewer for numerous granting agencies and is currently a member of the scientific advisory boards of the funding agencies PrioNet Canada and Alberta Prion Research Institute.

Kenneth D. Clinkenbeard, D.V.M., Ph.D. Professor & Coordinator, Veterinary Biomedical Sciences Graduate Program Department of Veterinary Pathobiology College of Veterinary Medicine Oklahoma State University Stillwater, Oklahoma

Dr. Kenneth D. Clinkenbeard is Professor of Veterinary Pathobiology and coordinator of the Veterinary Biomedical Sciences Graduate Program at the College of Veterinary Medicine, Oklahoma State University where he teaches graduate and veterinary students and conducts research in the areas of infectious disease pathogenesis and ecology. Ken earned his PhD degree at The Johns Hopkins University School of Medicine in physiological chemistry in Albert Lehninger’s department studying enzymology and was a NIH postdoctoral fellow under Nobel prize winner Dr. Edwin G. Krebs at the University of California at Davis, where he also earned his DVM degree. Dr. Clinkenbeard has over thirty-five years experience working with infectious diseases including disseminate histoplasmosis in dogs and cats; shipping fever, pinkeye, and E coli O157:H7 in cattle; tularemia and plague in wildlife; and chronic wasting disease in cervids. Recently, he has along with his collaborators from DNA Solutions, Inc. developed an in vitro model for detection and study of chronic wasting disease using an immortalized whitetail deer cell line developed in his laboratory under Phase II Small Business Innovative Research funding from the DoD.

Christina Egan, Ph.D. Director, Biodefense Laboratory Wadsworth Center New York State Department of Health Albany, New York

Dr. Christina Egan is the Director of the Biodefense Laboratory at the Wadsworth Center, New York State Department of Health (NYSDOH). Dr. Egan has been with the NYSDOH since 1999 joining the Wadsworth Center as a New York State Emerging Infectious Disease fellow and then as a research scientist and member of the Bioterrorism Response Team which was responsible for the analysis of environmental and clinical specimens for anthrax in 2001. Dr. Egan has 10 years experience working with biological pathogens and high containment laboratories and has obtained specialized certification as a C.B.S.P (Certified Biosafety Professional) through the National Registry of Microbiologists. She has been involved in the development of new diagnostic assays designed to test clinical specimens and environmental samples for bacterial, toxins, and viral agents and oversees the validation process of these molecular assays. Additionally, she has been involved with the development and presentation of many training courses for laboratorians, first responders, Civil Support Teams, and members of the law enforcement community in New York State. She has participated on a number of different federal, state, and scientific panels and committees such as Association of Analytical Communities Biothreat Methods Committee to create standards for biothreat detection method and the EPA Science Advisory Board. She has numerous publications and book chapters related to the development of diagnostic assays for biothreat assays and other issues related to public health preparedness and is an Assistant Professor in the SUNY School of Public Health, Departments of Biomedical Sciences and Environmental Health Sciences.

Kurt Giles, D. Phil. Assistant Adjunct Professor Department of Neurology Institute for Neurodegenerative Diseases University of California at San Francisco San Francisco, California

Dr. Kurt Giles is an Assistant Adjunct Professor at the University of California San Francisco (UCSF). He is director of the transgenics core and a senior scientist at the Institute for Neurodegenerative Diseases (directed by Nobel laureate Dr Stanley B. Prusiner). Kurt received his Ph.D. in pharmacology from Oxford University, United Kingdom, where he used biochemical tools to determine abnormally functioning proteins in Alzheimer’s disease. This was followed by post-doctoral research at the Weizmann Institute of Science, Israel, where he expanded on these studies focusing on protein structure analysis. Kurt has held faculty positions at the Weizmann Institute and at Oxford University prior to moving to UCSF. He has taught undergraduate and graduate courses, and given workshops in many countries, and serves on the editorial board of the journal Biochemistry and Molecular Biology Education. He is also involved in education outreach with High Schools. Kurt has over 15 years experience in neurodegenerative disease research, and he uses transgenic mouse models to understand the molecular basis of various neurodegenerative diseases. He is an expert in prion diseases, where his research encompasses determining the molecular basis for transmission of prion strains between species, understanding the endogenous function of the prion protein, and devising methods to inactivate prions. He has also pioneered the use of survival analysis techniques to more rigorously quantify prion inactivation. Kurt has published widely on the use of transgenic mouse models to measure prion infectivity, and on the inactivation of prions.

