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From: TSS ()
Subject: U.S. Allowed Canada Beef Imports Despite 'Mad-Cow' Concerns WSJ
Date: June 2, 2005 at 6:08 pm PST

U.S. Allowed Canada Beef Imports Despite 'Mad-Cow' Concerns

May 31, 2005 9:11 p.m.; Page C5

WASHINGTON -- Five months after Canada disclosed its first case of mad-cow disease in May 2003, a U.S. Agriculture Department agency made unpublicized policy changes that helped the U.S. meat industry gain access to more beef products from Canada, despite safety concerns, according to a document obtained by Dow Jones Newswires.

In October 2003, Ron DeHaven, who was then deputy administrator of the Agriculture Department's Animal and Plant Health Inspection Service, or APHIS, sent a "decision memorandum" to then-Administrator Bobby Acord recommending that Mr. Acord allow in processed and rendered beef from Canada. Mr. Acord agreed, even though the memorandum warned it would be "a significant change in policy without opportunity for public comment," and it would increase "the possibility that higher risk product may be imported into the United States."

Mr. Acord retired in 2004; Mr. DeHaven succeeded him as administrator.

Mr. DeHaven, in an interview with Dow Jones Newswires, said the decision to allow in processed and rendered beef was made after APHIS was asked to do so by the U.S.-based "National Food Processors Association and others." Mr. DeHaven stressed that U.S. food safety wasn't endangered.

The October 2003 memorandum convinced the rancher group R-CALF United Stockgrowers of America to sue the Agriculture Department, an action that led to the current federal injunction barring U.S. imports of live Canadian cattle, said Bill Bullard, the group's CEO.

The U.S. closed its borders to all Canadian beef and live cattle on May 20, 2003, the day Canada announced finding a case of mad-cow disease, or bovine spongiform encephalopathy. The move was made to protect U.S. cattle and consumers. In August 2003, the Agriculture Department announced it was easing that ban, but only to allow in boneless boxed beef and beef trimmings from cattle under 30 months old. The department considered only the younger cattle to present no risk of transmitting BSE.

The "decision memorandum" was signed by Mr. Acord on Oct. 23, 2003. Mr. DeHaven said Mr. Acord wasn't breaking any regulations by approving permits for Canadian processed and rendered beef, as long as he had "a sound scientific basis for the actions." That basis, he said, came from a risk analysis by APHIS in October 2003.

Mr. Acord didn't return calls.

The change in policy, according to a February audit by the department's inspector general, made it possible for U.S. importers to buy about 5.6 million pounds of the product through April 2004, before an injunction halted the imports.

Even though the department eased its ban in August 2003, Canadian ground beef was still prohibited at the time from cows of any age. The memorandum explained: "Processed meat products such as ground meat and low temperature rendered product are not eligible because these products contain meat from vertebral column, which could be contaminated with neural tissue (which) poses a risk of carrying the BSE agent."

In the memo, Mr. Acord was given four options. "Option 4," the one agreed to by Mr. Acord, "would reverse current USDA import permit policy and allow the entry of processed meat from animals less than 30 months of age."

Write to Bill Tomson at



Vet Pathol 42:107–108 (2005)

Letters to the Editor


Absence of evidence is not always evidence of absence.

In the article ‘‘Failure to detect prion protein (PrPres) by

immunohistochemistry in striated muscle tissues of animals

experimentally inoculated with agents of transmissible spongiform

encephalopathy,’’ recently published in Veterinary

Pathology (41:78–81, 2004), PrPres was not detected in striated

muscle of experimentally infected elk, cattle, sheep, and

raccoons by immunohistochemistry (IHC). Negative IHC,

however, does not exclude the presence of PrPSc. For example,

PrPres was detected in skeletal muscle in 8 of 32

humans with the prion disease, sporadic Creutzfeldt-Jakob

disease (CJD), using sodium phosphotungstic acid (NaPTA)

precipitation and western blot.1 The NaPTA precipitation,

described by Wadsworth et al.,3 concentrates the abnormal

isoform of the prion, PrPres, from a large tissue homogenate

volume before western blotting. This technique has increased

the sensitivity of the western blot up to three orders

of magnitude and could be included in assays to detect

PrPres. Extremely conspicuous deposits of PrPres in muscle

were detected by IHC in a recent case report of an individual

with inclusion body myositis and CJD.2 Here, PrPres was

detected in the muscle by immunoblotting, IHC, and paraf-

fin-embedded tissue blot. We would therefore caution that,

in addition to IHC, highly sensitive biochemical assays and

bioassays of muscle are needed to assess the presence or

absence of prions from muscle in experimental and natural

TSE cases.

