Monday, July 9, 2012

Spread of Classic BSE Prions from the Gut via the Peripheral Nervous System to the Brain

Study Finds "Mad Cow Disease" in Cattle Can Spread Widely in Autonomic Nervous System before Detectable in the Central Nervous System





New pathway for infection reported in The American Journal of Pathology


Philadelphia, PA, July 9, 2012 – Bovine spongiform encephalopathy (BSE, or “mad cow disease”) is a fatal disease in cattle that causes portions of the brain to turn sponge-like. This transmissible disease is caused by the propagation of a misfolded form of protein known as a prion, rather than by a bacterium or virus. The average time from infection to signs of illness is about 60 months. Little is known about the pathogenesis of BSE in the early incubation period. Previous research has reported that the autonomic nervous system (ANS) becomes affected by the disease only after the central nervous system (CNS) has been infected. In a new study published online in the August issue of The American Journal of Pathology, researchers found that the ANS can show signs of infection prior to involvement of the CNS.


“Our results clearly indicate that both pathways are involved in the early pathogenesis of BSE, but not necessarily simultaneously,” reports lead investigator Martin H. Groschup, PhD, Institute for Novel and Emerging Infectious Diseases at the Friedrich-Loeffler-Institut, Riems, Germany.


To understand the pathogenesis of BSE, fifty-six calves between four and six months of age were infected orally with BSE from infected cattle. Eighteen calves were inoculated orally with BSE-negative material from calf brainstem as controls. The study also included samples collected from a calf that had died naturally of BSE. Tissue samples from the gut, the CNS, and the ANS were collected from animals every four months from 16 to 44 months after infection. The samples were examined for the presence of prions by immunohistochemistry. Samples were also used to infect experimental mice that are highly sensitive to a BSE infection.


A distinct accumulation of the pathological prion protein was observed in the gut in almost all samples. BSE prions were found in the sympathetic ANS system, located in the thoracic and lumbar spinal cord, starting at 16 months after infection; and in the parasympathetic ANS, located in the sacral region of the spinal cord and the medulla, from 20 months post infection. There was little or no sign of infection in the CNS in these samples. The sympathetic part of the ANS was more widely involved in the early pathogenesis than its parasympathetic counterpart. More bovines showing clinical symptoms revealed signs of infection in the sympathetic nervous system structures at a higher degree than in the parasympathetic tissue samples. The earliest detection of BSE prions in the brainstem was at 24 months post infection. However, infection detected in the spinal cord of one animal at 16 months post infection suggests the existence of an additional pathway to the brain.


“The clear involvement of the sympathetic nervous system illustrates that it plays an important role in the pathogenesis of BSE in cattle,” notes Dr. Groschup. “Nevertheless, our results also support earlier research that postulated an early parasympathetic route for BSE.”


The results, Dr. Groschup says, indicate three possible neuronal routes for the ascension of BSE prions to the brain: sympathetic, parasympathetic, and spinal cord projections, in order of importance. “Our study sheds light on the pathogenesis of BSE in cattle during the early incubation period, with implications for diagnostic strategies and food-safety measures.”


# # #


Notes for Editors “Spread of Classical BSE Prions from the Gut via the Peripheral Nervous System to the Brain,” M. Kaatz, C. Fast, U. Zieg ler, A. Balkema-Buschmann, B. Hammerschmidt, M. Keller, A. Oelschlegel, L. McIntyre, M. H. Groschup (DOI 10.1016/j.ajpath.2012.05.001). It appears online in advance of publication in The American Journal of Pathology, Volume 181, Issue 2 (August 2012) published by Elsevier.


Full text of the article is available to credentialed journalists upon request; contact David Sampson at +1 215 239 3171 or ajpmedia@elsevier.com. Journalists wishing to interview the authors may contact Elke Reinking, Public Relations, Friedrich-Loeffler-Institut at +49 3835171244 or elke.reinking@fli.bund.de.


About The American Journal Of Pathology The American Journal of Pathology ( http://ajp.amjpathol.org), official journal of the American Society for Investigative Pathology, seeks to publish high-quality, original papers on the cellular and molecular biology of disease. The editors accept manuscripts that advance basic and translational knowledge of the pathogenesis, classification, diagnosis, and mechanisms of disease, without preference for a specific analytic method. High priority is given to studies on human disease and relevant experimental models using cellular, molecular, animal, biological, chemical, and immunological approaches in conjunction with morphology.


The leading global forum for reporting quality original research on cellular and molecular mechanisms of disease, The American Journal of Pathology is the most highly cited journal in Pathology – over 38,000 cites in 2011 – with an Impact Factor of 4.890 according to Thomson Reuters Journal Citation Reports® 2011.


About Elsevier Elsevier is a world-leading provider of scientific, technical and medical information products and services. The company works in partnership with the global science and health communities to publish more than 2,000 journals, including The Lancet and Cell, and close to 20,000 book titles, including major reference works from Mosby and Saunders. Elsevier’s online solutions include ScienceDirect, Scopus, Reaxys, MD Consult and Mosby’s Nursing Suite, which enhance the productivity of science and health professionals, and the SciVal suite and MEDai’s Pinpoint Review, which help research and health care institutions deliver better outcomes more cost-effectively.


A global business headquartered in Amsterdam, Elsevier employs 7,000 people worldwide. The company is part of Reed Elsevier Group PLC, a world-leading publisher and information provider, which is jointly owned by Reed Elsevier PLC and Reed Elsevier NV. The ticker symbols are REN (Euronext Amsterdam), REL (London Stock Exchange), RUK and ENL (New York Stock Exchange).