Nancy J. Hanson, Ph.D. Associate Professor Department of Medical Microbiology Director of Molecular Biology Center for Research in Anti-Infectives and Biotechnology Creighton University School of Medicine Omaha, Nebraska

Dr. Nancy D. Hanson is an Associate Professor and Director of Molecular Biology for the Center for Research in Anti-Infectives and Biotechnology in the Department of Medical Microbiology and Immunology at Creighton University. Dr. Hanson received her PhD in Medical Microbiology from the University of Nebraska Medical Center. She joined the faculty of Creighton University in 1995. Dr. Hanson has an active research laboratory and has trained several Master and PhD level students. Her area of expertise involves the study of molecular mechanisms of antibiotic resistance in Gram-negative organisms such as E. coli, K. pneumoniae, Salmonella spp. and Pseudomonas aeruginosa. Her research explores two aspects of antibiotic resistance mechanisms: 1) the regulation of the genes involved in resistance and 2) the development of PCR-based diagnostic tests that can be used by clinical laboratories to detect resistance genes in clinical isolates. Dr. Hanson has served as an ad-hoc grant reviewer for National Institutes of Health study sections, the Wellcome Trust, and the British Society for Antimicrobial Chemotherapy. Dr. Hanson has been the invited speaker for the Australian Society of Microbiology, General Society for Microbiology held in Edinburgh Scotland, the American Society of Microbiology and the Interscience Conference on Antimicrobial Agents and Chemotherapy. She serves as an ad-hoc reviewer for 12 scientific journals. Dr. Hanson has also been involved in the Fulbright mentoring program training recipients of the fellowship from countries such as Nigeria and Egypt. In 2007, Dr. Hanson was awarded researcher of the year by the Nebraska Chapter of the Cystic Fibrosis Foundation for her work on P. aeruginosa infecting patients with cystic fibrosis.

Corinne I. Lasmezas, D.V.M., Ph.D. Professor, Department of Infectology The Scripps Research Institute, Scripps Florida Jupiter, Florida

Dr. Corinne I. Lasmézas is Professor at the Department of Infectology of The Scripps Research Institute, Scripps Florida where she directs a research laboratory focusing on the study of prion diseases. Corinne Lasmézas has a Doctorate of Veterinary Medicine from the University of Toulouse, France, and a Ph.D. in Neurosciences from the University Pierre&Marie Curie in Paris, France. She has over fifteen years of experience in the study of prion diseases. Her research in France has contributed to demonstrate the transmissibility to humans of bovine spongiform encephalopathy by showing the similarity of this prion strain with that of the human variant Creutzfeldt-Jakob Disease. She has established a non-human primate model for the study of the pathogenesis and iatrogenic risk from the bovine prion. She has studied prion pathogenesis in rodent models, including the involvement of the lymphoreticular system, the relationship between infectivity and the misfolded prion protein, prion therapy and the interaction of the prion protein with cell surface proteins. Since 2005 Corinne Lasmézas continues her research in the USA at the newly created Department of Infectology of the Scripps Research Institute located in Jupiter, Florida, where her group focuses on the mechanisms of neurodegeneration in prion diseases, the search for a therapy, and a better understanding of the molecular mechanisms underlying prion replication and the strain phenomenon. She serves as a scientific reviewer for research programs and journals, and is a member of several advisory panels in Europe for issues related to ruminant and human prion diseases including the iatrogenic risk linked to human derived medicinal products.

Laura Manuelidis, M.D. Professor & Head of Neuropathology Department of Surgery Yale University School of Medicine New Haven, Connecticut

Dr. Laura Manuelidis is a Professor and Head of the Section of Neuropathology in the Department of Surgery at Yale, as well as on the interdepartmental faculty of Virology and Neuroscience. She received her MD at Yale and trained in both pathology and neuropathology. Major research contributions have been the discovery and sequencing of alpha satellite DNA and retroviral LINES in the 1970s, with the development of non-isotopic in-situ methods for defining chromosome and nuclear structure at high resolution. She also has done broad diagnostic work as Chief of the Neuropathology service for many years, and has been deeply involved in Creutzfeldt-Jakob disease (CJD) research. The first small animal models of CJD were developed at Yale in the 1970s and these have been fundamental for pathogenesis and infectivity studies. Recent tissue culture models of various CJD and a variety of distinct scrapie agent strains have simplified the study of these agents, including variant CJD (vCJD). The vCJD human isolate is derived from the "mad cow disease" agent (UK BSE). Dr. Manuelidis has been a consultant for the NIH, FDA, NATO, the Wellcome Trust, SEAC and the USDA and continues to participate in editorial boards and activities.

Suzette A. Priola, Ph.D. Senior Investigator & Chief - TSE/Prion Molecular Biology Section Laboratory of Persistent Viral Diseases NIH/NIAID Rocky Mountain Laboratories Hamilton, Montana

Dr. Suzette A. Priola is a Senior Investigator and Chief of the TSE/Prion Molecular Biology Section in the Laboratory of Persistent Viral Diseases at the National Institutes of Health’s Rocky Mountain Laboratories. She obtained her PhD in Microbiology and Immunology from the University of California, Los Angeles and specializes in infectious diseases of the central nervous system. She has over 18 years of research experience in the field of prion diseases during which time her laboratory has identified novel prion disease inhibitors and studied multiple different aspects of prion pathogenesis including how prions infect cells and the molecular basis of prion species barriers and strains. She was a member of the Food and Drug Administration (FDA) Transmissible Spongiform Encephalopathy (TSE) Advisory Committee for five years and Chair for almost three years. She has served as a consultant to both the FDA’s Center for Biologics Evaluation and Research and the World Health Organization (WHO) and was a member of the National Prion Research Program administered by the Department of Defense’s Congressionally Directed Medical Research Programs. She has been an editorial board member at the Journal of Biological Chemistry and is currently on the editorial board of the journal Virology.

Juergen A. Richt, DVM, Ph.D. Regents Distinguished Professor Kansas State University College of Veterinary Medicine Diagnostic Medicine/Pathobiology Manhattan, Kansas

Dr. Jürgen A. Richt, DVM, PhD, is the Regents Distinguished Professor at the College of Veterinary Medicine at Kansas State University in Manhattan, KS. He received his DVM from the University of München, Germany, and his PhD in Virology from the University of Giessen, Germany. Dr. Richt has been working in the area of emerging zoonotic diseases for more than 20 years. In his early research years, Dr. Richt focused on the immunopathogenesis and molecular biology of Borna Disease Virus (BDV). After his move to the United States, Dr. Richt’s work focused on influenza virus infections in animals, especially swine, and on animal transmissible spongiform encephalopathies (TSEs) or prion diseases. Dr. Richt has published more than 90 peer-reviewed manuscripts in his area of expertise. He is one of the Editors for the journal Virus Genes and on the Editorial Board of numerous other journals. His research program is funded by the NIH and the CDC. He was recently appointed to the Scientific Advisory Board of OIE, Paris, France.

Lynne Sehulster, Ph.D. Health Scientist Division of Healthcare Quality Promotion Centers for Disease Control and Prevention Atlanta, Georgia

Dr. Lynne Sehulster is a Health Scientist in the Division of Healthcare Quality Promotion (DHQP) within the National Center for Preparedness, Detection, and Control of Infectious Diseases (NCPDCID) at the Centers for Disease Control and Prevention (CDC). She has been at CDC for 12 years. She received her MS and PhD in Microbiology from Rutgers, the State University of New Jersey, and has her certificate as a Microbiologist with the American Society of Clinical Pathologists (M[ASCP]). Prior to coming to CDC, she completed a postdoctoral assignment in the Department of Virology and Epidemiology at Baylor College of Medicine in Houston doing laboratory research in hepatitis B virus inactivation. She subsequently served as an infectious disease epidemiologist for 15 years at the Texas Department of Health (currently known as the Texas Department of State Health Services). While in Texas she was the state health department’s point of contact for viral hepatitis and influenza epidemiology and surveillance activities. Her current areas of expertise at CDC focus on environmental infection control, transmission of infectious diseases, and microbial inactivation. She advises the agency, health care professionals, and the public on issues concerning indoor environmental cleaning, sterilization and disinfection, prion inactivation and risk assessment, and environmental management of emerging diseases. She also provides perspective to CDC on regulated medical waste and other healthcare facility issues such as laundry and environmental services. She is the coordinator of and contributor to the CDC/HICPAC “Guidelines for Environmental Infection Control in Health-Care Facilities” that was released in 2003.

Claudio Soto, Ph.D. Professor, Department of Neurology University of Texas Medical School at Houston Houston, Texas

Dr. Claudio Soto is the Director of the George and Cynthia Mitchell Center for Neurodegenerative Diseases and Professor on the Departments of Neurology, Neuroscience & Cell Biology and Biochemistry & Molecular Biology at the University of Texas Medical Branch in Galveston. Dr. Soto holds the Green Distinguished University Chair in Neuroscience, the largest endowed professorship in the University of Texas. Currently he is also the Founder, Vice-President and Chief Scientific Officer of AMPRION Inc. He received his PhD in biochemistry and molecular biology from the University of Chile in 1993 and was a postdoctoral fellow at the Catholic University of Chile and at the New York University School of Medicine, where he became an assistant professor of research in 1995. Between 1999-2003, Dr Soto was Senior Scientist, Chairman of the Department of Molecular Neuropathology and Senior Executive Scientific Advisor for Neurobiology at Serono International in Switzerland. For the past 13 years, he and his colleagues have engaged in research into the molecular basis of neurodegenerative diseases associated to the misfolding and brain accumulation of proteins, particularly focusing in Alzheimer’s and prion-related disorders. His work has led to the development of novel strategies for treatment and diagnosis of these diseases. He has published more than 90 peer review scientific publications and contributed to more than 15 books, including one written entirely by Dr. Soto. Many of his studies have been published in the most prestigious scientific journals (including Cell, Nature, Science, Nature medicine, EMBO Journal, etc) and several of them have produced a large impact in the scientific community.

