Health knowledge made personal
Join this community!
› Share page:
Go
Search posts:

A closer look at prion strains Characterization and important implications

Posted Mar 05 2013 6:18pm
Prion 7:2, 99–108; March/April 2013; © 2013 Landes Bioscience



mini-Rev iew Mini-REVIEW



A closer look at prion strains



Characterization and important implications



Laura Solforosi,†,* Michela Milani,† Nicasio Mancini, Massimo Clementi and Roberto Burioni


Laboratory of Microbiology and Virology; University Vita-Salute San Raffaele; Milan, Italy


†These authors contributed equally to this work.


Keywords: cellular prion protein (PrPC), scrapie prion protein (PrPSc), transmissible spongiform encephalopathies (TSEs), prion strains, strain mutation, variant Creutzfeldt-Jakob disease, sporadic Creutzfeldt-Jakob disease


Abbreviations: PrPC, cellular prion protein; PrPSc, scrapie prion protein; TSEs, transmissible spongiform encephalopathies; TME, transmissible mink encephalopathy; CJD, Creutzfeldt-Jakob disease; sCJD, sporadic CJD; vCJD, variant CJD; FFI, fatal familial insomnia; BSE, bovine spongiform encephalopathy; CWD, chronic wasting disease; PK, proteinase K; SAF, scrapie-associated fibrils; CNS, central nervous system; WB, western blot; PE, phosphatidylethanolamine; sPMCA, serial protein misfolding cyclic amplification; CPA, cell panel assay





Prions are infectious proteins that are responsible for transmissible spongiform encephalopathies (TSEs) and consist primarily of scrapie prion protein (PrPSc), a pathogenic isoform of the host-encoded cellular prion protein (PrPC). The absence of nucleic acids as essential components of the infectious prions is the most striking feature associated to these diseases. Additionally, different prion strains have been isolated from animal diseases despite the lack of DNA or RNA molecules. Mounting evidence suggests that prion-strain-specific features segregate with different PrPSc conformational and aggregation states.



Strains are of practical relevance in prion diseases as they can drastically differ in many aspects, such as incubation period, PrPSc biochemical profile (e.g., electrophoretic mobility and glycoform ratio) and distribution of brain lesions. Importantly, such different features are maintained after inoculation of a prion strain into genetically identical hosts and are relatively stable across serial passages.



This review focuses on the characterization of prion strains and on the wide range of important implications that the study of prion strains involves.



Introduction



Transmissible spongiform encephalopathies (TSEs) or prion diseases, such as Creutzfeldt-Jakob disease (CJD) in human, bovine spongiform encephalopathy (BSE) in cattle, chronic wasting disease (CWD) in cervids and scrapie in sheep, are a group of fatal neurodegenerative disorders. The major neuropathological hallmarks of TSEs are extensive spongiosis, neuronal cell loss in the central nervous system, gliosis,1 and deposition of amyloid plaques.2



*Correspondence to: Laura Solforosi; Email: solforosi.laura@hsr.it Submitted: 08/13/12; Revised: 12/20/12; Accepted: 01/03/13 http://dx.doi.org/10.4161/pri.23490



Prions are infectious proteins that are responsible for transmissible spongiform encephalopathies (TSEs) and consist primarily of scrapie prion protein (PrPSc), a pathogenic isoform of the host-encoded cellular prion protein (PrPC). The absence of nucleic acids as essential components of the infectious prions is the most striking feature associated to these diseases. Additionally, different prion strains have been isolated from animal diseases despite the lack of DNA or RNA molecules. Mounting evidence suggests that prion-strain-specific features segregate with different PrPSc conformational and aggregation states.



Strains are of practical relevance in prion diseases as they can drastically differ in many aspects, such as incubation period, PrPSc biochemical profile (e.g., electrophoretic mobility and glycoform ratio) and distribution of brain lesions. Importantly, such different features are maintained after inoculation of a prion strain into genetically identical hosts and are relatively stable across serial passages.



This review focuses on the characterization of prion strains and on the wide range of important implications that the study of prion strains involves. ...




snip...