Media contact David Sampson Executive Publisher Elsevier +1 215 239 3171 ajpmedia@elsevier.com


Dr. Chhavi Chauhan Scientific Editor The American Journal of Pathology +1 301 634 7953 cchauhan@asip.org


http://www.sciencedirect.com/science/article/pii/S0002944012003409


http://www.journals.elsevierhealth.com/periodicals/ajpa/content/press





Subject: Spread of Classic BSE Prions from the Gut via the Peripheral Nervous System to the Brain


Spread of Classic BSE Prions from the Gut via the Peripheral Nervous System to the Brain


Martin Kaatz,* Christine Fast,* Ute Ziegler,* Anne Balkema-Buschmann,* Bärbel Hammerschmidt,* Markus Keller,* Anja Oelschlegel,† Leila McIntyre,* and Martin H. Groschup*


From the Institute for Novel and Emerging Infectious Diseases,* Friedrich-Loeffler-Institute, Greifswald-Isle of Riems, Germany; and the Scripps Institute,† Florida



An experimental oral bovine spongiform encephalopathy (BSE) challenge study was performed to elucidate the route of infectious prions from the gut to the central nervous system in preclinical and clinical infected animals. Tissue samples collected from the gut and the central and autonomic nervous system from animals sacrificed between 16 and 44 months post infection (mpi) were examined for the presence of the pathological prion protein (PrPSc) by IHC. Moreover, parts of these samples were also bioassayed using bovine cellular prion protein (PrPC) overexpressing transgenic mice (Tgbov XV) that lack the species barrier for bovine prions. A distinct accumulation of PrPSc was observed in the distal ileum, confined to follicles and/or the enteric nervous system, in almost all animals. BSE prions were found in the sympathetic nervous system starting at 16 mpi, and in the parasympathetic nervous system from 20 mpi. A clear dissociation between prion infectivity and detectable PrPSc deposition became obvious. The earliest presence of infectivity in the brain stem was detected at 24 mpi, whereas PrPSc accumulation was first detected after 28 mpi. In summary, our results decipher the centripetal spread of BSE prions along the autonomic nervous system to the central nervous system, starting already halfway in the incubation time.



snip...



Concerning the involvement of the different parts of the ANS during the early spread of the infectious agent, the most interesting results were found in the youngest animals of our study. Both animals at 16 mpi showed BSE infectivity in sympathetic projections (GCC and splanchnic nerves). In addition, one of these cows revealed infectivity in the spinal cord most likely as a result of the sympathetic spread. The parasympathetic tissues were free of infectivity in these animals, whereas both cows sacrificed at 20 mpi contained BSE prions only in the parasympathetic nervous system (cervical vagus nerve and nodose ganglion) but not in purely sympathetic projections or in spinal cord. To our knowledge, this is the first report describing the presence of infectivity in the ANS before the involvement of the CNS in several peripheral neural tissues between 16 and 20 mpi in BSE-infected bovines. These results clearly indicate that both pathways are involved in the early pathogenesis of BSE, but not necessarily simultaneously. Our theory is supported by the coexistence of either none or only spurious amounts of infectivity in the CNS and a remarkable involvement of the sympathetic fibers in cows slightly later in the incubation period.



In addition to the more frequent involvement of the sympathetic samples, a higher transmission rate compared with the parasympathetic samples is obvious. Considering all these results, it is tempting to assume a more dominant and crucial role of the sympathetic nervous system in the pathogenesis of BSE in cattle. The delayed onset of disease in sympathectomized mice infected with scrapie is indicative for this pathway as well.25 Although our results are in accordance with previous studies showing a spread along the CMGC and the splanchnic nerves, notably, our data favor a further distribution via the sympathetic ganglia chain, including the stellate ganglia and the GCC. The occurrence of a mild PrPSc accumulation in the brain stem in association with infectivity solely in sympathetic structures (IT24, 24 mpi) supports the importance of the sympathetic spread. Hence, a mandatory involvement of the intermediolateral column of the spinal cord is not observed. The detection of infectivity in the spinal cord of one animal at 16 mpi indicates a third, additional pathway to the brain as a result of the dissemination along the sympathetic splanchnic nerve. Moreover, we suspect a critical role of the comprehensively involved GCC, because the location close to the brain provides sympathetic fibers to almost all cranial nerves and possibly results in an effect on the brain in uncommon (formatio reticularis and nucleus motorius nervi trigemini) or parasympathetic-related areas (dorsal motor nucleus of the vagus nerve and nucleus tractus solitarii), as the initial PrPSc depositions in the CNS shown herein.



Nevertheless, our results also support the previously postulated early parasympathetic route of the BSE agent along the vagus nerve and the nodose ganglion, although to a lesser degree than the sympathetic structures. Furthermore, infectivity of the nodose ganglion before CNS involvement presumes a centripetal spread along sensory fibers of the vagus nerve, which are in contrast to the assumption that the vagus-associated nodose ganglion might be affected via the centrifugal spread.26 Taken together, our results indicate that there are three independent possible neuronal ascension routes for BSE prions (in order of putative importance): sympathetic parasympathetic spinal cord projections.



Results from scrapie studies in hamster and sheep determined CMGC to be a part of the sympathetic circuitry, which also contains parasympathetic fibers21,22,24 as a possible route of ascension of the agent to the CNS. Our analysis revealed infectivity in the CMGC already from 16 mpi for both possible centripetal routes, leading to the question of where the initial determination of infected fibers takes place. We assume that the route toward the brain likely depends on the nerve type initially infected at the ENS. Sensory fibers of the vagus nerve were found widely distributed in the gut.27,28 Furthermore, vagal efferent synapses in intrinsic ganglia of the ENS innervate the intestinal wall, including the mucosa and submucosa.29 However, a more extensive sympathetic presence in the ENS30 and the CMGC31 and wide innervations of lymphoid structures by the sympathetic nervous system32–34 were reported. These facts could explain the wider and earlier involvement of the sympathetic fibers, as previously discussed. Furthermore, it cannot be excluded that the CMGC may influence the route of infection by the close contact of both sympathetic and parasympathetic nerve types within this ganglion as an operating center of the ANS.



In summary, our data prove an early and widespread distribution of infectivity in the ANS in preclinical cattle before an infection of the CNS. This study is able to confirm the assumed spread via sympathetic and parasympathetic structures for the BSE agent (Figure 4), but we determined a more crucial role of the sympathetic nervous system in the initial neuronal distribution. However, both pathways could be separately involved. According to our results, the spinal cord seems to represent an additional route of ascension, in addition to the more prominent pathways of the ANS.



snip...see full text @



http://www.journals.elsevierhealth.com/periodicals/ajpa/home



Greetings,


seems the price of prion poker played by the USDA et al, just keeps going up and up and up.


so, I gather that the BSE 30 month rule is/was and has been, flawed from the beginning, missing many other tissues that hold prion infectivity, thus, loading up not on the cattle, but everything else that consumes meat and meat by-products with the PrP mad cow agent.


so, I gather that the ARS research on BSE and atypical BSE, the study that claimed that the SRM removal would be changed _if_ and _when_ infectivity was found elsewhere. and when might this take place now $$$


a final thought, this should, with all certainty right $$$ since not only in early stage of disease, but in the later stages of disease as well, with such a wide array of muscle and nerve tissues now involved in infectivity with BSE, and since there is not any way that all these prion infected tissues could be cut out of any product, this should bring the CREEKSTONE MAD COW TESTING DEBATE back to the forefront of consumer safety, right ???


not if the usda, oie, and the industry have anything to do with it, I can assure you of that $


I can hear their same old excuses now, before they even same them, or shall we call them what they really are, just more BSe i.e. lies.


we have a triple mad cow bse firewall.


bbbut, they will NOT tell you that these firewalls ALL failed. ...



lie number 1.


mad cow feed ban in effect since 1997.


bbbut, they will not tell you this PARTIAL and VOLUNTARY mad cow feed ban failed terribly, year, after year, after year, all the way up to 2007, one decade post partial and voluntary feed ban, when 10,000,000 LBS. of banned blood laced meat and bone meal went out into commerce to be fed out, never to return. 2006 was even a worse than that with banned mad cow feed going out into commerce, in Alabama too, where a case of mad cow disease was confirmed. ...



lie number 2.


SRM removal, where this too has failed, time and time again, up until and as late as 2010.



lie number 3.


BSE surveillance


this also was a complete failure as well, to a point that the GAO caught the USDA et al in their BSE testing surveillance program, red handed testing cattle they knew were healthy, free of BSE. yes, up to 100 farms testing for mad cow disease, but the animals in question, were all healthy animal brains, and they knew it. but that was not the only failures in the BSE testing program, that was just part of it. the USDA covered up two mad cows in Texas, one finally confirmed after an act of Congress by the OIG made the USDA retest that cow, some 7 months later, and finally confirm, what they already knew with a SECRET test that had tested positive 7 months previously, and finally were forced to confirm this second mad cow in Texas. it got so bad around 2005, that the top prion scientist at the NIH Paul Brown, said "Everything they did on the Texas cow makes everything they did before 2005 suspect," Brown said.


http://www.upi.com/Health_News/2006/03/15/Analysis-What-that-mad-cow-means/UPI-12841142465253/


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



Wednesday, May 2, 2012

ARS FLIP FLOPS ON SRM REMOVAL FOR ATYPICAL L-TYPE BASE BSE RISK HUMAN AND ANIMAL HEALTH



 http://transmissiblespongiformencephalopathy.blogspot.com/2012/05/ars-flip-flops-on-srm-removal-for.html




USDA TRIPLE BSE MAD COW FIREWALL, SRM, FEED, AND SURVEILLANCE

2012

***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



MAD COW USDA ATYPICAL L-TYPE BASE BSE, the rest of the story...

***Oral Transmission of L-type Bovine Spongiform Encephalopathy in Primate
 Model

http://wwwnc.cdc.gov/eid/article/18/1/pdfs/11-1092.pdf



***Infectivity in skeletal muscle of BASE-infected cattle

http://www.neuroprion.org/resources/pdf_docs/conferences/prion2009/prion2009_bookofabstracts.pdf



***feedstuffs- It also suggests a similar cause or source for atypical BSE in these countries.

http://www.neuroprion.org/resources/pdf_docs/conferences/prion2009/prion2009_bookofabstracts.pdf



***Also, a link is suspected between atypical BSE and some apparently sporadic cases of Creutzfeldt-Jakob disease in humans.

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



The present study demonstrated successful intraspecies transmission of H-type BSE to cattle and the distribution and immunolabeling patterns of PrPSc in the brain of the H-type BSE-challenged cattle. TSE agent virulence can be minimally defined by oral transmission of different TSE agents (C-type, L-type, and H-type BSE agents) [59]. Oral transmission studies with H-type BSEinfected cattle have been initiated and are underway to provide information regarding the extent of similarity in the immunohistochemical and molecular features before and after transmission.

In addition, the present data will support risk assessments in some peripheral tissues derived from cattle affected with H-type BSE.

http://www.veterinaryresearch.org/content/pdf/1297-9716-42-79.pdf



Thursday, June 21, 2012


Clinical and Pathologic Features of H-Type Bovine Spongiform Encephalopathy Associated with E211K Prion Protein Polymorphism


Justin J. Greenlee1*, Jodi D. Smith1, M. Heather West Greenlee2, Eric M. Nicholson1


1 National Animal Disease Center, United States Department of Agriculture, Agricultural Research Service, Ames, Iowa, United States of America, 2 Iowa State University, Ames, Iowa, United States of America


Abstract


The majority of bovine spongiform encephalopathy (BSE) cases have been ascribed to the classical form of the disease. Htype and L-type BSE cases have atypical molecular profiles compared to classical BSE and are thought to arise spontaneously. However, one case of H-type BSE was associated with a heritable E211K mutation in the prion protein gene. The purpose of this study was to describe transmission of this unique isolate of H-type BSE when inoculated into a calf of the same genotype by the intracranial route. Electroretinograms were used to demonstrate preclinical deficits in retinal function, and optical coherence tomography was used to demonstrate an antemortem decrease in retinal thickness. The calf rapidly progressed to clinical disease (9.4 months) and was necropsied. Widespread distribution of abnormal prion protein was demonstrated within neural tissues by western blot and immunohistochemistry. While this isolate is categorized as BSE-H due to a higher molecular mass of the unglycosylated PrPSc isoform, a strong labeling of all 3 PrPSc bands with monoclonal antibodies 6H4 and P4, and a second unglycosylated band at approximately 14 kDa when developed with antibodies that bind in the C-terminal region, it is unique from other described cases of BSE-H because of an additional band 23 kDa demonstrated on western blots of the cerebellum. This work demonstrates that this isolate is transmissible, has a BSE-H phenotype when transmitted to cattle with the K211 polymorphism, and has molecular features that distinguish it from other cases of BSE-H described in the literature.


snip...