Christina Sigurdson, Markus Glatzel, and Adriano Aguzzi

Institute of Neuropathology

University Hospital of Zurich

Zurich, Switzerland


1 Glatzel M, Abela E, et al: Extraneural pathologic prion

protein in sporadic Creutzfeldt-Jakob disease. N Engl J

Med 349(19):1812–1820, 2003

2 Kovacs GG, Lindeck-Pozza E, et al: Creutzfeldt-Jakob

disease and inclusion body myositis: abundant diseaseassociated

prion protein in muscle. Ann Neurol 55(1):

121–125, 2004

3 Wadsworth JDF, Joiner S, et al: Tissue distribution of protease

resistant prion protein in variant CJD using a highly

sensitive immuno-blotting assay. Lancet 358:171–180,



THE findings from the cow in Japan with tissue infectivity in the
peripheral nerve tissue, suprarenal gland,
First time from non-Specified Risk Material ;

Japan Consumer Press online
Nippon shouhisha shinbun
Last modified, 11/09/2004 13:42:49
BSE death cow's anomalous prion detected from peripheral nerve tissue,
suprarenal gland
First time from non-Specified Risk Material, or SRM
National Institute of Animal Health Animal announced on November 1 that
it had detected the anomalous prion protein that was the etiologic agent
of the mad cow disease, or BSE, or bovine spongiform encephaalopathy,
from the peripheral nerve tissue and the suprarenal gland of the cow of
the age in the mad cow disease for the dying infection 94 months on
March 9 this year.
Japan is obligating the removal of the Specified Risk Material, or SRM
such as the head, the spinal cord, the vertebral columns, and the small
intestines that accumulate the anomalous prion protein easily as a BSE
(bovine spongiform encephaalopathy) measures.
Because the mad cow disease etiologic agent was detected from a tissue
different from the Specified Risk Material, or SRM, the review of the
Specified Risk Material, or SRM might be urged on the Japanese Government.
International Symposium of PRION DISEASES for food and drug safety
national institute of animal health(only in Japanese)
The statement of the Ministry of Health, Labour and Welfare
(only in Japanese)
Yomiuri on line (only in Japanese)
Asahi on line(only in Japanese)
Mainichi on line(only in Japanese)


EMBO reports AOP Published online: 11 April 2003

Widespread PrPSc
accumulation in muscles of hamsters orally infected with scrapie

Thomzig, Christine Kratzel, Gudrun Lenz, Dominique Krüger & Michael
Beekes Robert Koch-Institut, P26, Nordufer 20, D-13353 Berlin, Germany

Received 13 February 2003; Accepted 13 March 2003; Published online 11
April 2003.

Abstract :

Scrapie, bovine spongiform encephalopathy and chronic wasting disease
are orally communicable, transmissible spongiform encephalopathies
(TSEs). As zoonotic transmissions of TSE agents may pose a risk to human
health, the identification of reservoirs for infectivity in animal
tissues and their exclusion from human consumption has become a matter
of great importance for consumer protection. In this study, a variety of
muscles from hamsters that were orally challenged with scrapie was
screened for the presence of a molecular marker for TSE infection, PrPSc
(the pathological isoform of the prion protein PrP). Sensitive western
blotting revealed consistent PrPSc accumulation in skeletal muscles from
forelimb and hindlimb, head, back and shoulder, and in tongue.
Previously, our animal model has provided substantial baseline
information about the peripheral routing of infection in naturally
occurring and orally acquired ruminant TSEs. Therefore, the findings
described here highlight further the necessity to investigate thoroughly
whether muscles of TSE-infected sheep, cattle, elk and deer contain
infectious agents.

some previous data on TSE in muscle;



JANUARY 1990, p.68


1 Dr Pattison, a retired but eminent worker on scrapie for many years in
the AFRC, has pointed out that in one of his experimental studies of
scrapie in goats he found scrapie agent in the biceps femoris (rump)
muscle of one animal with clinical disease but not in 2 others with
clinical disease and in none with pre-clinical disease. MAFF have based
their policy on BSE in regard to meat (beef) on the results of studies
of natural scrapie (ie disease occurring under farm conditions) in both
sheep and goats by Hadlow 1979, 80, 81.

Other Infectivity Studies

2. These studies on 52 animals by equally eminent scrapie workers
(Hadlow et al) revealed no evidence whatever of infectivity in skeletal
muscle from these natural cases either in the pre-clinical or even
clinical stages of disease.

It is clear that the pathogenesis of experimental (Pattison) and natural
(Hadlow) scrapie may be different and it was therefore considered wise
to base present policy on knowledge of the natural disease.

3. Pattison exposed his 14 goats to intracerebral inoculation of thrice
passaged scrapie virus (in goats). This may have resulted in strain
selection and/or mutation of the natural agent. In contrast Hadlow's
study involved natural strains (probably multiple) in a flock with a
high incidence of disease in which exposure would almost certainly have
been by the mouth.