This classification arises from the hypothesis that if the polymorphism 129 can modulate the phenotype of the familial prion diseases (fCJD and FFI, as explained earlier in this review), then probably it can modulate also that of sporadic prion diseases, justifying their heterogeneity. According to this hypothesis, the cases affected by sCJD were divided into six groups according to the genotype of the polymorphism in position 129 and the type of PrPSc. Then, the phenotypes of every group were analyzed to evaluate the homogeneity within every group. The results have permitted a molecular sub-classification of the sCJD.90,91 However, this classification seems not to be sufficient to explain the complexity of the sporadic form of CJD. In fact, in some molecular subtypes, additional variants have been reported, such as MM or VV patients with amyloid plaques, which are absent in the majority of patients with these genotypes.44 Moreover, among patients belonging to the same subgroup, important phenotypic differences can be found, such as, for instance, the extent of neuronal loss or PrPSc deposition differences.92




Even at the biochemical level the complexity is higher: indeed, aside from the migratory differences of the PrPSc of types 1 and 2, there are other properties that could be important during the propagation of the strain, like the presence of other fragments derived from differential cleavage at the C- and N-terminus of the protein, which probably coincide with the presence of other forms of PrPSc with different resistance to PK digestion.44 All these molecular classifications are based upon the principle that in all CNS districts the type of PrPSc is the same, but there are pieces of evidence pointing to the fact that different types of PrPSc can be found in different brain areas.64,93 The first evidence of the presence of more than one form of PrPSc in the brain of a sCJD patient was reported by Puoti in 1999.94 These different types of PrPSc can be found to coexist in the same brain region or they can infect distinct districts. Such co-infection influences the vacuolization and the amyloid aggregates formation.95 Even the ratio between the different glycoforms is determined in a regionspecific manner according to the type of PrPSc (1 or 2) and the genotype of codon 129.




The high degree of phenotypic heterogeneity characterizing sCJD90 can lead to the conclusion that transmission studies will probably identify a broad panel of different prions with a great divergence between strains. However, quite surprisingly, many of the recent studies focusing on the characterization of sCJD subtypes have shown that there is a strong tendency to converge to a limited number of strains. This aspect can find an explanation considering the selection conditions, already described in this review, mediated by the environment in which the prion replicates and by the differences in the amino acid sequence of the PrPC. In particular, studies with bank voles96 and mice97 lead to results that support the idea that there are two principal strains responsible of the sCJD, M1 and V2, and two potential strains, M2 and V1, which need further studies to be confirmed.




Different is the case of vCJD. vCJD has been observed in 12 different countries, but in every registered case the same clinical and pathological characteristics have been found.39 In particular, the PrPSc responsible of the vCJD shows a peculiar WB profile, with the unglycosylated form of the protease-resistant PrPSc of 19 kDa (type 2) and a higher representation of the diglycosilated PrPSc (PrPSc 2B) compared with sCJD.39 Nevertheless, using specific antibodies against type 1 PrPSc, a small amount of PrPSc type 1 with a high percentage of diglycosilated form can be detected in association with PrPSc 2B.98 The 2B type is a useful marker for identifying the replication of BSE prions also in other species, including non-human primates.99 In addition, unlike sporadic and genetic CJD, in vCJD the same biological marker (2B type) has been found in all the analyzed brain areas.100 This strong biochemical and pathological homogeneity is in agreement with the hypothesis of the existence of a unique strain. However, unexpectedly, typization experiments of the strains in different transgenic models have given divergent results. In one of these studies, in a context of homotropic transmission, transgenic mice expressing high levels of human PrPC-M129 were inoculated with vCJD isolates coming from France and from the UK.101 All of the French isolates propagated as vCJD, with abundant amyloid plaques and presence of PrPSc 2B.102 Instead, the isolates from the UK led to the propagation of either vCJD or sCJD.103 In particular, the incubation time was shorter and the lesion profile was different compared with the one obtained with the propagation of the classical vCJD strain. Moreover, early replication of the typical agent of the vCJD in lymphoid tissues was detected, indicating that both strains were present in the inoculum.




This new strain with phenotypical features that were similar to sCJD was found to be of type 1 and the transmission in transgenic mice expressing the bovine PrPC failed, unlike the vCJD classical strain (Type 2B).26 The idea that the infection of vCJD contains a minor component of sCJD prions is supported by many pieces of evidence such as the presence of this prion strain at the first passage or the persistence of both types of PrPSc through serial passages in mice.98 In conclusion, although vCJD is one of the most standardized phenotypes among the prion human diseases characterized by a typical form of PrPSc, the transmission studies of vCJD have shown the great potential of divergence of prions, contrary to the results obtained from the studies of sCJD. This data challenge our ability to recognize the pathologies that can derive from the divergence of the BSE strains when they infect humans, both at the pathological and at the biochemical level.