http://www.epa.gov/scipoly/sap/meetings/2009/march/033109panelmembers.html


AGENDAFIFRA SCIENTIFIC ADVISORY PANEL (SAP)OPEN MEETINGMarch 31 - April 1, 2009FIFRA SAP WEB SITE http://www.epa.gov/scipoly/sap/ OPP Docket Telephone: (703) 305-5805Docket Number: EPA-HQ- OPP-2008-0859U.S. Environmental Protection AgencyConference Center - Lobby LevelOne Potomac Yard (South Bldg.)2777 S. Crystal Drive, Arlington, VA 22202Scientific Issues Associated with Designating a Prion as a “Pest” under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA), and Related Efficacy Test MethodsPlease note that all times are approximate(See note at the end of the Agenda)Tuesday, March 31, 20098:30 A.M. Opening of Meeting and Administrative Procedures by Designated Federal Official – Myrta R. Christian, M.S., Designated Federal Official, Office of Science Coordination and Policy, EPA8:35 A.M. Introduction and Identification of Panel Members - Steven G. Heeringa, Ph.D., FIFRA Scientific Advisory Panel Chair8:50 A.M. Welcome and Opening Remarks – Steven Bradbury, Ph.D., Deputy Director, Office of Pesticide Programs, EPA9:00 A.M Background and Overview - Jeff Kempter, Senior Advisor, Antimicrobials Division, Office of Pesticide Programs, EPA9:20 A.M. A Regulatory Approach to C&D for CWD and EPA’s Role in the Process – Dean Goeldner, D.V.M., Chronic Wasting Disease Program Manager, USDA-APHIS-VS-NCAHP-RHP, Riverdale, MD9:40 A.M. FDA Approach to Claims for Reducing TSE Infectivity on Medical Devices - Sheila Murphey, M.D., Chief, Infection Control Devices Branch; Division of Anesthesiology, General Hospital, Infection Control and Dental Devices; Office of Device Evaluation; Center for Devices and Radiologic Health; FDA, Rockville, MD10:15 A.M. Break10:30 A.M. EPA’s “White Paper” – Richard Wiggins, Ph.D., National Health and Environmental Effects Research Laboratory, Office of Research and Development, EPA, Research Triangle Park, NC10:50 A.M. EPA’s Guidance for Efficacy Test Methods for Products Bearing11:15 A.M. Prion Infectivity Assays – Christopher J. Silva, Research Chemist, Foodborne contaminants Research Unit, Western Regional Research Center, Albany, CA11:40 A.M. Transmissible Spongiform Encephalopathies (TSEs/Prion Diseases): Target Criteria for Assessing Agent Clearance – David M. Asher, MD, Chief, Laboratory of Bacterial, Parasitic and Unconventional Agents; Division of Emerging and Transfusion-Transmitted Diseases; Office of Blood Research and Review; Center for Biologics Evaluation and Research; FDA, Rockville, Maryland3:45 P.M. Charge to Panel – Question 11. White Paper Issue: Whether EPA’s draft review paper, “Scientific Information Concerning the Issue of Whether Prions Are a ‘Pest’ under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA),” adequately identifies and summarizes available, relevant scientific studies.Prion-Related Claims – Richard Wiggins, Ph.D., National Health and Environmental Effects Research Laboratory, Office of Research and Development, EPA, Research Triangle Park, NC12:00 P.M. Lunch1:00 P.M. Public Comment3:30 P.M. BreakIn 2005, EPA established a Work Group to develop a Notice of Proposed Rulemaking (NPRM) that defines a prion as a “pest” under FIFRA. To assure that it considers key available scientific studies that are relevant to the issue of whether a prion is a “pest” under FIFRA, the Work Group drafted a review paper. While the paper received intra-Agency review, it was not subjected to peer review outside of EPA. Accordingly, EPA seeks the SAP’s peer review of the attached, draft review paper (USEPA 2008). Some of the key references cited in the review paper have been provided to the SAP.EPA wishes to point out that the NPRM will also focus on legal and policy matters that are not addressed in depth in the “white paper.” EPA is presenting this paper to the SAP solely for review as to its characterization of the scientific issues, and is not asking the SAP to interpret legal/policy issues such as Congress’ intent in drafting FIFRA.•Please comment on the accuracy of the characterization of the nature of prions, and the adequacy of the review of the relevant scie ific information to support that characterization, as presented in EPA’s draft paper, “Scientific Information Concerning the Issue of Whether Prions Are a ‘Pest’ under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA).”5:00 P.M. AdjournmentOPEN MEETINGAGENDAFIFRA SCIENTIFIC ADVISORY PANEL (SAP)March 31 - April 1, 2009FIFRA SAP WEB SITE http://www.epa.gov/scipoly/sap/ OPP Docket Telephone: (703) 305-5805Docket Number: EPA-HQ- OPP-2008-0859U.S. Environmental Protection AgencyConference Center - Lobby LevelOne Potomac Yard (South Bldg.) 2777 S. Crystal Drive, Arlington, VA 22202Scientific Issues Associated with Designating a Prion as a “Pest” under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA), and Related Efficacy Test MethodsWednesday, April 1, 20098:30 A.M. Opening of Meeting - Administrative Procedures by Designated Federal Official - Myrta R. Christian, M.S., Designated Federal Official, Office of Science Coordination and Policy, EPA8:35 A.M. Introduction and Identification of Panel Members -Steven G. Heeringa, Ph.D., FIFRA Scientific Advisory Panel Chair8:50 A.M. Follow-up from Previous Day’s Discussion – Jeff Kempter, Senior Advisor, Antimicrobial Division, Office of Pesticide Programs, EPA9:15 A.M. Charge to Panel – Question 22. Efficacy Guidance Test Method Issue: Whether the specific test systems recommended in the draft guidance document are scientifically appropriate to support the registration of pesticide products with prion-related claims.The draft efficacy guidance document (USEPA 2009) recommends a carrier-based, animal infectivity test method, if the intended use of a product is for treating environmental surfaces, and a suspension-based, animal infectivity test method if the intended use of a product is for treating liquids. The draft efficacy guidance document also states that the test methods may either be end-point titration or incubation time interval assays. EPA is interested in knowing the SAP’s opinion on whether these recommended test systems are scientifically sound and appropriate approaches to evaluating the efficacy of pesticide products with prion-related claims. EPA would also like to know whether the SAP recommends that other test methods be considered to evaluate the efficacy of pesticide products used either on•b.3. Efficacy Guidance Performance Criterion Issue: Whether the product performance criterion specified in the draft guidance document to support the registration of pesticide products with prion-related claims is scientifically sound.environmental surfaces or in liquid media.Please comment on the scientific appropriateness of:a.Carrier-based, animal infectivity assays recommended by EPA’s guidance for evaluating the efficacy of pesticide products used on environmental surfaces (e.g., hard, nonporous surfaces).Suspension-based, animal infectivity assays recommended by EPA’s guidance for evaluating the efficacy of pesticide products used in liquid media (e.g., wastewater).Any other known test methods for evaluating the efficacy of pesticide products used on either environmental surfaces or in liquid media.10:30 A.M. Break10:45 A.M. Charge to Panel - Question 3The draft efficacy guidance document recommends a target efficacy criterion of six (6) logs of reduction of infectivity in the treated versus untreated (control) groups. This criterion is widely used in the current scientific literature. EPA would like the SAP’s comment on this proposed product performance criterion.•Please comment on the scientific soundness of the product performance criterion recommended in the draft guidance document to support the registration of pesticide products with a prion claim.12:00 P.M. Lunch1:00 P.M. Charge to Panel – Question 44. Efficacy Guidance Labeling Claim Issue: Whether the labeling claim described in the draft guidance document is scientifically appropriate based on the recommended test systems and product performance standard.The draft efficacy guidance document recommends a carefully worded labeling claim statement: “Has been demonstrated to reduce infeci ity of prions (TSE agents) based on testing using (insert type of organism in which the prions were raised) (insert prion type).” EPA believes that claims that may normally be applied to microorganisms (e.g., “destroy,” “mitigate,” “eliminate,” “control”) may be misleading when applied to prions. Because currently available test methods can only measure a reduction in infectivity, and the total elimination or destruction of prions cannot be•5. Efficacy Guidance Hierarchy Issue: Whether different prion types exhibit variation in the degree of resistance to inactivation by pesticide chemicals and whether a hierarchy of resistance by prion type can be reliably determined at this time.Comparisons of different types of prions in a common animal infectivity assay indicate there may be significant differences with regard to their ability to resist inactivation by pesticide chemicals. For example, Peretz et al. (2006) compared the resistance of hamster scrapie and human CJD prions in transgenic mice expressing either hamster PrP or a chimeric mouse-human PrP transgene and found that human sCJD prion tested was 100,000 fold more difficult to inactivate than hamster Sc237 prion. Preliminary additional studies indicate that the cow BSE prion may be even more resistant to inactivation than the human CJD prion (Giles et al. 2006; 2008 in press).measured, EPA believes that “reduce infectivity” is the only appropriate claim.Please comment on the scientific appropriateness of the term “reduce infectivity” in a label claim to reflect the action of a pesticide on prions.3:00 P.M. Break3:15 P.M. Charge to Panel – Question 5•Please comment on whether a hierarchy of resistance among prion types can be reliably demonstrated for different pesticide chemicals based on the available data.5:00 P.M. AdjournmentPlease be advised that agenda times are approximate; when the discussion for one topic is completed, discussions for the next topic will begin. For further information, please contact the

http://www.epa.gov/scipoly/sap/meetings/2009/march/033109agenda.pdf


FIFRA Scientific Advisory Panel; Notice of Public Meeting PDF Version (3 pp, 80K, About PDF)

[Federal Register: December 17, 2008 (Volume 73, Number 243)] [Notices] [Page 76639-76641] From the Federal Register Online via GPO Access [wais.access.gpo.gov] [DOCID:fr17de08-76]

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ENVIRONMENTAL PROTECTION AGENCY [EPA-HQ-OPP-2008-0859; FRL-8392-9]

FIFRA Scientific Advisory Panel; Notice of Public Meeting

AGENCY: Environmental Protection Agency (EPA). ACTION: Notice.

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SUMMARY: There will be a 2-day meeting of the Federal Insecticide, Fungicide, and Rodenticide Act Scientific Advisory Panel (FIFRA SAP) to consider and review Scientific Issues Associated with Designating a Prion as a ``Pest'' under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA), and Related Efficacy Test Methods.

http://www.epa.gov/EPA-MEETINGS/2008/December/Day-17/m29977.htm


Associated with Designating a Prion as a "Pest" under the Federal insecticide,. Fungicide, and Rodenticide Act (FlFRA), and Related Efficacy Test Methods. These ... whether Prions Are a Pest' under the Federal insecticide, Fungicide, and Rodenticide Act (fifra)." 2. Efficacy Guidance Test Method issue: Whether the ...

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----- Original Message -----

From: "Terry S. Singeltary Sr." flounder9@verizon.net

To: "Bovine Spongiform Encephalopathy" BSE-L@aegee.org

Cc: heggem.daniel@epa.gov; sibert.christopher@epa.gov; denne.jane@epa.gov; hazen.susan@epa.gov; mcrosby@ucsusa.org; erobinson@ucsusa.org; enegin@ucsusa.org; cjdvoice@yahoogroups.com; madcow@lists.iatp.org Sent: Monday, April 28, 2008 9:48 PM

Subject: Interference at the EPA Science and Politics at the U.S. Environmental Protection Agency

Reports and Research

Interference at the EPA

Science and Politics at the U.S. Environmental Protection Agency

The U.S. Environmental Protection Agency (EPA) has the simple yet profound charge "to protect human health and the environment." EPA scientists apply their expertise to protect the public from air and water pollution, clean up hazardous waste, and study emerging threats such as global warming. Because each year brings new and potentially toxic chemicals into our homes and workplaces, because air pollution still threatens our public health, and because environmental challenges are becoming more complex and global, a strong and capable EPA is more important than ever.

Yet challenges from industry lobbyists and some political leaders to the agency's decisions have too often led to the suppression and distortion of the scientific findings underlying those decisions—to the detriment of both science and the health of our nation. While every regulatory agency must balance scientific findings with other considerations, policy makers need access to the highest-quality scientific information to make fully informed decisions.

Concern over this problem led the Union of Concerned Scientists (UCS) to investigate political interference in science at the EPA. The investigation combines dozens of interviews with current and former EPA staff, analysis of government documents, more than 1,600 responses to a survey sent to current EPA scientists, and written comments from EPA scientists.

The results of these investigations show an agency under siege from political pressures. On numerous issues—ranging from mercury pollution to groundwater contamination to climate change—political appointees have edited scientific documents, manipulated scientific assessments, and generally sought to undermine the science behind dozens of EPA regulations.

These findings highlight the need for strong reforms to protect EPA scientists, make agency decision making more transparent, and reduce politicization of the regulatory process. Congress, the next president, and the next EPA Administrator must restore independence and scientific integrity to the EPA by:

Protecting EPA Scientists: Scientists should be free to report the distortion, manipulation, and suppression of their work without fear of retribution. Congress should pass a whistleblower law that includes protection for scientists. The EPA should adopt a communications policy that lets scientists speak freely to the press about their findings. Making the EPA More Transparent: Too many decisions are made behind closed doors with little accountability. The EPA’s scientific findings should be freely available to the public. The EPA should open up its decision-making process to congressional and public scrutiny to help reveal misuses of science Reforming the Regulatory Process: The White House should not change scientific findings in order to weaken, delay, or prevent new public protections. Ensuring Robust Scientific Input to EPA's Decision Making: The EPA should review and strengthen how it uses the scientific expertise of its staff and external advisory committees to create policies—especially when scientific input is critical or required by law. Depoliticizing Funding, Monitoring, and Enforcement: Problems with funding, monitoring and enforcement also need to be addressed by Congress and the next President to ensure that the EPA is the robust environmental agency that our country needs. Political interference is not unique to the EPA. Use the links on this page to explore surveys of scientists at other federal agencies and scores of examples of the abuse of science on issues ranging from prescription drugs to endangered species.

Program Overview Political Interference in Science Restoring Scientific Integrity Stay Informed

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Contents Scientist Statement on Scientific Integrity 2008 Statement: Scientific Freedom and the Public Good Evidence of Political Interference Report: Interference at the EPA Report: Federal Science and the Public Good Examples of Political Interference in Science Surveys of Scientists at Federal Agencies Focus on Climate Science Focus on Endangered Species Science more... News & Views Scientific Integrity Update--01/2008 Scientific Integrity in the News Editorials on the Misuse of Science Poll: The Public's Belief in Independent Science Science, Evolution, and Intelligent Design Resources & Information Info for the Media Info For Congressional Staff Scientific Integrity Curriculum Guide Other Groups Addressing Scientific Integrity Science Idol: The Scientific Integrity Editorial Cartoon Contest

The Report Press Release Executive Summary (PDF) Interference at the EPA: Full Report (PDF) FAQ's about the Report (PDF) Essay Responses From Scientists Select Quotes (PDF) All Essays (PDF) Survey of EPA Scientists Survey Summary and Supporting Documents Congress Reacts Letter to EPA from Rep. Waxman (CA) Statement by Senator Whitehouse (RI) Statement by Rep. Holt (NJ) Other Resources EPA and the White House (PDF) Air Pollution and the EPA (PDF) Climate Change and the EPA (PDF) Toxics and the EPA (PDF) Focus on Region 4 (PDF) Focus on Region 9 (PDF) Related Information Take Action A-to-Z Guide to Political Interference

http://www.ucsusa.org/scientific_integrity/interference/a-to-z-alphabetical.html


Executive Summary

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The Bush administration’s direct abuse of science—combined with systemic changes to the regulatory system that threaten the in- tegrity of EPA science—highlight the need for strong action by the next president and Con- gress to restore scientific integrity to the agen- cy’s decision making. Only then can the EPA fully mobilize to serve the public good and ensure the nation’s health.

Report: Federal Science and the Public Good

http://www.ucsusa.org/scientific_integrity/interference/interference-at-the-epa.html


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April 29, 2004 (Supercedes March 2, 2004 memorandum) Consideration of Prions as a Pest under FIFRA

http://www.epa.gov/oppad001/records_of_decision_on_prions.pdf


CHAMBER OF COMMERCE OF THE UNITED STATES OF AMERICA WILLIAM L. KOVACS 1615 H S TREET , N.W. VICE PRESIDENT WASHINGTON , D.C. 20062 ENVIRONMENT , TECHNOLOGY & (202) 463 5457 REGULATORY AFFAIRS December 22, 2005

Likewise, some agency records of decision, as well as internal memoranda, establish precedent for regulatory policy making that at times extend the regulatory reach of federal agencies far beyond the statutorily mandated powers given by Congress. A recent example of a record of decision with regulatory impact would be the EPA’s decision to regulate prions.4 Prions are protein structures which, when infectious, are suspected of causing transmissible spongiform encephalopathy diseases, such as mad cow disease in cattle.5 EPA’s decision to classify prions as “pests” under FIFRA stems from an internal agency memorandum asserting jurisdiction over prions,6 even though prions are not living things (a prerequisite for EPA jurisdiction under FIFRA).7 Moreover, acting under the authority granted to itself in this memorandum, EPA issued emergency exemptions to several states to authorize the use of pesticides not registered under FIFRA to treat prioninfected surfaces. Therefore, EPA is treating this memorandum as though it is the issuance of a rule, without providing notice to the public or the opportunity to comment on the agency’s interpretation of its authoritative scope.8 The U.S. Chamber specifically requested EPA publish its prior discussion in the Federal Register for notice and comment, but EPA did not respond to that request. 3 Letter from Robert P. Murphy, General Counsel, General Accounting Office, to The Honorable David M. McIntosh, U.S. House of Representatives, January 20, 1999. 4 S.B. Hazen, Memorandum “Consideration of Prions as a Pest under FIFRA” to the Record, April 29, 2004; accessed at:

http://www.epa.gov/oppad001/records_of_decision_on_prions.pdf.

5 See definition of prion at http://en.wikipedia.org/wiki/Prion. 6 Memorandum from Susan B. Hazen, Principle Deputy Assistant Administrator, to the record, dated April 29, 2004. The memorandum is available on EPA’s Web site at:

http://www.epa.gov/oppad001/records_of_decision_on_prions.pdf.

7 7 U.S.C. 136(t). 8 The Administrative Procedure Act defines a “rule” as … an agency statement of general or particular applicability and future effect designed to implement, interpret, or proscribe law or policy…5 U.S.C. 551(4).

snip...full text ;

http://www.whitehouse.gov/omb/inforeg/good_guid/c-commerce.pdf


Rulemaking to Establish Criteria for the Importation of Designated Ruminants and Ruminant Products From Canada into the United States Final Environmental Assessment, December 2004

While FSIS recommends the use of disinfectants, EPA regulates disinfectants under FIFRA. Prior to 2003, prions were not considered pests, and therefore their treatment with disinfectants was not regulated. In September of 2003, EPA classified prions as a pest (Hazen, 2004) and, therefore, the agency was required to regulate the “microorganisms” under the Federal Insecticide, Fungicide, and Rodenticide Act (FIFRA).

http://www.aphis.usda.gov/newsroom/hot_issues/bse/background/documents/03-080-3%20environmental%20assessment.pdf


From: flounder9@verizon.net

Date: 2008-06-21 11:28:34

Subject: Re: [CJDVoice] Interference at the EPA Science and Politics at the U.S. Environmental Protection Agency

White House invokes executive privilege in EPA inquiry

The Bush administration refuses to turn over subpoenaed documents related to the agency's decision to prevent California from enacting stricter emissions standards than the federal government.

By Richard Simon, Los Angeles Times Staff Writer

June 21, 2008

WASHINGTON -- Escalating a fight with Democrats on Capitol Hill, the White House on Friday invoked executive privilege in refusing to turn over documents to a congressional committee investigating the Environmental Protection Agency's decision to deny California permission to implement its own vehicle emission standards.

The Bush administration asserted executive privilege hours before the House Oversight and Government Reform Committee was to vote on whether to bring contempt-of-Congress proceedings against EPA Administrator Stephen L. Johnson and Susan Dudley, administrator of regulatory affairs in the White House Office of Management and Budget, for refusing to turn over subpoenaed documents.

Committee Chairman Henry A. Waxman (D-Beverly Hills) put off a vote on the contempt resolutions while he considers his options.

"I don't think we've had a situation like this since Richard Nixon was president," he said, appearing determined to press ahead, even if it leads to a court fight. "We don't know whether this privilege that's being asserted is valid or not."

Presidents since George Washington have claimed rights to executive branch confidentiality, according to the nonpartisan Congressional Research Service. The Bush White House invoked executive privilege to prevent officials from testifying about the dismissal of nine U.S. attorneys in 2006. President Clinton cited presidential privilege during investigations into the Monica Lewinsky scandal and on other issues.

House and Senate committees have been investigating what role the White House played in EPA decisions preventing California and other states from enacting tougher emissions rules than the federal government and in the EPA's approval of new ozone pollution standards.

The administration's claim of executive privilege is the latest twist in the escalating legal and political battle over California's efforts to implement its own law combating global warming. Critics of the EPA decision contend that it was based on politics, not science or the law.

As Waxman considered his next move in his fight with the White House, another House committee in the room next door grilled former Bush Press Secretary Scott McClellan, who wrote a revealing book about his days in the White House. The hearings were a sign of determination by Democrats not to ease up on their oversight activities, even in the final months of the Bush administration.

In asserting executive privilege in the EPA inquiry, the administration made public a copy of a letter sent to the president by Atty. Gen. Michael B. Mukasey saying that releasing internal documents "could inhibit the candor of future deliberations among the president's staff."

EPA spokesman Tim Lyons said the agency had provided the committee with more than 7,000 documents and devoted 2,200 hours of staff time to responding to requests for information, and he called it "disappointing" that the committee had decided to "politicize environmental regulations."

Jim Nussle, director of the Office of Management and Budget, took issue with Waxman's "sudden and unwarranted" move to consider contempt proceedings, noting that Dudley had appeared before Waxman's committee last month and was asked "only four questions" -- and only one by the panel chairman.

"There is no valid reason for moving from mutual cooperation to unilateral confrontation," Nussle wrote Waxman.

Waxman said: "I am very disappointed and disturbed that the administration is keeping this information from us, and I think we have a right to it."

richard.simon@latimes.com

http://www.latimes.com/news/nationworld/nation/la-na-epa21-2008jun21,0,1939720.story


snip...please see full text ;


http://sciencebushwhacked.blogspot.com/2008/06/white-house-invokes-executive-privilege.html


http://sciencebushwhacked.blogspot.com/


Wednesday, January 19, 2011

EFSA BIOHAZ Scientific Opinion on the revision of the quantitative risk assessment (QRA) of the BSE risk posed by processed animal proteins (PAPs)

EFSA Journal 2011;9(1):1947

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-biohaz-scientific-opinion-on.html


Monday, January 17, 2011

MAD COW Update on Feed Enforcement Activities to Limit the Spread of BSE January 13, 2011

January 2011


http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/mad-cow-update-on-feed-enforcement.html


Friday, January 7, 2011

MEAT AND BONE MEAL AND MINERAL FEED ADDITIVES MAY INCREASE THE RISK OF ORAL PRION DISEASE TRANSMISSION

Journal of Toxicology and Environmental Health, Part A, 74:161-166, 2011 Copyright © Taylor & Francis Group, LLC ISSN: 1528-7394 print / 1087-2620 online DOI: 10.1080/15287394.2011.529066


http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/meat-and-bone-meal-and-mineral-feed.html


Wednesday, January 19, 2011

EFSA and ECDC review scientific evidence on possible links between TSEs in animals and humans Webnachricht 19 Januar 2011

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/efsa-and-ecdc-review-scientific.html


UPDATED DATA ON 2ND CWD STRAIN

Wednesday, September 08, 2010

CWD PRION CONGRESS SEPTEMBER 8-11 2010

http://chronic-wasting-disease.blogspot.com/2010/09/cwd-prion-2010.html


Tuesday, January 25, 2011

Generation of a new form of human PrPSc in vitro by inter-species transmission from cervids prions

http://chronic-wasting-disease.blogspot.com/2011/01/generation-of-new-form-of-human-prpsc.html


Tuesday, January 18, 2011

Agent strain variation in human prion disease: insights from a molecular and pathological review of the National Institutes of Health series of experimentally transmitted disease

http://transmissiblespongiformencephalopathy.blogspot.com/2011/01/agent-strain-variation-in-human-prion.html


2009 UPDATE ON ALABAMA AND TEXAS MAD COWS 2005 and 2006

http://bse-atypical.blogspot.com/2006/08/bse-atypical-texas-and-alabama-update.html


Tuesday, December 14, 2010

Infection control of CJD, vCJD and other human prion diseases in healthcare and community settings part 4, Annex A1, Annex J, UPDATE DECEMBER 2010

http://creutzfeldt-jakob-disease.blogspot.com/2010/12/infection-control-of-cjd-vcjd-and-other.html


Friday, November 30, 2007

CJD QUESTIONNAIRE USA CWRU AND CJD FOUNDATION

http://cjdquestionnaire.blogspot.com/


CAN someone please tell me why hunters can have their deer and elk tested for CWD i.e. prion disease, but consumers cannot have their beef tested for the BSE PrPSc TSE i.e. prion disease ???


what's the difference $$$


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


Don't look, don't find, and damn sure don't let anybody else look, i.e. USA SSS BSE policy of shoot, shovel, and shut the hell up $$$