Friday, November 21, 2014

Detection of Infectious Prion Protein by Seeded Conversion of Recombinant Prion Protein



National Institutes of Health Prospective Grant of Exclusive License:


Detection of Infectious Prion Protein by Seeded Conversion of Recombinant Prion Protein


AGENCY: National Institutes of Health, HHS.


ACTION: Notice.


SUMMARY: This is notice, in accordance with 35 U.S.C. 209 and 37 CFR Part 404, that the National Institutes of Health (NIH), Department of Health and Human Services, is contemplating the grant of an exclusive patent license to Amprion, Inc. located in Houston Texas, USA, to practice the inventions embodied in the following Patents and Patent Applications, each entitled ‘‘Detection of Infectious Prion Protein by Seeded Conversion of Recombinant Prion Protein’’:


1. US provisional Application 60/ 961,364 filed July 20, 2007 [HHS Ref. No. E–109–2007/0–US–01]


2. PCT/US2008/070656, filed July 21, 2008; [HHS Ref. No E–109–2007/1– PCT–01]


3. EPC application No 08796382.3 filed July 21, 2008 [HHS Ref. No E–109– 2007/1–EP–03]


VerDate Sep<11>2014 16:16 Nov 18, 2014 Jkt 235001 PO 00000 Frm 00051 Fmt 4703 Sfmt 4703 E:\FR\FM\19NON1.SGM 19NON1 mstockstill on DSK4VPTVN1PROD with NOTICES Federal Register /Vol. 79, No. 223 /Wednesday, November 19, 2014 /Notices 68893


4. US Application No. 12/177,012, filed July 21, 2008 and issued as US patent 8,216,788 on July 10, 2012 [HHS Ref. No E–109–2007/1–US–02];


5. US Application No. 13/489,321, filed June 5, 2012 [E–109–2007/1–US– 04];


6. US Application No. 14/263,703, filed April 28, 2014 [E–109–2007/1–US– 011]


The patent rights in these inventions have been assigned to the United States of America.


The prospective exclusive licensed territory may be worldwide and the field of use may be limited to in vitro diagnostics of prion-associated diseases requiring FDA premarket approval, or the equivalent thereof outside of the United States, and USDA licensed veterinary diagnostics, or the equivalents thereof outside of the United States.


DATES: Only written comments and/or application for a license that are received by the NIH Office of Technology Transfer on or before 11:59 p.m. Eastern Time on December 19, 2014 will be considered.


ADDRESSES: Requests for a copy of the patents and applications, inquiries, comments and other materials relating to the contemplated license should be directed to: Tedd Fenn, Senior Licensing and Patenting Manager, Office of Technology Transfer, National Institutes of Health, 6011 Executive Boulevard, Suite 325, Rockville, MD 20852–3804; Email:; Telephone: 424–297– 0336; Facsimile: 301–402–0220.


SUPPLEMENTARY INFORMATION: The invention relates to methods and compositions for the detection of infectious prions and diagnosis of prion related diseases. Currently, available tests for disease-causing prions are incapable of detecting low concentrations and must be confirmed post-mortem. This technology enables rapid and economical detection of sublethal concentrations of prions by using recombinant protein (rPrP-sen) as a marker. A seeded sample polymerizes rPrP-sen, which is detected as an amplified indicator of prions in the sample. This assay does not require multiple amplification cycles unless a higher degree of sensitivity is required. This technology potentially may be combined with additional prion-detection technologies to further improve the sensitivity of the assay.


The prospective exclusive license will be royalty bearing and will comply with the terms and conditions of 35 U.S.C. 209 and 37 CFR Part 404. The prospective exclusive license may be granted unless within thirty (30) days from the date of this published notice, the NIH receives written evidence and argument that establishes that the grant of the license would not be consistent with the requirements of 35 U.S.C. 209 and 37 CFR Part 404.


Any additional applications for a license in the field of use, filed in response to this notice, will be treated as objections to the grant of the contemplated exclusive license. Comments and objections submitted to this notice will not be made available for public inspection and, to the extent permitted by law, will not be released under the Freedom of Information Act, 5 U.S.C. 552.


Dated: November 10, 2014. Richard U. Rodriguez, Acting Director, Office of Technology Transfer, National Institutes of Health. [FR Doc. 2014–27342 Filed 11–18–14; 8:45 am] BILLING CODE 4140–01–P



Development of a Biochemical Diagnosis for Creutzfeldt-Jakob disease


Period of Performance: 09/01/2014 - 08/31/2015


$501K Phase 2 STTR


Recipient Firm Amprion, Inc. Houston, TX 77019 Principal Investigator Claudio Soto


Principal Investigator Russell M Lebovitz


Research Topics Affect Age Animals Antibodies authority Autopsy base Biochemical Biological Biological Assay Biological Availability Blinded Blood Blood specimen Blood Tests Blood Transfusion Bovine Spongiform Encephal Brain Businesses Cattle Cerebrospinal Fluid Clinical clinical Diagnosis Code commercialization Communicable Diseases Abstract DESCRIPTION (provided by applicant): Human prion diseases are infectious and invariably fatal forms of neurodegenerative diseases, including sporadic Creutzfeldt-Jakob disease (sCJD), the most common form, and variant CJD (vCJD) which is associated to consumption of cattle meat infected by bovine spongiform encephalopathy. Currently there is not sensitive, objective and non-invasive biochemical diagnosis for these diseases, and even less a procedure to detect people incubating the disease in the pre-symptomatic period. This is a major problem for public health, because prion diseases are known to transmit iatrogenically between human-to-human and because due to the long pre-symptomatic stage of the disease-which may span five decades-the asymptomatic carriers far outnumber the clinically affected individuals. To make the situation even more complicated, the infectious agent responsible for these diseases, termed prion, is composed exclusively of a conformationally altered form of a naturally occurring protein, named PrPSc, which has the unique ability to infect individuals and propagate in the body without the need for genetic material. PrPSc is not only the infectious agent and the likely culprit of neurodegeneration, but also the best surrogate marker for the disease. The challenge is that its quantity is high only in the brain at late stages of the disease However, compelling evidences indicate that PrPSc is present in minute amounts in various peripheral tissues and biological fluids. The main goal of this proposal is to develop a blood- and cerebrospinal fluid (CSF)-based detection assay for PrPSc associated with sCJD and vCJD. Our strategy utilizes two pioneering proprietary technologies developed in our lab: First the protein misfolding cyclic amplification (PMCA) technique which enables to amplify the amount of PrPSc present in the sample to detect as little as a single molecule of PrPSc. PMCA, has a similar power of amplification as PCR and allowed us to detect, for the first time, prions in blood and urine, even at the pre-symptomatic stages of the disease. Second, PrPSc-specific monoclonal antibodies (called PrioC) raised against prion-infected brain homogenates in PrP knock out mice. In this project we will optimize a technology combining PMCA amplification of PrPSc with detection by sandwich ELISA using the PrioC conformational antibodies. The assay will be optimized using animal and human samples for high throughput detection of prions in biological fluids, and will be validated for sensitivity and specificity according to the requiremets of the regulatory authorities with the aim to obtain approval for commercialization. The results generated in this project may lead to the first biochemical test validated for the diagnosis of CJD. With this validated technology, Amprion will establish an International Reference Laboratory for the Detection and Eradication of human prion diseases.



Contact Information Claudio Soto, PhD Phone: 713-5007086 Houston, United States


Professional Information Professor and Center Director University of Texas Medical School at Houston


Financial Disclosure Member reports the following financial or other potential conflicts of interest: [Last updated: May 6, 2009]


I am Founder, Vice-President and Chief Scientific Officer of Amprion Inc, a company focusing on development sensitive biochemical diagnosis for neurodegenerative diseases



UTHealth researchers discover infectious prion protein in urine of patients with variant Creutzfeldt-Jakob disease


Claudio Soto, Ph.D., in one of his labs at The University of Texas Health Science Center at Houston (UTHealth) Claudio Soto, Ph.D., in one of his labs at The University of Texas Health Science Center at Houston (UTHealth)


HOUSTON – (August 7, 2014) – The misfolded and infectious prion protein that is a marker for variant Creutzfeldt-Jakob disease – linked to the consumption of infected cattle meat – has been detected in the urine of patients with the disease by researchers at The University of Texas Health Science Center at Houston (UTHealth) Medical School.


The results of the international study, led by Claudio Soto, Ph.D., professor of neurology at the UTHealth Medical School, is published in the Aug. 7 issue of the New England Journal of Medicine.