Conclusion





The discovery of prions has led to new interpretations of the pathogenetic mechanism of protein misfolding diseases. Indeed, the common thought was that a protein misfolding disease could only be caused by a mutation in the primary sequence of an endogenous protein, but the discovery of prions changed this view. In fact, it was demonstrated that a seed of misfolded protein can arise from an exogenous infectious protein, which is able to act as a template or as a catalyst for the formation of new aberrant protein.5,6 Importantly, new evidence shows how processes similar to those described for prions could be implicated in the propagation of misfolded proteins of other neurodegenerative pathologies like Alzheimer disease, Parkinson disease, Huntington disease and amyotrophic lateral sclerosis.104,105




Certainly, one of the most puzzling aspects in the prion field is the existence of different strains of an infectious protein. Nevertheless, such diversity can be accommodated within the protein-only hypothesis, as several robust pieces of experimental evidence indicate that strain-specificity is encoded at the level of the different conformations that the pathogenic protein can adopt. The identification of factors and mechanisms influencing the generation of new prion strains or the selection, from a conformationally heterogeneous PrPSc population, of the most suitable prion conformation in a specific environment, represents an important milestone toward the understanding of the mechanisms of prion strain diversity, which can have fundamental clinical and therapeutic implications. Although considerable advances have been made in the understanding of the phenomenon of prion strains, many pieces of information are still missing, foremost among them the definitive evidence for the structural nature of the differences between prion strains.



















Thursday, February 21, 2013


National Prion Disease Pathology Surveillance Center Cases Examined January 16, 2013









16 YEAR OLD SPORADIC FFI ?


Monday, January 14, 2013


Gambetti et al USA Prion Unit change another highly suspect USA mad cow victim to another fake name i.e. sporadic FFI at age 16 CJD Foundation goes along with this BSe









Sunday, February 10, 2013


Creutzfeldt-Jakob disease (CJD) biannual update (February 2013) Infection report/CJD











*** The discovery of previously unrecognized prion diseases in both humans and animals (i.e., Nor98 in small ruminants) demonstrates that the range of prion diseases might be wider than expected and raises crucial questions about the epidemiology and strain properties of these new forms. We are investigating this latter issue by molecular and biological comparison of VPSPr, GSS and Nor98.







VARIABLY PROTEASE-SENSITVE PRIONOPATHY IS TRANSMISSIBLE ...price of prion poker goes up again $




OR-10: Variably protease-sensitive prionopathy is transmissible in bank voles




Romolo Nonno,1 Michele Di Bari,1 Laura Pirisinu,1 Claudia D’Agostino,1 Stefano Marcon,1 Geraldina Riccardi,1 Gabriele Vaccari,1 Piero Parchi,2 Wenquan Zou,3 Pierluigi Gambetti,3 Umberto Agrimi1 1Istituto Superiore di Sanità; Rome, Italy; 2Dipartimento di Scienze Neurologiche, Università di Bologna; Bologna, Italy; 3Case Western Reserve University; Cleveland, OH USA




Background. Variably protease-sensitive prionopathy (VPSPr) is a recently described “sporadic”neurodegenerative disease involving prion protein aggregation, which has clinical similarities with non-Alzheimer dementias, such as fronto-temporal dementia. Currently, 30 cases of VPSPr have been reported in Europe and USA, of which 19 cases were homozygous for valine at codon 129 of the prion protein (VV), 8 were MV and 3 were MM. A distinctive feature of VPSPr is the electrophoretic pattern of PrPSc after digestion with proteinase K (PK). After PK-treatment, PrP from VPSPr forms a ladder-like electrophoretic pattern similar to that described in GSS cases. The clinical and pathological features of VPSPr raised the question of the correct classification of VPSPr among prion diseases or other forms of neurodegenerative disorders. Here we report preliminary data on the transmissibility and pathological features of VPSPr cases in bank voles.




Materials and Methods. Seven VPSPr cases were inoculated in two genetic lines of bank voles, carrying either methionine or isoleucine at codon 109 of the prion protein (named BvM109 and BvI109, respectively). Among the VPSPr cases selected, 2 were VV at PrP codon 129, 3 were MV and 2 were MM. Clinical diagnosis in voles was confirmed by brain pathological assessment and western blot for PK-resistant PrPSc (PrPres) with mAbs SAF32, SAF84, 12B2 and 9A2.




Results. To date, 2 VPSPr cases (1 MV and 1 MM) gave positive transmission in BvM109. Overall, 3 voles were positive with survival time between 290 and 588 d post inoculation (d.p.i.). All positive voles accumulated PrPres in the form of the typical PrP27–30, which was indistinguishable to that previously observed in BvM109 inoculated with sCJDMM1 cases.