4. The fact that Hadlow identified no infectivity in muscle by mouse
inoculation (whereas some other tissues not normally consumed had
detectable infectivifcy) shows that cross contamination of his tissues
did not occur. Pattison's experiments were reported about 20 years
earlier when much less was known about Scrapie. In the intervening
period the knowledge available to Hadlow on the insensitivity of scrapie
agent to heat became available. There is therefore at least the
possibility that Pattison's instruments were not sterilised effectively,
thus possibly giving the false positive result for muscle.

5. Pattison used a more sensitive model for the detection of
infectivifcy, namely goats, whereas Hadlow used mice ie necessitating
crossing the species barrier and possibly reducing the test sensitivity.



6. In regard to the choice of species for agent assay, mice (Hadlow),
these would be guaranteed free of pre-existing Scrapie infection.
Pattison could offer no such guarantee that this was the case in the
animal to which muscle was passaged and disease could have developed
from exposure from a source other than muscle.

7. Pattison did not report that his recipient animals, including the one
inoculated with muscle, were examined by histopathology to confirm the
presence of disease. This is a significant deficit. Clinical diagnosis
alone is not acceptable as adequate evidence for the existence of scrapie.

8. Even in Pattison's studies only in 1 out of 14 goats was infectivity
detected in muscle and that was in a CLINICAL case. In BSE all clinical
cases are notified and do not enter any food chain.

9. The last paragraph of Pattison's letter is illogical. Furthermore,
this is no evidence whatsoever that scrapie or BSE is a danger to man.

W A WATSON 19 January 1990

Private Offices Mr K C Meldrum Mrs E Attridge Mr R Lowson Ms L Austin Mr
R Bradley


Prions in skeletal muscle

Patrick J. Bosque*,dagger ,Dagger , Chongsuk Ryou*, Glenn Telling*,§,
David Peretz*,dagger , Giuseppe Legname*,dagger , Stephen J.
DeArmond*,dagger ,¶, and Stanley B. Prusiner*,dagger ,||,**

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

Contributed by Stanley B. Prusiner, December 28, 2001

Considerable evidence argues that consumption of beef products from
cattle infected with bovine spongiform encephalopathy (BSE) prions
causes new variant Creutzfeldt-Jakob disease. In an effort to prevent
new variant Creutzfeldt-Jakob disease, certain "specified offals,"
including neural and lymphatic tissues, thought to contain high titers
of prions have been excluded from foods destined for human consumption
[Phillips, N. A., Bridgeman, J. & Ferguson-Smith, M. (2000) in The BSE
Inquiry (Stationery Office, London), Vol. 6, pp. 413-451]. Here we
report that mouse skeletal muscle can propagate prions and accumulate
substantial titers of these pathogens. We found both high prion titers
and the disease-causing isoform of the prion protein (PrPSc) in the
skeletal muscle of wild-type mice inoculated with either the Me7 or
Rocky Mountain Laboratory strain of murine prions. Particular muscles
accumulated distinct levels of PrPSc, with the highest levels observed
in muscle from the hind limb. To determine whether prions are produced
or merely accumulate intramuscularly, we established transgenic mice
expressing either mouse or Syrian hamster PrP exclusively in muscle.
Inoculating these mice intramuscularly with prions resulted in the
formation of high titers of nascent prions in muscle. In contrast,
inoculating mice in which PrP expression was targeted to hepatocytes
resulted in low prion titers. Our data demonstrate that factors in
addition to the amount of PrP expressed determine the tropism of prions
for certain tissues. That some muscles are intrinsically capable of
accumulating substantial titers of prions is of particular concern.
Because significant dietary exposure to prions might occur through the
consumption of meat, even if it is largely free of neural and lymphatic
tissue, a comprehensive effort to map the distribution of prions in the
muscle of infected livestock is needed. Furthermore, muscle may provide
a readily biopsied tissue from which to diagnose prion disease in
asymptomatic animals and even humans. Dagger Present address: Department
of Medicine, Denver Health Medical Center, Denver, CO 80204.

§ Present address: Department of Microbiology and Immunology, University
of Kentucky, Lexington, KY 40536-0230.

** To whom reprint requests should be addressed. E-mail:


Extraneural Pathologic Prion Protein in Sporadic Creutzfeldtâ¬Jakob Disease

Markus Glatzel, M.D., Eugenio Abela, Manuela Maissen, M.S., and Adriano Aguzzi, M.D., Ph.D.


Conclusions Using sensitive techniques, we identified extraneural deposition
of PrPSc in spleen and muscle samples from approximately one third of patients
who died with sporadic Creutzfeldtâ¬Jakob disease. Extraneural PrPSc appears
to correlate with a long duration of disease.


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