Most significantly it must be determined if the molecular phenotype of this cattle TSE remains stable when transmitted to cattle without the E211K polymorphism as several other isolates of atypical BSE have been shown to adopt a molecular profile consistent with classical BSE after passage in transgenic mice expressing bovine PrPC [40] or multiple passages in wild type mice [23]. Results of ongoing studies, namely passage of the E211K Htype isolate into wild-type cattle, will lend further insight into what role, if any, genetic and sporadic forms of BSE may have played in the origins of classical BSE. Atypical cases presumably of spontaneous or, in the case of E211K BSE-H, genetic origins highlight that it may not be possible to eradicate BSE entirely and that it would be hazardous to remove disease control measures such as prohibiting the feeding of meat and bone meal to ruminants.


http://bse-atypical.blogspot.com/2012/06/clinical-and-pathologic-features-of-h.html



Saturday, May 26, 2012


Are USDA assurances on mad cow case 'gross oversimplification'?


SNIP...


What irks many scientists is the USDA’s April 25 statement that the rare disease is “not generally associated with an animal consuming infected feed.”


The USDA’s conclusion is a “gross oversimplification,” said Dr. Paul Brown, one of the world’s experts on this type of disease who retired recently from the National Institutes of Health. "(The agency) has no foundation on which to base that statement.”


“We can’t say it’s not feed related,” agreed Dr. Linda Detwiler, an official with the USDA during the Clinton Administration now at Mississippi State.


In the May 1 email to me, USDA’s Cole backed off a bit. “No one knows the origins of atypical cases of BSE,” she said


The argument about feed is critical because if feed is the cause, not a spontaneous mutation, the California cow could be part of a larger outbreak.


SNIP...


http://bseusa.blogspot.com/2012/05/are-usda-assurances-on-mad-cow-case.html



October 2009 O.11.3 Infectivity in skeletal muscle of BASE-infected cattle


Silvia Suardi1, Chiara Vimercati1, Fabio Moda1, Ruggerone Margherita1, Ilaria Campagnani1, Guerino Lombardi2, Daniela Gelmetti2, Martin H. Groschup3, Anne Buschmann3, Cristina Casalone4, Maria Caramelli4, Salvatore Monaco5, Gianluigi Zanusso5, Fabrizio Tagliavini1 1Carlo Besta" Neurological Institute,Italy; 2IZS Brescia, Italy; 33FLI Insel Riems, D, Germany; 4CEA-IZS Torino, Italy; 5University of Verona, Italy


Background: BASE is an atypical form of bovine spongiform encephalopathy caused by a prion strain distinct from that of BSE. Upon experimental transmission to cattle, BASE induces a previously unrecognized disease phenotype marked by mental dullness and progressive atrophy of hind limb musculature. Whether affected muscles contain infectivity is unknown. This is a critical issue since the BASE strain is readily transmissible to a variety of hosts including primates, suggesting that humans may be susceptible.


Objectives: To investigate the distribution of infectivity in peripheral tissues of cattle experimentally infected with BASE. Methods: Groups of Tg mice expressing bovine PrP (Tgbov XV, n= 7-15/group) were inoculated both i.c. and i.p. with 10% homogenates of a variety of tissues including brain, spleen, cervical lymph node, kidney and skeletal muscle (m. longissimus dorsi) from cattle intracerebrally infected with BASE. No PrPres was detectable in the peripheral tissues used for inoculation either by immunohistochemistry or Western blot.


Results: Mice inoculated with BASE-brain homogenates showed clinical signs of disease with incubation and survival times of 175±15 and 207±12 days. Five out of seven mice challenged with skeletal muscle developed a similar neurological disorder, with incubation and survival times of 380±11 and 410±12 days. At present (700 days after inoculation) mice challenged with the other peripheral tissues are still healthy. The neuropathological phenotype and PrPres type of the affected mice inoculated either with brain or muscle were indistinguishable and matched those of Tgbov XV mice infected with natural BASE.


Discussion: Our data indicate that the skeletal muscle of cattle experimentally infected with BASE contains significant amount of infectivity, at variance with BSE-affected cattle, raising the issue of intraspecies transmission and the potential risk for humans. Experiments are in progress to assess the presence of infectivity in skeletal muscles of natural BASE.


http://www.prion2009.com/sites/default/files/Prion2009_Book_of_Abstracts.pdf



Friday, December 05, 2008


Detection of Prion Infectivity in Fat Tissues of Scrapie-Infected Mice


Brent Race1#, Kimberly Meade-White1#, Michael B. A. Oldstone2, Richard Race1, Bruce Chesebro1*


http://scrapie-usa.blogspot.com/2008/12/detection-of-prion-infectivity-in-fat.html



Prion Infectivity in Fat of Deer with Chronic Wasting Disease▿


Brent Race#, Kimberly Meade-White#, Richard Race and Bruce Chesebro*


http://jvi.asm.org/content/83/18/9608.long



P.9.21


Molecular characterization of BSE in Canada


Jianmin Yang1, Sandor Dudas2, Catherine Graham2, Markus Czub3, Tim McAllister1, Stefanie Czub1 1Agriculture and Agri-Food Canada Research Centre, Canada; 2National and OIE BSE Reference Laboratory, Canada; 3University of Calgary, Canada


Background: Three BSE types (classical and two atypical) have been identified on the basis of molecular characteristics of the misfolded protein associated with the disease. To date, each of these three types have been detected in Canadian cattle.


Objectives: This study was conducted to further characterize the 16 Canadian BSE cases based on the biochemical properties of there associated PrPres. Methods: Immuno-reactivity, molecular weight, glycoform profiles and relative proteinase K sensitivity of the PrPres from each of the 16 confirmed Canadian BSE cases was determined using modified Western blot analysis.


Results: Fourteen of the 16 Canadian BSE cases were C type, 1 was H type and 1 was L type. The Canadian H and L-type BSE cases exhibited size shifts and changes in glycosylation similar to other atypical BSE cases. PK digestion under mild and stringent conditions revealed a reduced protease resistance of the atypical cases compared to the C-type cases. N terminal- specific antibodies bound to PrPres from H type but not from C or L type. The C-terminal-specific antibodies resulted in a shift in the glycoform profile and detected a fourth band in the Canadian H-type BSE.


Discussion: The C, L and H type BSE cases in Canada exhibit molecular characteristics similar to those described for classical and atypical BSE cases from Europe and Japan. This supports the theory that the importation of BSE contaminated feedstuff is the source of C-type BSE in Canada.


*** It also suggests a similar cause or source for atypical BSE in these countries.


http://www.prion2009.com/sites/default/files/Prion2009_Book_of_Abstracts.pdf



10,000,000+ LBS. of PROHIBITED BANNED MAD COW FEED I.E. BLOOD LACED MBM IN COMMERCE USA 2007

Date: March 21, 2007 at 2:27 pm PST

RECALLS AND FIELD CORRECTIONS: VETERINARY MEDICINES -- CLASS II

PRODUCT

Bulk cattle feed made with recalled Darling's 85% Blood Meal, Flash Dried, Recall # V-024-2007

CODE

Cattle feed delivered between 01/12/2007 and 01/26/2007

RECALLING FIRM/MANUFACTURER

Pfeiffer, Arno, Inc, Greenbush, WI. by conversation on February 5, 2007.

Firm initiated recall is ongoing.

REASON

Blood meal used to make cattle feed was recalled because it was cross- contaminated with prohibited bovine meat and bone meal that had been manufactured on common equipment and labeling did not bear cautionary BSE statement.

VOLUME OF PRODUCT IN COMMERCE

42,090 lbs.

DISTRIBUTION

WI


___________________________________



PRODUCT

Custom dairy premix products: MNM ALL PURPOSE Pellet, HILLSIDE/CDL Prot- Buffer Meal, LEE, M.-CLOSE UP PX Pellet, HIGH DESERT/ GHC LACT Meal, TATARKA, M CUST PROT Meal, SUNRIDGE/CDL PROTEIN Blend, LOURENZO, K PVM DAIRY Meal, DOUBLE B DAIRY/GHC LAC Mineral, WEST PIONT/GHC CLOSEUP Mineral, WEST POINT/GHC LACT Meal, JENKS, J/COMPASS PROTEIN Meal, COPPINI - 8# SPECIAL DAIRY Mix, GULICK, L-LACT Meal (Bulk), TRIPLE J - PROTEIN/LACTATION, ROCK CREEK/GHC MILK Mineral, BETTENCOURT/GHC S.SIDE MK-MN, BETTENCOURT #1/GHC MILK MINR, V&C DAIRY/GHC LACT Meal, VEENSTRA, F/GHC LACT Meal, SMUTNY, A- BYPASS ML W/SMARTA, Recall # V-025-2007

CODE

The firm does not utilize a code - only shipping documentation with commodity and weights identified.

RECALLING FIRM/MANUFACTURER

Rangen, Inc, Buhl, ID, by letters on February 13 and 14, 2007. Firm initiated recall is complete.

REASON

Products manufactured from bulk feed containing blood meal that was cross contaminated with prohibited meat and bone meal and the labeling did not bear cautionary BSE statement.

VOLUME OF PRODUCT IN COMMERCE

9,997,976 lbs.

DISTRIBUTION

ID and NV

END OF ENFORCEMENT REPORT FOR MARCH 21, 2007

http://www.fda.gov/Safety/Recalls/EnforcementReports/2007/ucm120446.htm


what about that ALABAMA MAD COW, AND MAD COW FEED THERE FROM IN THAT STATE ???

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)

BANNED MAD COW FEED IN COMMERCE IN ALABAMA

Date: September 6, 2006 at 7:58 am PST PRODUCT

a) EVSRC Custom dairy feed, Recall # V-130-6;

b) Performance Chick Starter, Recall # V-131-6;

c) Performance Quail Grower, Recall # V-132-6;

d) Performance Pheasant Finisher, Recall # V-133-6.

CODE None RECALLING FIRM/MANUFACTURER Donaldson & Hasenbein/dba J&R Feed Service, Inc., Cullman, AL, by telephone on June 23, 2006 and by letter dated July 19, 2006. Firm initiated recall is complete.

REASON
Dairy and poultry feeds were possibly contaminated with ruminant based protein.
VOLUME OF PRODUCT IN COMMERCE 477.72 tons

DISTRIBUTION AL


______________________________


PRODUCT Bulk custom dairy pre-mixes,

Recall # V-120-6 CODE None RECALLING FIRM/MANUFACTURER Ware Milling Inc., Houston, MS, by telephone on June 23, 2006. Firm initiated recall is complete. REASON Possible contamination of dairy animal feeds with ruminant derived meat and bone meal.

VOLUME OF PRODUCT IN COMMERCE 350 tons

DISTRIBUTION AL and MS
______________________________
PRODUCT

a) Tucker Milling, LLC Tm 32% Sinking Fish Grower, #2680-Pellet, 50 lb. bags, Recall # V-121-6;

b) Tucker Milling, LLC #31120, Game Bird Breeder Pellet, 50 lb. bags, Recall # V-122-6;

c) Tucker Milling, LLC #31232 Game Bird Grower, 50 lb. bags, Recall # V-123-6;

d) Tucker Milling, LLC 31227-Crumble, Game Bird Starter, BMD Medicated, 50 lb bags, Recall # V-124-6;

e) Tucker Milling, LLC #31120, Game Bird Breeder, 50 lb bags, Recall # V-125-6;

f) Tucker Milling, LLC #30230, 30 % Turkey Starter, 50 lb bags, Recall # V-126-6;

g) Tucker Milling, LLC #30116, TM Broiler Finisher, 50 lb bags, Recall # V-127-6

CODE All products manufactured from 02/01/2005 until 06/20/2006 RECALLING FIRM/MANUFACTURER Recalling Firm: Tucker Milling LLC, Guntersville, AL, by telephone and visit on June 20, 2006, and by letter on June 23, 2006. Manufacturer: H. J. Baker and Brothers Inc., Stamford, CT. Firm initiated recall is ongoing.

REASON Poultry and fish feeds which were possibly contaminated with ruminant based protein were not labeled as "Do not feed to ruminants".


VOLUME OF PRODUCT IN COMMERCE 7,541-50 lb bags

DISTRIBUTION AL, GA, MS, and TN

END OF ENFORCEMENT REPORT FOR AUGUST 9, 2006


###



Subject: MAD COW FEED RECALL AL AND FL VOLUME OF PRODUCT IN COMMERCE 125 TONS Products manufactured from 02/01/2005 until 06/06/2006


Date: August 6, 2006 at 6:16 pm PST PRODUCT

a) CO-OP 32% Sinking Catfish, Recall # V-100-6;
b) Performance Sheep Pell W/Decox/A/N, medicated, net wt. 50 lbs, Recall # V-101-6;

c) Pro 40% Swine Conc Meal -- 50 lb, Recall # V-102-6;

d) CO-OP 32% Sinking Catfish Food Medicated, Recall # V-103-6;

e) "Big Jim's" BBB Deer Ration, Big Buck Blend, Recall # V-104-6;

f) CO-OP 40% Hog Supplement Medicated Pelleted, Tylosin 100 grams/ton, 50 lb. bag, Recall # V-105-6;

g) Pig Starter Pell II, 18% W/MCDX Medicated 282020, Carbadox -- 0.0055%, Recall # V-106-6;
h) CO-OP STARTER-GROWER CRUMBLES, Complete Feed for Chickens from Hatch to 20 Weeks, Medicated, Bacitracin Methylene Disalicylate, 25 and 50 Lbs, Recall # V-107-6;
i) CO-OP LAYING PELLETS, Complete Feed for Laying Chickens, Recall # 108-6;

j) CO-OP LAYING CRUMBLES, Recall # V-109-6;

k) CO-OP QUAIL FLIGHT CONDITIONER MEDICATED, net wt 50 Lbs, Recall # V-110-6;

l) CO-OP QUAIL STARTER MEDICATED, Net Wt. 50 Lbs, Recall # V-111-6;
m) CO-OP QUAIL GROWER MEDICATED, 50 Lbs, Recall # V-112-6 CODE

Product manufactured from 02/01/2005 until 06/06/2006

RECALLING FIRM/MANUFACTURER Alabama Farmers Cooperative, Inc., Decatur, AL, by telephone, fax, email and visit on June 9, 2006. FDA initiated recall is complete.

REASON Animal and fish feeds which were possibly contaminated with ruminant based protein not labeled as "Do not feed to ruminants".

VOLUME OF PRODUCT IN COMMERCE 125 tons

DISTRIBUTION AL and FL

END OF ENFORCEMENT REPORT FOR AUGUST 2, 2006

###



MAD COW FEED RECALL USA EQUALS 10,878.06 TONS NATIONWIDE Sun Jul 16, 2006 09:22 71.248.128.67
RECALLS AND FIELD CORRECTIONS: VETERINARY MEDICINE -- CLASS II
______________________________



PRODUCT
a) PRO-LAK, bulk weight, Protein Concentrate for Lactating Dairy Animals, Recall # V-079-6;
b) ProAmino II, FOR PREFRESH AND LACTATING COWS, net weight 50lb (22.6 kg), Recall # V-080-6;

c) PRO-PAK, MARINE & ANIMAL PROTEIN CONCENTRATE FOR USE IN ANIMAL FEED, Recall # V-081-6;

d) Feather Meal, Recall # V-082-6 CODE

a) Bulk
b) None
c) Bulk
d) Bulk
RECALLING FIRM/MANUFACTURER H. J. Baker & Bro., Inc., Albertville, AL, by telephone on June 15, 2006 and by press release on June 16, 2006. Firm initiated recall is ongoing.
REASON

Possible contamination of animal feeds with ruminent derived meat and bone meal.


VOLUME OF PRODUCT IN COMMERCE 10,878.06 tons

DISTRIBUTION Nationwide


END OF ENFORCEMENT REPORT FOR July 12, 2006


###


Saturday, July 23, 2011

CATTLE HEADS WITH TONSILS, BEEF TONGUES, SPINAL CORD, SPECIFIED RISK MATERIALS (SRM's) AND PRIONS, AKA MAD COW DISEASE


Saturday, November 6, 2010

TAFS1 Position Paper on Position Paper on Relaxation of the Feed Ban in the EU Berne, 2010 TAFS
INTERNATIONAL FORUM FOR TRANSMISSIBLE ANIMAL DISEASES AND FOOD SAFETY a non-profit Swiss Foundation



North Dakota Firm Recalls Whole Beef Head Products That Contain Prohibited Materials
Recall Release CLASS II RECALL FSIS-RC-023-2010 HEALTH RISK: LOW

Congressional and Public Affairs (202) 720-9113 Catherine Cochran

WASHINGTON, April 5, 2010 - North American Bison Co-Op, a New Rockford, N.D., establishment is recalling approximately 25,000 pounds of whole beef heads containing tongues that may not have had the tonsils completely removed, which is not compliant with regulations that require the removal of tonsils from cattle of all ages, the U.S. Department of Agriculture's Food Safety and Inspection Service (FSIS) announced today.


Tonsils are considered a specified risk material (SRM) and must be removed from cattle of all ages in accordance with FSIS regulations. SRMs are tissues that are known to contain the infective agent in cattle infected with Bovine Spongiform Encephalopathy (BSE), as well as materials that are closely associated with these potentially infective tissues. Therefore, FSIS prohibits SRMs from use as human food to minimize potential human exposure to the BSE agent.


New York Firm Recalls Beef Carcass That Contains Prohibited Materials

Recall Release CLASS II RECALL FSIS-RC-003-2010 HEALTH RISK: LOW

Congressional and Public Affairs (202) 720-9113 Atiya Khan

WASHINGTON, January 15, 2010 - Jerry Hayes Meats Inc., a Newark Valley, N.Y., establishment is recalling approximately 490 pounds of a beef carcass that may not have had the spinal column removed, which is not compliant with regulations that require the removal of spinal cord and vertebral column from cattle over 30 months of age, the U.S. Department of Agriculture's Food Safety and Inspection Service (FSIS) announced today.
Spinal cord and vertebral column are considered a specified risk material (SRM) and must be removed from cattle over 30 months of age in accordance with FSIS regulations. SRMs are tissues that are known to contain the infective agent in cattle infected with Bovine Spongiform Encephalopathy (BSE), as well as materials that are closely associated with these potentially infective tissues. Therefore, FSIS prohibits SRMs from use as human food to minimize potential human exposure to the BSE agent.


Two Companies Recall Beef Tongues Because of Specified Risk Material (SRM)




in the url that follows, I have posted


SRM breaches first, as late as 2011.


then
MAD COW FEED BAN BREACHES AND TONNAGES OF MAD COW FEED IN COMMERCE up until 2007, when they ceased posting them.


then,
MAD COW SURVEILLANCE BREACHES.


Friday, May 18, 2012
Update from APHIS Regarding a Detection of Bovine Spongiform Encephalopathy (BSE) in the United States Friday May 18, 2012


Thursday, June 21, 2012


MEATINGPLACE.COM WAVES MAGIC WAND AND EXPECTS THE USDA MAD COW FOLLIES BSE TO BE GONE




Thursday, June 14, 2012

R-CALF USA Calls USDA Dishonest and Corrupt; Submits Fourth Request for Extension
R-CALF United Stockgrowers of America




Friday, May 25, 2012

R-CALF USDA’s New BSE Rule Eliminates Important Protections Needed to Prevent BSE Spread
Monday, June 18, 2012
R-CALF Submits Incomplete Comments Under Protest in Bizarre Rulemaking “Bovine Spongiform Encephalopathy; Importation of Bovines and Bovine Products”

Sunday, February 12, 2012


National Prion Disease Pathology Surveillance Center Cases Examined1 (August 19, 2011) including Texas





Wednesday, June 27, 2012
First US BSE Case Since 2006 Underscores Need for Vigilance
Neurology Today 21 June 2012




Wednesday, June 13, 2012

MEXICO IS UNDER or MIS DIAGNOSING CREUTZFELDT JAKOB DISEASE AND OTHER PRION DISEASE SOME WITH POSSIBLE nvCJD



previous USA PRION UNIT reports ;



Saturday, March 5, 2011

MAD COW ATYPICAL CJD PRION TSE CASES WITH CLASSIFICATIONS PENDING ON THE RISE IN NORTH AMERICA



Sunday, February 12, 2012
National Prion Disease Pathology Surveillance Center Cases Examined1 (August 19, 2011) including Texas




Tuesday, June 26, 2012
Creutzfeldt Jakob Disease Human TSE report update North America, Canada, Mexico, and USDA PRION UNIT as of May 18, 2012

type determination pending Creutzfeldt Jakob Disease (tdpCJD), is on the rise in Canada and the USA




Sunday, June 3, 2012
A new neurological disease in primates inoculated with prion-infected blood or blood components
Monday, June 11, 2012

Guidance for Industry Draft Guidance for Industry: Amendment to “Guidance for Industry: Revised Preventive Measures to Reduce the Possible Risk of Transmission of Creutzfeldt-Jakob Disease and Variant Creutzfeldt-Jakob Disease by Blood and Blood Products”




Thursday, August 12, 2010
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...

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.



Monday, October 10, 2011

EFSA Journal 2011 The European Response to BSE: A Success Story

snip...


EFSA and the European Centre for Disease Prevention and Control (ECDC) recently delivered a scientific opinion on any possible epidemiological or molecular association between TSEs in animals and humans (EFSA Panel on Biological Hazards (BIOHAZ) and ECDC, 2011). This opinion confirmed Classical BSE prions as the only TSE agents demonstrated to be zoonotic so far but the possibility that a small proportion of human cases so far classified as "sporadic" CJD are of zoonotic origin could not be excluded. Moreover, transmission experiments to non-human primates suggest that some TSE agents in addition to Classical BSE prions in cattle (namely L-type Atypical BSE, Classical BSE in sheep, transmissible mink encephalopathy (TME) and chronic wasting disease (CWD) agents) might have zoonotic potential.


snip...
see follow-up here about North America BSE Mad Cow TSE prion risk factors, and the ever emerging strains of Transmissible Spongiform Encephalopathy in many species here in the USA, including humans ;





Saturday, June 25, 2011


Transmissibility of BSE-L and Cattle-Adapted TME Prion Strain to Cynomolgus Macaque


"BSE-L in North America may have existed for decades"





Over the next 8-10 weeks, approximately 40% of all the adult mink on the farm died from TME.
snip...
The rancher was a ''dead stock'' feeder using mostly (>95%) downer or dead dairy cattle...





Wednesday, April 25, 2012

USA MAD COW DISEASE AND CJD THERE FROM SINGELTARY ET AL 1999 – 2012

Greetings again APHIS ET AL,
THIS is not correct. IN fact, there are several factors i would like to kindly address. Muscle tissue has recently been detected with PrPSc in the peripheral nerves (sciatic nerve, tibial nerve, vagus nerve) of the 11th BSE cow in Japan (Yoshifumi Iwamaru et al). also recently, Aguzzi et al Letter to the Editor Vet Pathol 42:107-108 (2005), Prusiner et al CDI test is another example of detection of the TSE agent in muscle in sCJD, Herbert Budka et al CJD and inclusion body myositis: Abundant Disease-Associated Prion Protein in Muscle, and older studies from Watson Meldrum et al Scrapie agent in muscle - Pattison I A (1990), references as follow ;

PrPSc distribution of a natural case of bovine spongiform encephalopathy

Yoshifumi Iwamaru, Yuka Okubo, Tamako Ikeda, Hiroko Hayashi, Mori- kazu Imamura, Takashi Yokoyama and Morikazu Shinagawa Priori Disease Research Center, National Institute of Animal Health, 3-1-5 Kannondai, Tsukuba 305-0856 Japan gan@affrc.go.jp
Abstract

Bovine spongiform encephalopathy (BSE) is a disease of cattle that causes progressive neurodegeneration of the central nervous system. Infectivity of BSE agent is accompanied with an abnormal isoform of prion protein (PrPSc).


The specified risk materials (SRM) are tissues potentially carrying BSE infectivity. The following tissues are designated as SRM in Japan: the skull including the brain and eyes but excluding the glossa and the masse- ter muscle, the vertebral column excluding the vertebrae of the tail, spinal cord, distal illeum. For a risk management step, the use of SRM in both animal feed or human food has been prohibited. However, detailed PrPSc distribution remains obscure in BSE cattle and it has caused con- troversies about definitions of SRM. Therefore we have examined PrPSc distribution in a BSE cattle by Western blotting to reassess definitions of SRM.


The 11th BSE case in Japan was detected in fallen stock surveillance. The carcass was stocked in the refrigerator. For the detection of PrPSc, 200 mg of tissue samples were homogenized. Following collagenase treatment, samples were digested with proteinase K. After digestion, PrPSc was precipitated by sodium phosphotungstate (PTA). The pellets were subjected to Western blotting using the standard procedure. Anti-prion protein monoclonal antibody (mAb) T2 conjugated horseradish peroxidase was used for the detection of PrPSc.


PrPSc was detected in brain, spinal cord, dorsal root ganglia, trigeminal ganglia, sublingual ganglion, retina. In addition, PrPSc was also detected in the peripheral nerves (sciatic nerve, tibial nerve, vagus nerve). Our results suggest that the currently accepted definitions of SRM in BSE cattle may need to be reexamined. ...


179 T. Kitamoto (Ed.) PRIONS Food and Drug Safety

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



ALSO from the International Symposium of Prion Diseases held in Sendai, October 31, to November 2, 2004;
Bovine spongiform encephalopathy (BSE) in Japan

snip...
"Furthermore, current studies into transmission of cases of BSE that are atypical or that develop in young cattle are expected to amplify the BSE prion"


NO. Date conf. Farm Birth place and Date Age at diagnosis
8. 2003.10.6. Fukushima Tochigi 2001.10.13. 23

9. 2003.11.4. Hiroshima Hyogo 2002.1.13. 21

Test results
# 8b, 9c cows Elisa Positive, WB Positive, IHC negative, histopathology negative

b = atypical BSE case

c = case of BSE in a young animal

b,c, No PrPSc on IHC, and no spongiform change on histology


International Symposium of Prion Diseases held in Sendai, October 31, to November 2, 2004.

The hardback book title is 'PRIONS' Food and Drug Safety T. Kitamoto (Ed.)

Tetsuyuki Kitamoto Professor and Chairman Department of Prion Research Tohoku University School of Medicine 2-1 SeiryoAoba-ku, Sendai 980-8575, JAPAN TEL +81-22-717-8147 FAX +81-22-717-8148 e-mail; kitamoto@mail.tains.tohoku.ac.jp

Symposium Secretariat Kyomi Sasaki TEL +81-22-717-8233 FAX +81-22-717-7656 e-mail: kvomi-sasaki@mail.tains.tohoku.ac.ip

snip...see full text ;

Importation of Whole Cuts of Boneless Beef from Japan [Docket No. 05-004-1] RIN 0579-AB93


Subject: Importation of Whole Cuts of Boneless Beef from Japan [Docket No. 05-004-1] RIN 0579-AB93 TSS SUBMISSION
Date: August 24, 2005 at 2:47 pm PST August 24, 2005

Sunday, August 29, 2010

Prion Disease Round Table Conducted Wednesday December 11, 2003 at Denver, Colorado R-CALF-USA Sponsored (REVISITED AUGUST 2010)

From: Terry S. Singeltary Sr.




Owens, Julie
From: Terry S. Singeltary Sr. [flounder9@verizon.net]

Sent: Monday, July 24, 2006 1:09 PM

To: FSIS RegulationsComments

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


Page 1 of 98

8/3/2006
Greetings FSIS,
I would kindly like to comment on the following ;

[Federal Register: July 12, 2006 (Volume 71, Number 133)]
[Notices]
[Page 39282-39283]
From the Federal Register Online via GPO Access [wais.access.gpo.gov]

[DOCID:fr12jy06-35]
-----------------------------------------------------------------------


DEPARTMENT OF AGRICULTURE
Food Safety and Inspection Service
[Docket No. FSIS-2006-0011]
snip...
HOWEVER, JAPAN has already shown infectivity in tissues other than CNS in there atypical TSE in cattle, so why should we wait, and expose many to this agent needlessly, since the last two mad cows in the USA were also atypical TSE ?

PrPSc distribution of a natural case of bovine spongiform encephalopathy

see full text ;
Response to Public Comments on the Harvard Risk Assessment of Bovine Spongiform Encephalopathy Update October 31, 2005 INTRODUCTION The United States Department of Agriculture’s Food Safety and Inspection Service (FSIS) held a public meeting on July 25, 2006 in Washington, D.C. to present findings from the Harvard Risk Assessment of Bovine Spongiform Encephalopathy Update, October 31, 2005 (report and model located on the FSIS website:



http://www.fsis.usda.gov/Science/Risk_Assessments/index.asp).

Comments on technical aspects of the risk assessment were then submitted to FSIS. Comments were received from Food and Water Watch, Food Animal Concerns Trust (FACT), Farm Sanctuary, R-CALF USA, Linda A Detwiler, and Terry S. Singeltary. This document provides itemized replies to the public comments received on the 2005 updated Harvard BSE risk assessment. Please bear the following points in mind:


03-025IFA 03-025IFA-2 Terry S. Singeltary

From: Terry S. Singeltary Sr. [flounder9@verizon.net]

Sent: Thursday,

September 08, 2005 6:17 PM

Subject: [Docket No. 03-025IFA] FSIS Prohibition of the Use of Specified

Risk Materials for Human Food and Requirements for the Disposition of Non-Ambulatory Disabled Cattle


THE SEVEN SCIENTIST REPORT ***


USDA/OIG-A/50601-10-KC





Monday, December 26, 2011

Prion Uptake in the Gut: Identification of the First Uptake and Replication Sites



Saturday, January 16, 2010
Evidence For CJD TSE Transmission Via Endoscopes 1-24-3 re-Singeltary to Bramble et al
Evidence For CJD/TSE Transmission Via Endoscopes

From Terry S. Singletary, Sr flounder@wt.net 1-24-3



layperson
Terry S. Singeltary Sr.

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