In BvI109, 3 VPSPr cases (2 VV and 1 MM) showed positive transmission until now. Overall, 5 voles were positive with survival time between 281 and 596 d.p.i.. In contrast to what observed in BvM109, all BvI109 showed a GSS-like PrPSc electrophoretic pattern, characterized by low molecular weight PrPres. These PrPres fragments were positive with mAb 9A2 and 12B2, while being negative with SAF32 and SAF84, suggesting that they are cleaved at both the C-terminus and the N-terminus. Second passages are in progress from these first successful transmissions.




Conclusions. Preliminary results from transmission studies in bank voles strongly support the notion that VPSPr is a transmissible prion disease. Interestingly, VPSPr undergoes divergent evolution in the two genetic lines of voles, with sCJD-like features in BvM109 and GSS-like properties in BvI109.




The discovery of previously unrecognized prion diseases in both humans and animals (i.e., Nor98 in small ruminants) demonstrates that the range of prion diseases might be wider than expected and raises crucial questions about the epidemiology and strain properties of these new forms. We are investigating this latter issue by molecular and biological comparison of VPSPr, GSS and Nor98.












Wednesday, March 28, 2012


VARIABLY PROTEASE-SENSITVE PRIONOPATHY IS TRANSMISSIBLE, price of prion poker goes up again $









*** The discovery of previously unrecognized prion diseases in both humans and animals (i.e., Nor98 in small ruminants) demonstrates that the range of prion diseases might be wider than expected and raises crucial questions about the epidemiology and strain properties of these new forms. We are investigating this latter issue by molecular and biological comparison of VPSPr, GSS and Nor98.




*** atypical Nor-98 Scrapie has spread from coast to coast in the USA 2012



NIAA Annual Conference April 11-14, 2011



San Antonio, Texas










Thursday, February 14, 2013


The Many Faces of Mad Cow Disease Bovine Spongiform Encephalopathy BSE and TSE prion disease









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









FSIS, USDA, REPLY TO SINGELTARY









U.S.A. 50 STATE BSE MAD COW CONFERENCE CALL Jan. 9, 2001












Wednesday, February 16, 2011


IN CONFIDENCE


SCRAPIE TRANSMISSION TO CHIMPANZEES


IN CONFIDENCE









why do we not want to do TSE transmission studies on chimpanzees $




5. A positive result from a chimpanzee challenged severly would likely create alarm in some circles even if the result could not be interpreted for man. I have a view that all these agents could be transmitted provided a large enough dose by appropriate routes was given and the animals kept long enough. Until the mechanisms of the species barrier are more clearly understood it might be best to retain that hypothesis.



snip...



R. BRADLEY










Monday, April 25, 2011


Experimental Oral Transmission of Atypical Scrapie to Sheep


Volume 17, Number 5-May 2011









Sunday, April 18, 2010


SCRAPIE AND ATYPICAL SCRAPIE TRANSMISSION STUDIES A REVIEW 2010









Monday, March 19, 2012


Infectivity in Skeletal Muscle of Cattle with Atypical Bovine Spongiform Encephalopathy


PLoS One. 2012; 7(2): e31449.









***The pathology features of Nor98 in the cerebellum of the affected sheep showed similarities with those of sporadic Creutzfeldt-Jakob disease in humans.









*** Intriguingly, these conclusions suggest that some pathological features of Nor98 are reminiscent of Gerstmann-Sträussler-Scheinker disease.


119









*** These observations support the view that a truly infectious TSE agent, unrecognized until recently, infects sheep and goat flocks and may have important implications in terms of scrapie control and public health.









Friday, February 08, 2013


*** Behavior of Prions in the Environment: Implications for Prion Biology









Friday, November 09, 2012


*** Chronic Wasting Disease CWD in cervidae and transmission to other species









Sunday, November 11, 2012


*** Susceptibilities of Nonhuman Primates to Chronic Wasting Disease November 2012









Friday, December 14, 2012


Susceptibility Chronic Wasting Disease (CWD) in wild cervids to Humans 2005 - December 14, 2012









Wednesday, May 16, 2012


Alzheimer’s disease and Transmissible Spongiform Encephalopathy prion disease, Iatrogenic, what if ?


Proposal ID: 29403









Wednesday, September 21, 2011


PrioNet Canada researchers in Vancouver confirm prion-like properties in Amyotrophic Lateral Sclerosis (ALS)









Friday, February 15, 2013


Scottish TSE Network November Symposium Announcement Event: 12 November 2012 Title: Is Alzheimer’s Disease a transmissible disease?