Variant Creutzfeldt-Jakob disease in humans and bovine spongiform encephalopathy in animals – also known as Mad Cow disease – are fatal neurodegenerative disorders. There are currently no noninvasive tools available to diagnose the disease and there are no treatments.


Sporadic Creutzfeldt-Jakob disease occurs worldwide at a rate of around 1 new case per million people per year. The variant form is a new disease occurring in people who either ate the beef of cows with bovine spongiform encephalopathy or, in the case of three patients in the United Kingdom, received blood transfusions from asymptomatic infected donors.


The international team of researchers analyzed urine samples from 68 patients with sporadic Creutzfeldt-Jakob disease, 14 patients with variant Creutzfeldt-Jakob disease, four patients with genetic prion diseases, 50 patients with other neurodegenerative diseases, 50 patients with nondegenerative neurologic diseases and 52 healthy persons.


Soto’s laboratory used a protein misfolding cyclic amplification assay, invented in the lab, which mimics the prion replication process in vitro that occurs in prion disease. The misfolded prion proteins were detected in the urine of 13 of 14 patients with variant Creutzfeldt-Jakob disease. The single patient whose urine was negative had been receiving an experimental treatment of pentosan polysulfate directly into the brain. No misfolded prion proteins were detected in the urine of any the other study subjects, including the patients who had sporadic Creutzfeldt-Jakob disease.


“What could be less invasive than detecting this disease in urine? The fact that we were able to detect just the variant Creutzfeldt-Jakob disease form in the urine is very important. This could lead to the development of commercial technology for diagnosis as well as to determine the safety of donated blood and urinary products,” said Soto, who is the director of The George and Cynthia Mitchell Center for Research in Alzheimer’s disease and Related Brain Disorders, and founder of Amprion Inc, a biotech company developing the cyclic amplification technology for commercial application.


According to the World Health Organization (WHO), variant Creutzfeldt-Jakob disease affects younger patients, who have a median age of 28 at death, compared to sporadic Creutzfeldt-Jakob disease with a median age of 68. Most patients, after diagnosis of either form, live less than a year before death.


As of June 2, 2014, 177 of 229 people in the world with Creutzfeldt-Jakob disease were from the United Kingdom. A 2013 study published in the British Medical Journal has estimated that approximately 30,000 people in the United Kingdom might be carriers of the variant form of the disease.


“This study reports, for the first time, the detection of the abnormal prion protein in the urine from patients with variant Creutzfeldt-Jakob disease using the protein misfolding amplification technique pioneered by Dr. Claudio Soto,” said co-author James W. Ironside, FMedSci, FRSE, professor of clinical neuropathology at the National CJD Research and Surveillance Unit at the University of Edinburgh. “This has great potential to allow the development of a highly sensitive and specific non-invasive test that can be used for the diagnosis of variant Creutzfeldt-Jakob disease, and potentially as a screening tool for variant Creutzfeldt-Jakob disease infection in asymptomatic individuals, which is a topic of current interest in the United Kingdom.”


First author is Fabio Moda, Ph.D., who was a post-doctoral fellow in Soto’s lab at the UTHealth Medical School and is now with the Istituto Neurologico Carlo Besta in Milan.


Co-authors include Luis Concha-Marambio and Kyung-Won Park, Ph.D., from the UTHealth Medical School; and Fabrizio Tagliavini, M.D.; Marcella Catania, Ph.D.; Emanuela Maderna and Silvia Suardi from Istituto Neurologico Carlo Besta.


Pierluigi Gambetti, M.D., and Silvio Notari, Ph.D. are co-authors from the National Prion Disease Pathology Surveillance Center at Case Western Reserve University. Co-author Richard Knight, M.D., is with the National CJD Research and Surveillance Unit at the University of Edinburgh. Stephanie Haik, M.D., Ph.D., and Jean-Philippe Brandel, M.D., are co-authors from the Assistance Publique-Hopitaux de Paris.


The research was supported by grants from the National Institutes of Health (P01AI077774, R42NS079060, R01NS049173 and R01NS078745 to Soto); PrioNet Canada and Merck Serono (to Soto); the Italian Ministry of Health, Associazione Italniana Encfalopatie da Prioni and Minesterio dell’Universita e della Ricerca (to Tagliavini); the Charles S. Britton Fund (to Gambetti) and the U.K Department of Health and Scottish Government (to Ironside and Knight).


Deborah Mann Lake


Media Hotline: 713-500-3030



Original Article


Prions in the Urine of Patients with Variant Creutzfeldt–Jakob Disease


Fabio Moda, Ph.D., Pierluigi Gambetti, M.D., Silvio Notari, Ph.D., Luis Concha-Marambio, B.Sc., Marcella Catania, Ph.D., Kyung-Won Park, Ph.D., Emanuela Maderna, B.Sc., Silvia Suardi, B.Sc., Stéphane Haïk, M.D., Ph.D., Jean-Philippe Brandel, M.D., James Ironside, M.D., Richard Knight, M.D., Fabrizio Tagliavini, M.D., and Claudio Soto, Ph.D.


N Engl J Med 2014; 371:530-539August 7, 2014DOI: 10.1056/NEJMoa1404401




Prions, the infectious agents responsible for transmissible spongiform encephalopathies, consist mainly of the misfolded prion protein (PrPSc). The unique mechanism of transmission and the appearance of a variant form of Creutzfeldt–Jakob disease, which has been linked to consumption of prion-contaminated cattle meat, have raised concerns about public health. Evidence suggests that variant Creutzfeldt–Jakob disease prions circulate in body fluids from people in whom the disease is silently incubating.




To investigate whether PrPSc can be detected in the urine of patients with variant Creutzfeldt–Jakob disease, we used the protein misfolding cyclic amplification (PMCA) technique to amplify minute quantities of PrPSc, enabling highly sensitive detection of the protein. We analyzed urine samples from several patients with various transmissible spongiform encephalopathies (variant and sporadic Creutzfeldt–Jakob disease and genetic forms of prion disease), patients with other degenerative or nondegenerative neurologic disorders, and healthy persons.




PrPSc was detectable only in the urine of patients with variant Creutzfeldt–Jakob disease and had the typical electrophoretic profile associated with this disease. PrPSc was detected in 13 of 14 urine samples obtained from patients with variant Creutzfeldt–Jakob disease and in none of the 224 urine samples obtained from patients with other neurologic diseases and from healthy controls, resulting in an estimated sensitivity of 92.9% (95% confidence interval [CI], 66.1 to 99.8) and a specificity of 100.0% (95% CI, 98.4 to 100.0). The PrPSc concentration in urine calculated by means of quantitative PMCA was estimated at 1×10−16 g per milliliter, or 3×10−21 mol per milliliter, which extrapolates to approximately 40 to 100 oligomeric particles of PrPSc per milliliter of urine.




Urine samples obtained from patients with variant Creutzfeldt–Jakob disease contained minute quantities of PrPSc. (Funded by the National Institutes of Health and others.)


The views expressed in this article are those of the authors and not necessarily those of the U.K. Department of Health.


Supported by grants from the National Institutes of Health (P01AI077774, R42NS079060, R01NS049173, and R01NS078745, to Dr. Soto), PrioNet Canada and Merck Serono (to Dr. Soto), the Italian Ministry of Health, Associazione Italiana Encefalopatie da Prioni, and Ministero dell'Università e della Ricerca (RBAP11FRE9, to Dr. Tagliavini), the Charles S. Britton Fund (P01AG14359, to Dr. Gambetti), and the U.K. Department of Health and the Scottish Government (to Drs. Ironside and Knight).


Disclosure forms provided by the authors are available with the full text of this article at


We thank Suzanne Lowrie, F.I.B.M.S., for assistance in collecting urine samples, Denisse Gonzalez-Romero, M.Sc., of the University of Texas Medical School at Houston for technical assistance, and Dr. Glenn Telling of Colorado State University for providing colonies of transgenic mice expressing human prion protein.


Source Information


From the Mitchell Center for Research in Alzheimer's Disease and Related Brain Disorders, University of Texas Medical School at Houston, Houston (F.M., L.C.-M., K.-W.P., C.S.); Foundation Carlo Besta Neurologic Institute, Milan (F.M., M.C., E.M., S.S., F.T.); National Prion Disease Pathology Surveillance Center, Case Western Reserve University, Cleveland (P.G., S.N.); Universidad de los Andes, Facultad de Medicina, Santiago, Chile (L.C.-M.); Assistance Publique–Hôpitaux de Paris, Cellule Nationale de Référence des Maladies de Creutzfeldt–Jakob, Groupe Hospitalier Pitié–Salpêtrière, INSERM Unité 1127, Université Pierre et Marie Curie–Paris 6, and Centre Nationale de la Recherche Scientifique, Unité Mixte de Recherche — all in Paris (S.H., J.-P.B.); and the National CJD Research and Surveillance Unit, Western General Hospital, University of Edinburgh, Edinburgh (J.I., R.K.).


Address reprint requests to Dr. Soto at the University of Texas Medical School at Houston, 6431 Fannin St., Houston, TX77030, or at



Original Article


A Test for Creutzfeldt–Jakob Disease Using Nasal Brushings


Christina D. Orrú, Ph.D., Matilde Bongianni, Ph.D., Giovanni Tonoli, M.D., Sergio Ferrari, M.D., Andrew G. Hughson, M.S., Bradley R. Groveman, Ph.D., Michele Fiorini, Ph.D., Maurizio Pocchiari, M.D., Salvatore Monaco, M.D., Byron Caughey, Ph.D., and Gianluigi Zanusso, M.D., Ph.D.


N Engl J Med 2014; 371:519-529August 7, 2014DOI: 10.1056/NEJMoa1315200




Definite diagnosis of sporadic Creutzfeldt–Jakob disease in living patients remains a challenge. A test that detects the specific marker for Creutzfeldt–Jakob disease, the prion protein (PrPCJD), by means of real-time quaking-induced conversion (RT-QuIC) testing of cerebrospinal fluid has a sensitivity of 80 to 90% for the diagnosis of sporadic Creutzfeldt–Jakob disease. We have assessed the accuracy of RT-QuIC analysis of nasal brushings from olfactory epithelium in diagnosing sporadic Creutzfeldt–Jakob disease in living patients.




We collected olfactory epithelium brushings and cerebrospinal fluid samples from patients with and patients without sporadic Creutzfeldt–Jakob disease and tested them using RT-QuIC, an ultrasensitive, multiwell plate–based fluorescence assay involving PrPCJD-seeded polymerization of recombinant PrP into amyloid fibrils.




The RT-QuIC assays seeded with nasal brushings were positive in 30 of 31 patients with Creutzfeldt–Jakob disease (15 of 15 with definite sporadic Creutzfeldt–Jakob disease, 13 of 14 with probable sporadic Creutzfeldt–Jakob disease, and 2 of 2 with inherited Creutzfeldt–Jakob disease) but were negative in 43 of 43 patients without Creutzfeldt–Jakob disease, indicating a sensitivity of 97% (95% confidence interval [CI], 82 to 100) and specificity of 100% (95% CI, 90 to 100) for the detection of Creutzfeldt–Jakob disease. By comparison, testing of cerebrospinal fluid samples from the same group of patients had a sensitivity of 77% (95% CI, 57 to 89) and a specificity of 100% (95% CI, 90 to 100). Nasal brushings elicited stronger and faster RT-QuIC responses than cerebrospinal fluid (P<0 .001="" 105="" 107="" approximately="" at="" between-group="" brushings="" cerebrospinal="" comparison="" concentrations="" contained="" div="" fluid.="" for="" greater="" in="" individual="" logs10="" of="" prion="" response="" seeds="" several="" strength="" than="" the="" to="">



In this preliminary study, RT-QuIC testing of olfactory epithelium samples obtained from nasal brushings was accurate in diagnosing Creutzfeldt–Jakob disease and indicated substantial prion seeding activity lining the nasal vault. (Funded by the Intramural Research Program of the National Institute of Allergy and Infectious Diseases and others.)


Supported by the Intramural Research Program of the National Institute of Allergy and Infectious Diseases (NIAID), by a grant from Fondazione Cariverona (Disabilità cognitiva e comportamentale nelle demenze e nelle psicosi, to Dr. Monaco), by a grant from the Italian Ministry of Health (RF2009-1474758, to Drs. Zanusso and Pocchiari), by a grant from the Creutzfeldt–Jakob Disease Foundation (to Dr. Orrú), by a fellowship from Programma Master and Back–Percorsi di rientro (PRR-MAB-A2011-19199, to Dr. Orrú), and by donations to the NIAID Gift Fund from Mary Hilderman Smith, Zoë Smith Jaye, and Jenny Smith Unruh, in memory of Jeffrey Smith.


Disclosure forms provided by the authors are available with the full text of this article at


Drs. Orrú and Bongianni contributed equally to this article.


We thank our many colleagues (see Acknowledgments in the Supplementary Appendix) for their support of this project and for assistance with the preparation of earlier versions of the manuscript.


Source Information From the Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health, Hamilton, MT (C.D.O., M.B., A.G.H., B.R.G., B.C.); and the Department of Biomedical Sciences, University of Cagliari, Cagliari (C.D.O.), the Department of Neurologic and Movement Sciences, University of Verona, Verona (M.B., S.F., M.F., S.M., G.Z.), Clinica Otorinolaringoiatrica, Policlinico G.B. Rossi, Azienda Ospedaliera Universitaria Integrata, Verona (G.T.), and the Department of Cell Biology and Neurosciences, Istituto Superiore di Sanità, Rome (M.P.) — all in Italy.


Address reprint requests to Dr. Caughey at Rocky Mountain Laboratories, NIAID, 903 S. 4th St., Hamilton, MT 59840, or at; or to Dr. Zanusso at Policlinico G.B. Rossi, Piazzale L.A. Scuro, 10, 37134 Verona, Italy, or at




Wednesday, July 23, 2014


After the storm? UK blood safety and the risk of variant Creutzfeldt-Jakob Disease



Monday, June 02, 2014


Confirmed Human BSE aka mad cow Variant CJD vCJD or nvCJD Case in Texas



Jeff Schwan, sporadic cjd, clustering, and BSE aka mad cow type disease, is there a link ? *video*



Monday, November 3, 2014




National Prion Disease Pathology Surveillance Center Cases Examined1 (October 7, 2014)


***6 Includes 11 cases in which the diagnosis is pending, and 19 inconclusive cases;


***7 Includes 12 (11 from 2014) cases with type determination pending in which the diagnosis of vCJD has been excluded.


***The sporadic cases include 2660 cases of sporadic Creutzfeldt-Jakob disease (sCJD),


***50 cases of Variably Protease-Sensitive Prionopathy (VPSPr)


***and 21 cases of sporadic Fatal Insomnia (sFI).



Monday, November 3, 2014


The prion protein protease sensitivity, stability and seeding activity in variably protease sensitive prionopathy brain tissue suggests molecular overlaps with sporadic Creutzfeldt-Jakob disease



Tuesday, November 04, 2014


The pathological and molecular but not clinical phenotypes are maintained after second passage of experimental atypical bovine spongiform encephalopathy in cattle



*** Singeltary reply ; Molecular, Biochemical and Genetic Characteristics of BSE in Canada Singeltary reply ;



Tuesday, August 12, 2014





Thursday, October 02, 2014


[Docket No. APHIS-2013-0064] Concurrence With OIE Risk Designations for Bovine Spongiform Encephalopathy



Saturday, August 14, 2010


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






Six-year follow-up of a point-source exposure to CWD contaminated venison in an Upstate New York community: risk behaviours and health outcomes 2005–2011



Thursday, July 31, 2014 


EFSA Scrapie reduction unlikely without effective breeding programme



Sunday, July 06, 2014


Dietary Risk Factors for Sporadic Creutzfeldt-Jakob Disease: A Confirmatory Case-Control Study


Conclusions—The a priori hypotheses were supported.


*Consumption of various meat products may be one method of transmission of the infectious agent for sCJD.



Tuesday, November 04, 2014

Towards an Age-Dependent Transmission Model of Acquired and Sporadic Creutzfeldt-Jakob Disease

Wednesday, September 10, 2014

Creutzfeldt-Jakob disease (CJD) biannual update (August 2014), with updated guidance on decontamination of gastrointestinal endoscopy equipment

Research and analysis

Transmissible Spongiform Encephalopathy TSE Prion Disease North America 2014


Transmissible Spongiform Encephalopathy TSE Prion Disease have now been discovered in a wide verity of species across North America. typical C-BSE, atypical L-type BASE BSE, atypical H-type BSE, atypical H-G BSE, of the bovine, typical and atypical Scrapie strains, in sheep and goats, with atypical Nor-98 Scrapie spreading coast to coast in about 5 years. Chronic Wasting Disease CWD in cervid is slowly spreading without any stopping it in Canada and the USA and now has mutated into many different strains. Transmissible Mink Encephalopathy TME outbreaks. These Transmissible Spongiform Encephalopathy TSE Prion Disease have been silently mutating and spreading in different species in North America for decades.


The USDA, FDA, et al have assured us of a robust Triple BSE TSE prion Firewall, of which we now know without a doubt, that it was nothing but ink on paper. Since the 1997 mad cow feed ban in the USA, literally tons and tons of banned mad cow feed has been put out into commerce, never to return, as late as December of 2013, serious, serious breaches in the FDA mad cow feed ban have been documented. The 2004 enhanced BSE surveillance program was so flawed, that one of the top TSE prion Scientist for the CDC, Dr. Paul Brown stated ; Brown, who is preparing a scientific paper based on the latest two mad cow cases to estimate the maximum number of infected cows that occurred in the United States, said he has "absolutely no confidence in USDA tests before one year ago" because of the agency's reluctance to retest the Texas cow that initially tested positive.


see ;



The BSE surveillance and testing have also been proven to be flawed, and the GAO and OIG have both raised serious question as to just how flawed it has been (see GAO and OIG reports). North America has more documented TSE prion disease, in different documented species (excluding the Zoo BSE animals in the EU), then any other place on the Globe. This does not include the very likelihood that TSE prion disease in the domestic feline and canine have been exposed to high doses of the TSE prion disease vid pet food. To date, it’s still legal to include deer from cwd zone into pet food or deer food. Specified Risk Material i.e. SRM bans still being breach, as recently as just last month.


nvCJD or what they now call vCJD, another case documented in Texas last month, with very little information being released to the public on about this case? with still the same line of thought from federal officials, ‘it can’t happen here’, so another vCJD blamed on travel of a foreign animal disease from another country, while ignoring all the BSE TSE Prion risk factors we have here in the USA and Canada, and the time that this victim and others, do spend in the USA, and exposed to these risk factors, apparently do not count in any way with regard to risk factor. a flawed process of risk assessment.


sporadic CJD, along with new TSE prion disease in humans, of which the young are dying, of which long duration of illness from onset of symptoms to death have been documented, only to have a new name added to the pot of prion disease i.e. sporadic GSS, sporadic FFI, and or VPSPR. I only ponder how a familial type disease could be sporadic with no genetic link to any family member? when the USA is the only documented Country in the world to have documented two different cases of atypical H-type BSE, with one case being called atypical H-G BSE with the G meaning Genetic, with new science now showing that indeed atypical H-type BSE is very possible transmitted to cattle via oral transmission (Prion2014). sporadic CJD and VPSPR have been rising in Canada, USA, and the UK, with the same old excuse, better surveillance. You can only use that excuse for so many years, for so many decades, until one must conclude that CJD TSE prion cases are rising. a 48% incease in CJD in Canada is not just a blip or a reason of better surveillance, it is a mathematical rise in numbers. More and more we are seeing more humans exposed in various circumstance in the Hospital, Medical, Surgical arenas to the TSE Prion disease, and at the same time in North America, more and more humans are becoming exposed to the TSE prion disease via consumption of the TSE prion via deer and elk, cattle, sheep and goats, and for those that are exposed via or consumption, go on to further expose many others via the iatrogenic modes of transmission of the TSE prion disease i.e. friendly fire. I pondered this mode of transmission via the victims of sporadic FFI, sporadic GSS, could this be a iatrogenic event from someone sub-clinical with sFFI or sGSS ? what if?


Two decades have passed since Dr. Ironside first confirmed his first ten nvCJD victims in 1995. Ten years later, 2005, we had Dr. Gambetti and his first ten i.e. VPSPR in younger victims. now we know that indeed VPSPR is transmissible. yet all these TSE prion disease and victims in the USA and Canada are being pawned off as a spontaneous event, yet science has shown, the spontaneous theory has never been proven in any natural case of TSE prion disease, and scientist have warned, that they have now linked some sporadic CJD cases to atypical BSE, to atypical Scrapie, and to CWD, yet we don’t here about this in the public domain. We must make all human and animal TSE prion disease reportable in every age group, in ever state and internationally, we must have a serious re-evaluation and testing of the USA cattle herds, and we must ban interstate movement of all cervids. Any voluntary effort to do any of this will fail. Folks, we have let the industry run science far too long with regards to the TSE prion disease. While the industry and their lobbyist continues to funnel junk science to our decision policy makers, Rome burns. ...end




Sunday, June 29, 2014


Transmissible Spongiform Encephalopathy TSE Prion Disease North America 2014







Monday, June 02, 2014


Confirmed Variant CJD Case in Texas





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