SUMMARY









15 November 1999


British Medical Journal


vCJD in the USA * BSE in U.S.









2 January 2000


British Medical Journal


U.S. Scientist should be concerned with a CJD epidemic in the U.S., as well









2001


PDF]Freas, William TSS SUBMISSION


File Format: PDF/Adobe Acrobat - Page 1. J Freas, William


To: Subject: Terry S. Singeltary Sr. [flounder@wt.net]


Monday, January 08,200l 3:03 PM freas ...









Diagnosis and Reporting of Creutzfeldt-Jakob Disease Singeltary, Sr et al. JAMA.2001; 285: 733-734. Vol. 285 No. 6, February 14, 2001 JAMA


Diagnosis and Reporting of Creutzfeldt-Jakob Disease


To the Editor: In their Research Letter, Dr Gibbons and colleagues1 reported that the annual US death rate due to Creutzfeldt-Jakob disease (CJD) has been stable since 1985. These estimates, however, are based only on reported cases, and do not include misdiagnosed or preclinical cases. It seems to me that misdiagnosis alone would drastically change these figures. An unknown number of persons with a diagnosis of Alzheimer disease in fact may have CJD, although only a small number of these patients receive the postmortem examination necessary to make this diagnosis. Furthermore, only a few states have made CJD reportable. Human and animal transmissible spongiform encephalopathies should be reportable nationwide and internationally.


Terry S. Singeltary, Sr Bacliff, Tex


1. Gibbons RV, Holman RC, Belay ED, Schonberger LB. Creutzfeldt-Jakob disease in the United States: 1979-1998. JAMA. 2000;284:2322-2323.




FREE FULL TEXT











26 March 2003



Terry S. Singeltary, retired (medically) CJD WATCH



I lost my mother to hvCJD (Heidenhain Variant CJD). I would like to comment on the CDC's attempts to monitor the occurrence of emerging forms of CJD. Asante, Collinge et al [1] have reported that BSE transmission to the 129-methionine genotype can lead to an alternate phenotype that is indistinguishable from type 2 PrPSc, the commonest sporadic CJD. However, CJD and all human TSEs are not reportable nationally. CJD and all human TSEs must be made reportable in every state and internationally. I hope that the CDC does not continue to expect us to still believe that the 85%+ of all CJD cases which are sporadic are all spontaneous, without route/source. We have many TSEs in the USA in both animal and man. CWD in deer/elk is spreading rapidly and CWD does transmit to mink, ferret, cattle, and squirrel monkey by intracerebral inoculation. With the known incubation periods in other TSEs, oral transmission studies of CWD may take much longer. Every victim/family of CJD/TSEs should be asked about route and source of this agent. To prolong this will only spread the agent and needlessly expose others. In light of the findings of Asante and Collinge et al, there should be drastic measures to safeguard the medical and surgical arena from sporadic CJDs and all human TSEs. I only ponder how many sporadic CJDs in the USA are type 2 PrPSc?











2009




14th ICID International Scientific Exchange Brochure -


Final Abstract Number: ISE.114


Session: International Scientific Exchange


Transmissible Spongiform encephalopathy (TSE) animal and human TSE in North America update October 2009


T. Singeltary


Bacliff, TX, USA


Background:


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


Methods:


12 years independent research of available data


Results:


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


Conclusion:


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










Plosone



re-Human Prion Diseases in the United States Posted by flounder on 01 Jan 2010 at 18:11 GMT


I kindly disagree with your synopsis for the following reasons ;









Sunday, August 21, 2011


The British disease, or a disease gone global, The TSE Prion Disease


(see video here)









U.S.A. HIDING MAD COW DISEASE VICTIMS AS SPORADIC CJD ?


(see video at bottom)









Sunday, September 6, 2009


MAD COW USA 1997


(SEE SECRET VIDEO)










Creutzfeldt-Jakob Disease Public Health Crisis




















O.K. let's compare some recent cases of this prionpathy in other countries besides Gambetti's first 10 recently, that he claims is a spontaneous event, from a genetic disorder, that is not genetic, but sporadic, that is related to no animal TSE in North America, or the world. ...










Wednesday, October 27, 2010


A novel variant of human disease with a protease-sensitive prion protein and heterozygosity methionine/valine at codon 129: Case report















Sunday, August 09, 2009


CJD...Straight talk with...James Ironside...and...Terry Singeltary... 2009










Tuesday, August 18, 2009


BSE-The Untold Story - joe gibbs and singeltary 1999 – 2009










Friday, November 30, 2007


CJD QUESTIONNAIRE USA CWRU AND CJD FOUNDATION













DEEP THROAT TO TSS 2000-2001 (take these old snips of emails with how ever many grains of salt you wish. ...tss)


The most frightening thing I have read all day is the report of Gambetti's finding of a new strain of sporadic cjd in young people...Dear God, what in the name of all that is holy is that!!! If the US has different strains of scrapie.....why??than the UK...then would the same mechanisms that make different strains of scrapie here make different strains of BSE...if the patterns are different in sheep and mice for scrapie.....could not the BSE be different in the cattle, in the mink, in the humans.......




I really think the slides or tissues and everything from these young people with the new strain of sporadic cjd should be put up to be analyzed by many, many experts in cjd........bse.....scrapie Scrape the damn slide and put it into mice.....wait.....chop up the mouse brain and and spinal cord........put into some more mice.....dammit amplify the thing and start the damned research.....This is NOT rocket science...we need to use what we know and get off our butts and move....the whining about how long everything takes.....well it takes a whole lot longer if you whine for a year and then start the research!!!




Not sure where I read this but it was a recent press release or something like that: I thought I would fall out of my chair when I read about how there was no worry about infectivity from a histopath slide or tissues because they are preserved in formic acid, or formalin or formaldehyde.....for God's sake........ Ask any pathologist in the UK what the brain tissues in the formalin looks like after a year.......it is a big fat sponge...the agent continues to eat the brain ......you can't make slides anymore because the agent has never stopped........and the old slides that are stained with Hemolysin and Eosin......they get holier and holier and degenerate and continue...what you looked at 6 months ago is not there........Gambetti better be photographing every damned thing he is looking at.....




Okay, you need to know. You don't need to pass it on as nothing will come of it and there is not a damned thing anyone can do about it. Don't even hint at it as it will be denied and laughed at.......... USDA is gonna do as little as possible until there is actually a human case in the USA of the nvcjd........if you want to move this thing along and shake the earth....then we gotta get the victims families to make sure whoever is doing the autopsy is credible, trustworthy, and a saint with the courage of Joan of Arc........I am not kidding!!!! so, unless we get a human death from EXACTLY the same form with EXACTLY the same histopath lesions as seen in the UK nvcjd........forget any action........it is ALL gonna be sporadic!!!




And, if there is a case.......there is gonna be every effort to link it to international travel, international food, etc. etc. etc. etc. etc. They will go so far as to find out if a sex partner had ever traveled to the UK/europe, etc. etc. .... It is gonna be a long, lonely, dangerous twisted journey to the truth. They have all the cards, all the money, and are willing to threaten and carry out those threats....and this may be their biggest downfall...




Thanks as always for your help. (Recently had a very startling revelation from a rather senior person in government here..........knocked me out of my chair........you must keep pushing. If I was a power person....I would be demanding that there be a least a million bovine tested as soon as possible and agressively seeking this disease. The big players are coming out of the woodwork as there is money to be made!!! In short: "FIRE AT WILL"!!! for the very dumb....who's "will"! "Will be the burden to bare if there is any coverup!"




again it was said years ago and it should be taken seriously....BSE will NEVER be found in the US! As for the BSE conference call...I think you did a great service to freedom of information and making some people feign integrity...I find it scary to see that most of the "experts" are employed by the federal government or are supported on the "teat" of federal funds. A scary picture! I hope there is a confidential panel organized by the new government to really investigate this thing.




You need to watch your back........but keep picking at them.......like a buzzard to the bone...you just may get to the truth!!! (You probably have more support than you know. Too many people are afraid to show you or let anyone else know. I have heard a few things myself... you ask the questions that everyone else is too afraid to ask.)




END...TSS






IN CONFIDENCE


Perceptions of unconventional slow virus in the USA


GAH WELLS


Report of a visit to the U.S.A. April-May 1989


3. Prof. A Robertson gave a brief account of BSE. The US approach was to accord it a very low profile indeed.


Dr. A Thiermann showed the picture in the ''Independent'' with cattle being incinerated and thought this was a fantical incident to be avoided in the USA AT ALL COSTS.










Tuesday, November 02, 2010


IN CONFIDENCE


The information contained herein should not be disseminated further except on the basis of "NEED TO KNOW".


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










TSS

Post a comment
Write a comment: