Infectious Waste Fueling Alzheimer’s Disease, Autism

Reforming Policy, Practices Can Save Millions Of Lives

Neurodegenerative disease and autism have been surging around the world for the past 30 years. A man-made disaster is creating a public health disaster that’s still unfolding.

Neurotoxins are driving the epidemic more than age–in some countries than others. Teenagers are now dying of Creutzfeldt-Jakob disease–the most severe form of brain wasting disease.

Alzheimer’s disease alone is taking the lives of 50-100 million people around the world now. As millions die, even more will be diagnosed. Millions more are suffering in silence with a misdiagnosis or no diagnosis. Misinformation and mismanagement are fanning the flames.

Despite millions of deaths, experts suggest that the prevalence of the disease will quadruple by 2050, if not sooner. Unfortunately, there is a growing stack of evidence that Alzheimer’s disease, Parkinson’s disease and other brain diseases are transmissible. There is zero evidence to the contrary. Victims also are being misdiagnosed and undiagnosed at an alarming rate.

 

Prions

A variety of factors can trigger neurodegenerative disease, including genetics, head trauma and neurotoxins. Deadly, self-replicating proteins appear to be one of those neurotoxins.

Prions (PREE-ons) are a deadly and unstoppable form of protein that migrates, mutates, multiplies and kills with unparalleled efficiency. Dr. Prusiner coined the term as a contraction for proteinaceous infectious particlePrions cause fatal neurodegenerative disease in humans and animals by converting the cellular version of prion protein into a toxic form that erodes the brain and body. Prions migrate, mutate and multiply. They get stronger as they move up the food chain. At the top of the food chain, humans are highly vulnerable to prion disease. The prions shed from humans are the deadliest and most aggressive. Mismanaging human prions is a big mistake.

Alzheimer's disease and prion disease

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing prions and prion disease. President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. Unfortunately, Prusiner’s science is being ignored and we all are facing a public health disaster because of the negligence and reckless disregard for public health.

Prions are a formidable threat. When the U.S. government enacted the Bioterrorism Preparedness and Response Act of 2002, it included a provision to halt research on infectious prions in all but two laboratories. It classified prions as select agents that pose an extreme risk to food, water and health systems. Unfortunately, the Center For Disease Control quietly took prions off the list about two years ago because the classification criminalized multi-billion dollar industries and many industry practices.

Prion Disease

Prion disease also is known as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” Prusiner claims that all forms of TSE are caused by infectious prions. Prion disease often is described as a wasting disease that causes a loss of body mass and brain mass.

TSE is a spectrum disease that varies in severity and symptoms. It depends on which region of the brain is impacted first and by what prion mutation. Few cases are identical in terms of symptoms and diagnoses. When the presenting symptom is memory loss, the diagnoses flow along the following chart.

prion disease and CJD

In humans, the prion spectrum includes Alzheimer’s disease, Parkinson’s disease and an extremely aggressive version known as Creutzfeldt-Jakob disease. The difference between these diseases is very slight and often indistinguishable to neurologists. For example, millions of people have been told that they have Alzheimer’s disease, when, in reality, it’s CJD–where it’s clearly infectious.

“It is well known that CJD is transmissible via surgical or medical procedures involving prion-infected brain tissue. Our finding of infectious prions in skin is important since it not only raises concerns about the potential for disease transmission via common surgeries not involving the brain, but also suggests that skin biopsies and autopsies may enhance pre-mortem and post-mortem CJD diagnosis,” said Wenquan Zou, Associate Professor of Pathology and Neurology and Associate Director of the National Prion Disease Pathology Surveillance Center at Case Western Reserve School of Medicine. “The level of prion infectivity detected in CJD skin was surprisingly significant, but still much lower than that in CJD brains. Further investigation is necessary to determine whether extra precautions should be taken during non-neurosurgeries of CJD patients, especially when surgical instruments will be reused.”

Prion infectivity is highly concentrated in brain tissue, but it’s also in all bodily fluids and tissue. CJD transmission has occurred after patients were exposed to surgical tools previously contaminated by CJD victims. It’s also happening due to many other pathways.

According to neuroscientists Dr. Laura Manuelidis, at least 25 percent of Alzheimer’s disease diagnoses are actually CJD.

CJD, without dispute, is extremely infectious to caregivers and loved ones, but it has not been declared a reportable disease across the U.S. and many other nations.

Millions of cases of deadly CJD are being misdiagnosed as Alzheimer’s disease. Millions of patients and caregivers are being misinformed, misguided and exposed to an aggressive prion disease.

Read The Full Story About the Neurodegenerative Disease epidemic.

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Vancouver Spreading Infectious Waste Upstream

Sewage Sludge Contaminating Water Supplies

Residents of Canada’s Nicola Valley have said that something stinks about biosolids dumped near homes, rivers, aquifers and crops in their region. They set up roadblocks to stop the practice. A powerful new report backs them up.

John Werring, Senior Science Advisor with the environmental group, The Suzuki Foundation, recently came to the Nicola Valley where he met with some of the area Chiefs and with members of the Friends of the Nicola Valley Society. He listened to the concerns they raised about the land application of biosolids. He took samples from some of the biosolids which had been dumped in this beautiful alpine valley.

land application sewage sludge

Tests showed that the biosolids contained alarmingly high amounts of dangerous toxins. In fact, the “soils” tested indicate an area that could be classified as a “contaminated site” according to the BC Contaminated Sites Regulations guidelines.

The samples exceed the BC limits for contaminated sites under Schedules 4 and 7 of the BC Contaminated Sites Regulations on several parameters. The testing  shows that samples of biosolids taken from the Nicola Valley contained several dangerous toxins, including cadmium, uranium, lead, copper, mercury, tin, zinc, dichlorophenol, methylphenol, selenium, sodium, fecal coliform and much more.

Unfortunately, we also know that biosolids contain a deadly and unstoppable contagion known as a prion. Prions are associated with a global epidemic of neurological disease among people, wildlife and livestock. Prions are associated with Alzheimer’s disease, mad cow disease, chronic wasting disease, autism and other neurological maladies known as transmissible spongiform encephalopathies (TSE). The wastewater industry and governments prefer not to discuss prions or manage the killer proteins.

chronic wasting disease caused by prions

TSEs are caused by a deadly protein called a prion (PREE-on). As such, TSEs also are referred to as prion disease. The critical factor is that prions are unstoppable. The pathogen spreads through the bodily fluids and cell tissue of its victims. Blood, saliva, mucus, milk, urine and feces carry deadly prions from victims. All tissue is infectious just because of the contact with the contaminated blood.

TSEs also include Creutzfeldt-Jakob disease, Parkinson’s, Huntington’s, mad cow disease and chronic wasting disease in the deer family. Few, if any, mammals are immune. There is no cure.

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing deadly prions and prion disease. President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. According to Prusiner, TSEs all are on the same disease spectrum, which is more accurately described as prion disease. He claims that all TSEs are caused by prions.

prion disease epidemic

Prions are unstoppable and the pathogen spreads through the bodily fluids and cell tissue of its victims. Prions shed from humans are the most deadly mutation. They demand more respect than radiation. Infected surgical instruments, for example, are impossible to sterilize and hospitals throw them away. Prions are in the blood, saliva, urine, feces, mucus, and bodily tissue of its victims. Many factors are contributing to the epidemic. Prions are now the X factor. Industry and government are not accounting for them or regulating them. They are ignoring the threat completely, which violates the Bioterrorism Preparedness and Response Act of 2002 in the United States. Other nations also are ignoring laws developed to protect food, air and water.

“There is now real evidence of the potential transmissibility of Alzheimer’s disease,” says Thomas Wiesniewski M.D. a prion and Alzheimer’s researcher at New York University School of Medicine. “In fact, this ability to transmit an abnormal conformation is probably a universal property of amyloid-forming proteins (prions).”

A new study published in the journal Nature renews concern about the transmissibility of Alzheimer’s disease between people. A second study by the same scientist in early 2016 adds to the stack of evidence.

Alzheimer's disease epidemic

These findings support the local First Nations, and Friends of the Nicola Valley’s position that the practice of land application of biosolids is far too risky to be continued. In fact, once again, it makes one wonder how the practice ever gained approval in the first place. Sewage dumping poses a direct threat to First Nations’ traditional life-ways, and it threatens the health of all citizens within the Nicola Valley. It also threatens everyone downstream with exposure to toxins and neurological disease.

“The independent tests confirm that biosolids must not be applied to land,” said Chief Aaron Sam. “Biosolids contaminate our lands and waters, and it has serious potential negative effects on fish, animals and plants, First Nations people are reliant on the land for food and medicines. Biosolids put the health of our community members at risk. We can no longer sit back while the Government of British Columbia ignores our Constitutionally protected rights to our title and rights. Published, independent science concludes that land application of biosolids is very dangerous. We now have numbers to substantiate that, and these test results were determined by an independent lab. It is time to start looking at real alternatives to land application. The time of cheap, dangerous toxic dispersal throughout rural areas is over. Cities will have to find a greener, sustainable method of dealing with their toxins.”

biosolids land application and disease

The Biosolids Controversy, Coverup

The following information comes directly from minutes of Metro Vancouver’s Utilities Committee. It describes the biosolids controversy from the eyes of public servants in Vancouver. The minutes have been revised at least once, so let’s say the minutes are dated May 15, 2015. Public safety appears to be a non-issue. 

In November 2014, Metro Vancouver became aware of a controversial biosolids composting project situated in the Merritt area. Biosolids from Regional District of Central Okanagan were being sent to a biosolids composting facility operated by a company called BioCentral. A second BioCentral facility was slated to receive biosolids from Abbotsford upon approval of the Land Application Plan (a requirement of the Organic Matter Recycling Regulation).

A group calling themselves Friends of the Nicola Valley, led by a resident of a 44lot subdivision in close proximity to the second site, began to protest the operation in November 2014. This included conducting interviews, lobbying First Nations in the area, starting a petition and creating a Facebook site which opposes biosolids application in general, not just the BioCentral facility. Although Metro Vancouver projects have been identified on the Facebook site of Friends of the Nicola Valley, Metro Vancouver has not been the principal target to date.

Rey Creek Ranch

Rey Creek Ranch is a property northwest of Merritt that used Metro Vancouver’s biosolids for fertilization periodically from 1997 to 2014. Currently Metro Vancouver has a contract with Sperling Hansen Associates Inc. (SHA) to apply biosolids at Rey Creek Ranch in 2015 for hayfield, range and transitional forest land application. In late January, SHA received a letter from the Interior Health Authority, which allowed the project to proceed subject to notification of neighbors, including the adjacent Lower Nicola Indian Band. In response to this notification, SHA received a letter from the Lower Nicola Indian Band, referencing Tsilhqot’in v British Columbia 2014 SCC 44, the recent Supreme Court decision regarding Aboriginal Rights and Title. The letter stated that based on their current understanding of the practice of biosolids use they are strongly opposed to biosolids operations until a meaningful dialogue with the Crown and Ministry regulators could be completed to address their concerns, and threatening action for continued operation or new activities without consultation. Biosolids deliveries to Rey Creek Ranch were halted on January 26 with the hope that a meeting could be convened in short order and Lower Nicola Indian Band’s technical concerns could be addressed. No meeting has been scheduled by the Band to date.

Nicola Ranch

Nicola Ranch is a property just east of Merritt that used Metro Vancouver’s biosolids for fertilization from 19982005. At the Ranch Manager’s request, Metro Vancouver had scheduled biosolids to be delivered to the Ranch in January 2015 for hayfield fertilization. The parties have determined not to proceed with the delivery at this time.

Local First Nations

On December 12, 2014, the five Chiefs of the Nicola Valley (Nooaitch, Lower Nicola, Shackan, Coldwater, and Upper Nicola Indian Bands), wrote to the Ministry of Environment, demanding that all current biosolids applications cease until the Crown and ministry regulators establish a meaningful dialogue resulting in the five Chiefs’ support. On February 12, 2015, the Union of BC Indian Chiefs (UBCIC) Chiefs Council passed a resolution directing the UBCIC Executive to work with the First Nations Summit and the BC Assembly of First Nations to assist the Nicola Chiefs in halting applications of biosolids in the Nicola Valley, in particular the BioCentral composting site, and immediately call on the Provincial Government to develop a provincial strategy for dealing with biosolids including considering modification of current legislation and regulations.

On March 10, members of these five First Nations, in coordination with the Friends of the Nicola Valley, established a blockade on Highway 8 into Merritt, to stop trucks delivering biosolids from Regional District of Central Okanagan to the BioCentral facility.

Since the controversy began, the Friends of the Nicola Valley have been opposing biosolids use, and the response by BioCentral, the MOE and Interior Health Authority has been very limited and has failed to reassure the Merritt community of biosolids safety. As public confidence and support is critical for biosolids application projects and many of Metro Vancouver’s biosolids projects are located within the Thompson Nicola Regional District (TNRD), these events have the potential to significantly impact our program. Metro Vancouver has been dumping biosolids as a fertilizer throughout the province for 24 years.

Metro Vancouver has the ability to divert biosolids for disposal in Hinton, Alberta, at a higher hauling cost. If Metro Vancouver is unable to send biosolids to Rey Creek Ranch, Nicola Ranch, and OK Ranch in 2015, and is not able to find other comparable land application sites, the total additional cost to the program is estimated to be $1.6 M.

As the current situation has the potential to continue to escalate and impact other project sites, inability to continue with the biosolids beneficial use program could result in additional costs of up to $5M per year for the next 3 years.

Learn more about the perils of sewage mismanagement

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Crossbow Communications specializes in issue management and public affairs. Alzheimer’s disease, Creutzfeldt-Jakob disease and the prion disease epidemic is one of our special areas of practice. Please contact Gary Chandler to join our coalition for reform gary@crossbow1.com. Stop prion disease.

Transmissibility Of Prion Disease In Soil

Sewage Sludge Expands Prion Pathways

Soil may serve as an environmental reservoir for prion infectivity and contribute to the horizontal transmission of prion diseases (transmissible spongiform encephalopathies [TSEs]) of sheep, deer, and elk. TSE infectivity can persist in soil for years, and we previously demonstrated that the disease-associated form of the prion protein binds to soil particles and prions adsorbed to the common soil mineral montmorillonite (Mte) retain infectivity following intracerebral inoculation. Here, we assess the oral infectivity of Mte- and soil-bound prions.

land application sewage sludge

We establish that prions bound to Mte are orally bioavailable, and that, unexpectedly, binding to Mte significantly enhances disease penetrance and reduces the incubation period relative to unbound agent. Cox proportional hazards modeling revealed that across the doses of TSE agent tested, Mte increased the effective infectious titer by a factor of 680 relative to unbound agent. Oral exposure to Mte-associated prions led to TSE development in experimental animals even at doses too low to produce clinical symptoms in the absence of the mineral.

We tested the oral infectivity of prions bound to three whole soils differing in texture, mineralogy, and organic carbon content and found soil-bound prions to be orally infectious. Two of the three soils increased oral transmission of disease, and the infectivity of agent bound to the third organic carbon-rich soil was equivalent to that of unbound agent. Enhanced transmissibility of soil-bound prions may explain the environmental spread of some TSEs despite the presumably low levels shed into the environment. Association of prions with inorganic microparticles represents a novel means by which their oral transmission is enhanced relative to unbound agent.

chronic wasting disease caused by prions

Transmissible spongiform encephalopathies (TSEs) are a group of incurable neurological diseases likely caused by a misfolded form of the prion protein. TSEs include scrapie in sheep, bovine spongiform encephalopathy (“mad cow” disease) in cattle, chronic wasting disease in deer and elk, and Creutzfeldt-Jakob disease in humans. Scrapie and chronic wasting disease are unique among TSEs because they can be transmitted between animals, and the disease agents appear to persist in environments previously inhabited by infected animals.

Soil has been hypothesized to act as a reservoir of infectivity and to bind the infectious agent. In the current study, we orally dosed experimental animals with a common clay mineral, montmorillonite, or whole soils laden with infectious prions, and compared the transmissibility to unbound agent. We found that prions bound to montmorillonite and whole soils remained orally infectious, and, in most cases, increased the oral transmission of disease compared to the unbound agent. The results presented in this study suggest that soil may contribute to environmental spread of TSEs by increasing the transmissibility of small amounts of infectious agent in the environment.

biosolids land application LASS

Citation: Johnson CJ, Pedersen JA, Chappell RJ, McKenzie D, Aiken JM (2007) Oral Transmissibility of Prion Disease Is Enhanced by Binding to Soil Particles. PLoS Pathog 3(7): e93. doi:10.1371/journal.ppat.0030093

Introduction

Bovine spongiform encephalopathy, human Creutzfeldt-Jakob disease and kuru, sheep scrapie, and chronic wasting disease of deer, elk, and moose belong to the class of fatal, infectious neurodegenerative diseases known as transmissible spongiform encephalopathies (TSEs) or prion diseases. The precise nature of the etiological agent of these diseases remains controversial, but most evidence points to a misfolded isoform of the prion protein (PrPTSE) as the major, if not sole, component of the pathogen.

Sheep scrapie and cervid (deer, elk, and moose) chronic wasting disease are distinct among TSEs because epizootics can be maintained by horizontal transmission from infected to naïve animals, and transmission is mediated, at least in part, by an environmental reservoir of infectivity. The presence of an environmental TSE reservoir impacts several epidemiological factors including contact rate (the frequency animals come in contact with the disease agent), duration of exposure (time period over which animals come in contact with the pathogen), and the efficiency of transmission (the probability that an exposed individual contracts the disease).

The oral route of exposure appears responsible for environmental transmission of chronic wasting disease and scrapie; the propagation of bovine spongiform encephalopathy epizootics (feeding TSE-infected meat and bonemeal to cattle); the appearance of variant Creutzfeldt-Jacob disease in humans and feline spongiform encephalopathy in cats (presumably by consumption of bovine spongiform encephalopathy–infected beef); the spread of kuru among the Fore of Papua New Guinea (ritualistic endocannibalism); and outbreaks of transmissible mink encephalopathy (TME) in farm-reared mink. Following consumption, TSE agent is sampled by gut-associated lymphoid tissue, such as Peyer’s patches or isolated lymphoid follicles, and accumulates in lymphatic tissues before entering the central nervous system via the enteric nervous system. While ingestion is a biologically relevant TSE exposure route, oral dosing is a factor of ~105 less efficient than intracerebral inoculation in inducing disease in rodent models. The amounts of TSE agent shed into the environment are presumably small. The assumed low levels of TSE agent in the environment and the inefficiency of oral transmission have led to uncertainty about the contribution of environmental reservoirs of infectivity to prion disease transmission.

prion disease epidemic

We and others have hypothesized that soil may serve as a reservoir of TSE infectivity. Deliberate and incidental ingestion of soil by ruminants can amount to hundreds of grams daily. Prions enter soil environments via decomposition of infected carcasses, alimentary shedding, deliberate burial of diseased carcasses/material and possibly, urinary excretion. TSE agent persists for years when buried in soil. The disease-associated prion protein sorbs to soil particles, and the interaction of PrPTSE with the common aluminosilicate clay mineral montmorillonite (Mte) is remarkably avid. Despite this strong binding, PrPTSE–Mte complexes are infectious when inoculated into brains of recipient animals.

For TSEs to be transmitted via ingestion of prion-contaminated soil, prions bound to soil components must remain infectious by the oral route of exposure. We therefore investigated the oral infectivity of Mte- and soil-bound prions. We examined the effects of prion source (viz. infected brain homogenate [BH] and purified PrPTSE) and dose on disease penetrance (proportion of animals eventually exhibiting clinical TSE symptoms) and incubation period (time to onset of clinical symptoms) in experiments with Mte. We investigated the oral infectivity of soil particle–bound prions to Syrian hamsters using four dosing regimes: (1) infected BH mixed with Mte (BH–Mte mixtures), (2) isolated complexes of purified PrPTSE bound to Mte (PrPTSE–Mte complexes), (3) purified PrPTSE mixed with Mte (PrPTSE–Mte mixtures), and (4) PrPTSE mixed with each of three whole soils (PrPTSE–soil mixtures). The rationale for each dosing regime is described below. Survival analysis was used to assess risk of clinical disease manifestation and quantify differences in effective titer. Application of survival analysis to oral bioassays of TSE transmissibility is discussed in Figure S1 and Text S1.

biosolids land application and disease

Oral Infectivity of BH–Mte Mixtures

To examine the effect of Mte on the oral transmissibility of prions in BH, we incubated infected BH with clay particles for 2 h to allow sorption of the agent; controls lacking Mte were treated identically [22]. Three doses of 10% BH (30, 3, and 0.3 μL) were assayed. Diminished gastrointestinal bioavailability was expected to be evidenced by significant lengthening of incubation period, reduced disease penetrance, or both. Binding of either 30 or 3 μL of brain material to Mte yielded disease penetrance and incubation periods similar to BH alone (Figure 1A and 1B), a finding consistent with our previous report that a substantial fraction of PrPTSE in clarified BH binds to Mte and that Mte-bound prions remain infectious [22].

No Loss of Oral TSE Transmissibility Following Sorption of Prions from Infected BH to Mte (BH–Mte Mixtures)

The oral transmissibility of prions in 30 (A) and 3 (B) μL was not diminished by dosing with Mte. Indicates non-TSE intercurrent death. Animals dosed with Mte alone remained healthy throughout the course of the experiment (unpublished data).

Surprisingly, at the lowest BH dose (0.3 μL, Figure 2), sorption of TSE agent to Mte enhanced transmission, increasing disease penetrance and shortening incubation period. Adjusted for the amount of BH administered and combined across doses, Mte significantly enhanced oral transmissibility (p < 0.0001). Survival analysis indicated the risk of clinical disease manifestation relative to Mte-free controls was 3.03 (95% confidence interval [CI]: 1.68, 5.45), signifying an increase in the effective titer of TSE agent. While the influence of Mte was significant when tested across all BH doses, the effect was most readily observed at 0.3 μL. The dose-dependent difference in the influence of Mte on transmissibility may be attributable to competition between macromolecules in BH (e.g., lipids, other proteins, nucleic acids) with PrPTSE for sorption sites on the clay surface. Such competition was evidenced by detection of unbound PrPTSE and other proteins in incubations of Mte with 30 and 3 μL BH (unpublished data).

Ingestion of Mte mixed with a lower dose of TSE-infected BH (0.3 μL) markedly shortens incubation period and increases disease penetrance relative to an equal amount of unbound BH. * indicates non-TSE intercurrent death. Animals dosed with Mte alone remained healthy throughout the course of the experiment (unpublished data).

Oral Infectivity of PrPTSE–Mte Complexes

To examine the influence of Mte on oral transmissibility without the interference of other macromolecules from brain homogenate, we purified PrPTSE and inoculated hamsters using two different dosing regimes. The first dosing regime (PrPTSE–Mte complexes) was designed to directly assay the infectivity of PrPTSE sorbed to Mte surfaces (i.e., the amount of unbound PrPTSE was minimized in treatments containing Mte). Purified PrPTSE was clarified to remove large aggregates, and after 2-h incubation with Mte, PrPTSE–Mte complexes were separated from unbound protein by centrifugation through a sucrose cushion [22]. Hamsters were orally challenged with the isolated PrPTSE–Mte complexes [22] or an amount of unbound clarified PrPTSE (200 or 20 ng) equivalent to that introduced into the clay suspension (Table 1). Immunoblot analysis of the inocula (Figure S2A) demonstrated that the amount of PrP in the unbound samples was not less than that in PrPTSE–Mte complexes.

Prions Adsorbed to Mte Clay Are Infectious Perorally

Sorption of PrPTSE to Mte dramatically enhanced prion disease transmission (Table 1). Approximately 38% of animals receiving 200 ng of unbound clarified PrPTSE exhibited clinical symptoms with an incubation period for infected animals of 203 ± 33 (mean ± standard deviation) days post inoculation (dpi). In contrast, all animals orally dosed with an equivalent amount of Mte-bound PrPTSE manifested disease symptoms (incubation period = 195 ± 37 dpi), an enhancement of transmission comparable to that observed for the lowest BH dose (Figure 2). Animals inoculated with Mte alone or 10-fold less unbound clarified PrPTSE (20 ng) remained asymptomatic throughout the course of the experiment (>365 dpi), whereas 20 ng of clarified PrPTSE adsorbed to Mte produced TSE infection in 17% of animals. These data establish not only that the Mte-bound prions remain infectious via the oral route of exposure, but that agent binding to Mte increases disease penetrance, enhancing the efficiency of oral transmission.

Oral Infectivity of PrPTSE–Mte Mixtures

The second oral dosing regime using purified PrPTSE (PrPTSE–Mte mixtures) was designed to ensure that treatments with and without Mte contained equivalent PrPTSE doses. These experiments differed from those above in two important aspects. First, PrPTSE–Mte complexes were not separated from suspension prior to inoculation so that comparable amounts of infectious agent were administered to both treatment groups. In the first dosing regime, some PrPTSE may have been lost during sedimentation of PrPTSE–Mte complexes (Figure S2A). Second, the purified prion preparation was not clarified and therefore contained a range of PrPTSE aggregate sizes. The sizes of PrPTSE aggregates attached to Mte particles were expected to be more heterogeneous than those in the first dosing regime.

Compared to Mte-free controls, administration of purified PrPTSE mixed with Mte increased disease penetrance at all doses and shorted incubation times in the 1-μg PrPTSE treatment (Figure 3A). At the two lower doses (0.1 and 0.01 μg PrPTSE), binding of the agent to Mte dramatically increased disease penetrance (31%) at PrPTSE doses failing to yield clinical infection in 31 of 32 animals in the absence of the clay mineral (Figure 3B and 3C). Comparison of the survival curves in Figure 3A and 3C indicates that the 0.01-μg PrPTSE–Mte mixture was at least as infectious as 1-μg PrPTSE Mte-free samples, suggesting that sorption of purified PrPTSE to Mte enhanced transmission by a factor of ≥100.

Figure 3. Concurrent Peroral Administration of Mte and PrPTSE Dramatically Increases Disease Penetrance at Agent Doses That Typically Fail to Produce Clinical Symptoms (PrPTSE–Mte Mixture)

Mte increases disease penetrance and shortens incubation periods associated with ingestion of 1 μg of purified PrPTSE. Concurrent peroral dosage of lower, typically subclinical doses of purified PrPTSE (0.1 or 0.01 μg, [B and C]) with Mte increases disease incidence. Animals dosed with Mte alone remained healthy throughout the course of the experiment (unpublished data).

To quantify the contributions to changes in relative risk of prion dose and agent sorption to Mte, we constructed a multivariate Cox proportional hazards model with two covariates: log10 PrPTSE dose and Mte presence (Table 2). Each log10 increase in PrPTSE dose multiplies the relative risk by a factor of ~2 (i.e., a 10-fold increase in dose approximately doubles the risk of infection). Notably, sorption of purified PrPTSE to Mte multiplies the relative risk by a factor of ~8. These values allowed computation of a multiplicative equivalence factor between PrPTSE dose and Mte presence in the inoculum. Expressed in terms of PrPTSE dose, addition of Mte to the inoculum is equivalent to multiplying the PrPTSE dose by a factor of 680 (95% CI 16, ∞); that is, inclusion of Mte increases the effective titer of a given PrPTSE dose by 680-fold. Estimates of effective titer span a wide range (95% CI 16, ∞), and the present data do not allow us to place an upper bound on the increased risk associated with the presence of Mte in a sample. At a minimum, effective titer increased by 1.2 orders of magnitude, but the effect could be substantially larger. The best estimate of the Cox analysis represents a 2.8 order-of-magnitude increase in effective titer.

Estimated Hazard Ratios due to Prion Dose and Mte Addition

Strain PropertiesOral administration of Mte-bound PrPTSE did not appear to alter strain properties. Following limited proteinase K (PK) digestion, many PrPTSE strains can be discriminated by the size and glycoform pattern of PK-resistant core of PrPTSE (PrP-res) [3336]. Strain differences are also manifested in specific clinical symptoms. At the conclusion of the oral transmission experiments described above, the brains of clinically infected animals were assayed for PrP-res by immunoblotting (Figure S3). Differences in the molecular mass and glycoform distribution of PrP-res were not apparent between the treatment groups. Furthermore, clinical presentation of disease (symptoms or length of clinically positive period) did not differ between treatments.

The experiments described above were conducted using the Hyper (HY) strain of hamster-adapted TME agent (PrPHY). To further examine the strain stability of Mte-bound PrPTSE, we employed the Drowsy (DY) strain of hamster-passaged TME agent (PrPDY) to investigate the molecular mass of PrP desorbed from Mte and the effect of this clay mineral on oral transmissibility [35,36]. We previously reported the N-terminal cleavage of PrPHY extracted from Mte yielding a product similar in size to PK-digested PrPHY [22]. PK digestion of PrPHY and PrPDY results in products of characteristically different molecular masses [35,36]: the length of the PrPHY digestion product exceeds that of PrPDY by at least ten amino acids [35,36]. We found that extraction of bound PrPDY from Mte resulted in a product similar in molecular mass to PrPDY cleaved by PK (Figure 4). These data are consistent with the idea that strain properties are preserved when PrPTSE binds to Mte. DY agent is not orally transmissible [37], and we find that sorption of DY to Mte does not facilitate oral transmission (Text S1).

BH from hamsters clinically affected with either HY or DY agents were incubated with Mte to allow binding. Desorbed proteins were analyzed by SDS-PAGE and immunoblotting. Cleavage patterns of PrPHY and PrPDY extracted from Mte parallel PK cleavage patterns for the respective proteins: cleaved PrPDY migrates further (corresponding to a 1- to 2-kDa molecular mass difference) than cleaved PrPHY. Immunoblot used the PrP-specific antibody 3F4.

Natural soils are composed of a complex mixture of inorganic and organic components of various particle sizes. Smectitic clays such as Mte are important constituents of many natural soils and contribute significantly to their surface reactivity [38]. In natural soils, metal oxide and organic matter often coat smectite surfaces and may alter their propensity to bind PrPTSE. Furthermore, additional sorbent phases may be important in the binding of TSE agents to whole soils. We previously demonstrated that PrPTSE binds to whole soils of varying texture, mineralogy, and organic carbon content [22]. To examine the impact of agent binding to whole soil on oral TSE transmission, we incubated 1 μg of purified PrPTSE with each of three whole soil samples (Elliot, Dodge, and Bluestem soils) to allow sorption, and then orally dosed hamsters with the PrPTSE–soil mixtures. Soil-bound TSE agent remained infectious perorally, and two of the soils significantly enhanced oral disease transmission (Figure 5). Hazard ratios between Elliot (4.76 [95% CI: 1.38–16.4], p = 0.019) and Bluestem (6.04 [95% CI: 1.59–22.9], p = 0.013) soils and unbound PrPTSE indicate a significant increase in transmissibility, but no difference for the Dodge soil (1.66 [95% CI: 0.52–1.66], p = 0.578). The hazard ratios for the Elliot and Bluestem soils did not differ from one another (0.79 [95% CI: 0.19–3.25], p = 0.543) indicating statistical equivalence in transmissibility. The limited numbers of animals in the treatment groups precluded derivation of a multiplicative equivalence factor to equate the presence of Elliot or Bluestem soil with dose of infectious agent; however, substantially more animals in the Elliot and Bluestem treatment groups (14 of 16 animals, 87.5% penetrance) displayed clinical symptoms compared to the unbound PrPTSE treatment group (two of eight animals, 25% penetrance).

Prions Bound to Whole Soils Remain Orally Infectious and Some Soils Increase Transmission

Three soils (Dodge, Elliot, and Bluestem) were incubated in the presence of purified PrPTSE. The samples were orally dosed into hamsters and found to remain orally infectious. Agent association with Elliot and Bluestem soils increases disease incidence, whereas Dodge soil does not influence disease transmission. Animals dosed with soil alone remained healthy throughout the course of the experiment (unpublished data).

These experiments address the critical question of whether soil particle–bound prions are infectious by an environmentally relevant exposure route, namely, oral ingestion. Oral infectivity of soil particle–bound prions is a conditio sine qua non for soil to serve as an environmental reservoir for TSE agent. The maintenance of infectivity and enhanced transmissibility when TSE agent is bound to the common soil mineral Mte is remarkable given the avidity of the PrPTSE–Mte interaction [22]. One might expect the avid interaction of PrPTSE with Mte to result in the mineral serving as a sink, rather than a reservoir, for TSE infectivity. Our results demonstrate this may not be the case. Furthermore, sorption of prions to complex whole soils did not diminish bioavailability, and in two of three cases promoted disease transmission by the oral route of exposure. While extrapolation of these results to environmental conditions must be made with care, prion sorption to soil particles clearly has the potential to increase disease transmission via the oral route and contribute to the maintenance of TSE epizootics.

Two of three tested soils potentiated oral prion disease transmission. The reason for increased oral transmissibility associated with some, but not all, of the soils remains to be elucidated. One possibility is that components responsible for enhancing oral transmissibility were present at higher levels in the Elliot and Bluestem soils than in the Dodge soil. The major difference between the Dodge soil and the other two soils was the extremely high natural organic matter content of the former (34%, [22]). The Dodge and Elliot soils contained similar levels of mixed-layer illite/smectite, although the contribution of smectite layers was higher in the Dodge soil (14%–16%, [22]). The organic matter present in the Dodge soil may have obstructed access of PrPTSE to sorption sites on smectite (or other mineral) surfaces.

The mechanism by which Mte or other soil components enhances the oral transmissibility of particle-bound prions remains to be clarified. Aluminosilicate minerals such as Mte do not provoke inflammation of the intestinal lining [39]. Although such an effect is conceivable for whole soils, soil ingestion is common in ruminants and other mammals [25]. Prion binding to Mte or other soil components may partially protect PrPTSE from denaturation or proteolysis in the digestive tract [22,40] allowing more disease agent to be taken up from the gut than would otherwise be the case. Adsorption of PrPTSE to soil or soil minerals may alter the aggregation state of the protein, shifting the size distribution toward more infectious prion protein particles, thereby increasing the specific titer (i.e., infectious units per mass of protein) [41]. In the intestine, PrPTSE complexed with soil particles may be more readily sampled, endocytosed (e.g., at Peyer’s patches), or persorbed than unbound prions. Aluminosilicate (as well as titanium dioxide, starch, and silica) microparticles, similar in size to the Mte used in our experiments, readily undergo endocytotic and persorptive uptake in the small intestine [4244]. Enhanced translocation of the infectious agent from the gut lumen into the body may be responsible for the observed increase in transmission efficiency.

Survival analysis indicated that when bound to Mte, prions from both BH and purified PrPTSE preparations were more orally infectious than unbound agent. Mte addition influenced the effective titer of infected BH to a lesser extent than purified PrPTSE. Several nonmutually exclusive factors may explain this result: (1) other macromolecules present in BH (e.g., lipids, nucleic acids, other proteins) compete with PrPTSE for Mte binding sites; (2) prion protein is more aggregated in the purified PrPTSE preparation than in BH [45], and sorption to Mte reduces PrPTSE aggregate size, increasing specific titer [41]; and (3) sorption of macromolecules present in BH to Mte influences mineral particle uptake in the gut by altering surface charge or size, whereas the approximately 1,000-fold lower total protein concentration in purified PrPTSE preparations did not produce this effect.

We previously showed that other inorganic microparticles (kaolinite and silicon dioxide) also bind PrPTSE [22]. All three types of microparticles are widely used food additives and are typically listed as bentonite (Mte), kaolin (kaolinite), and silica (silicon dioxide). Microparticles are increasingly included in Western diets. Dietary microparticles are typically inert and considered safe for consumption by themselves, do not cause inflammatory responses or other pathologies, even with chronic consumption, and are often sampled in the gut and transferred from the intestinal lumen to lymphoid tissue [39,46,47]. Our data suggest that the binding of PrPTSE to dietary microparticles has the potential to enhance oral prion disease transmission and warrants further investigation.

In conclusion, our results provide compelling support for the hypothesis that soil serves as a biologically relevant reservoir of TSE infectivity. Our data are intriguing in light of reports that naïve animals can contract TSEs following exposure to presumably low doses of agent in the environment [5,79]. We find that Mte enhances the likelihood of TSE manifestation in cases that would otherwise remain subclinical (Figure 3B and 3C), and that prions bound to soil are orally infectious (Figure 5). Our results demonstrate that adsorption of TSE agent to inorganic microparticles and certain soils alter transmission efficiency via the oral route of exposure.

TSE agent source.

Syrian hamsters (cared for according to all institutional protocols) were experimentally infected with the HY or DY strain of hamster-adapted TME agent [48]. Brain homogenate, 10% w/v, was prepared in 10 mM NaCl. PrPTSE was purified to a P4 pellet from brains of hamsters infected with the HY strain using a modification of the procedure described by Bolton et al. [49,50]. The P4 pellet prepared from four brains was resuspended in 1 mL of 10 mM Tris (pH 7.4) with 130 mM NaCl. In the subset of experiments using PrPTSE–Mte complexes, larger prion aggregates were removed from the preparation by collecting supernatants from two sequential 5-min centrifugations at 800 g (clarification). Protein concentrations were determined using the Bio-Rad (http://www.bio-rad.com) DC protein assay as directed by the manufacturer’s instructions.

Preparation of inocula and oral dosing.Four types of Mte- or soil-containing inocula were prepared: BH–Mte mixtures, PrPTSE–Mte mixtures, PrPTSE–soil mixtures, and PrPTSE–Mte complexes (see below). To prepare mixtures of BH or PrPTSE with Mte, the indicated amount of 10% brain homogenate (Figures 1 and 2) or PrPTSE (Figure 3) was added to 500 μL of 10 mM NaCl in the presence or absence of 500 μg of Na+-saturated Mte (particle hydrodynamic diameter = 0.5–2 μm) (prepared per [51]). Mixtures of PrPTSE and whole soils (Figure 5) were prepared by adding 1 μg of PrPTSE to 500 μL of 5 mM CaCl2 in the presence or absence of 1 mg of each soil type. Samples were rotated at ambient temperature for 2 h, like samples were pooled, and the equivalent of 500 μg of Mte or 1 mg of whole soil was orally inoculated into each hamster. We previously showed that absorption of purified PrPTSE to Mte was complete within 2 h [22].

Isolated PrPTSE–Mte complexes were prepared as previously described [22]. Briefly, the indicated amount of clarified PrPTSE (200 or 20 ng, Table 1) was added to 500 μg of Mte in 10 mM NaCl (500 μL final volume) per sample. Mixtures were rotated at ambient temperature for 2 h. Each PrPTSE–Mte suspension was placed over a 750-mM sucrose cushion prepared in 10 mM NaCl and centrifuged at 800 g for 7 min to sediment mineral particles and adsorbed PrPTSE. PrPTSE–Mte complexes were resuspended in 500 μL of 10 mM NaCl and pooled. The equivalent of 500 μg of Mte was orally inoculated into each hamster. To control for potential sedimentation of unbound PrPTSE, “mock” samples lacking Mte were processed identically, and any sedimented material was inoculated into hamsters. As a positive control, unbound PrPTSE (200 or 20 ng) was orally administered to hamsters. All oral inoculations were via pipette and voluntary consumption. Following oral dosing, hamsters were observed twice weekly for the onset of clinical symptoms [48] for at least 300 d, a period of time found sufficient to observe most or all clinical cases.

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Crossbow Communications specializes in issue management and public affairs. Alzheimer’s disease, Creutzfeldt-Jakob disease, chronic wasting disease and the prion disease epidemic is an area of special expertise. Please contact Gary Chandler to join our coalition for reform gary@crossbow1.com.

Mad Cow, Creutzfeldt-Jakob, Alzheimer’s Disease Spreading With Sewage

Prions Connect Transmissible Spongiform Encephalopathies

The U.S. government’s monitoring system for cases of Creutzfeldt-Jakob disease, a fatal human brain illness, could be missing tens of thousands of victims, scientists and consumer advocates said.

Creutzfeldt-Jakob disease or CJD can be caused by prion exposure, including eating beef contaminated with mad cow disease, but the critics assert without a better tracking system it might be impossible to determine whether any CJD cases are due to mad cow disease or obtain an accurate picture of the prevalence of the disorder in the United States.

Alzheimer's disease epidemic

In order to understand the threat, one must understand the dynamics of this neurological disease. Alzheimer’s disease, for example, is a member of an aggressive family of neurodegenerative diseases known as Transmissible Spongiform Encephalopathy (TSE). The operative word is “transmissible.”

TSEs are caused by a deadly protein called a prion (PREE-on). As such, TSEs also are referred to as prion disease. The critical factor is that prions are unstoppable. The pathogen spreads through the bodily fluids and cell tissue of its victims. Blood, saliva, mucus, milk, urine and feces carry deadly prions from victims. All tissue is infectious just because of the contact with the contaminated blood.

TSEs also include Creutzfeldt-Jakob disease, Parkinson’s, Huntington’s, mad cow disease and chronic wasting disease in the deer family. Few, if any, mammals are immune. There is no cure.

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing deadly prions and prion disease. President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. According to Prusiner, TSEs all are on the same disease spectrum, which is more accurately described as prion disease. He claims that all TSEs are caused by prions.

prion disease epidemic

Prions are unstoppable and the pathogen spreads through the bodily fluids and cell tissue of its victims. Prions shed from humans are the most deadly mutation. They demand more respect than radiation. Infected surgical instruments, for example, are impossible to sterilize and hospitals throw them away. Prions are in the blood, saliva, urine, feces, mucus, and bodily tissue of its victims. Many factors are contributing to the epidemic. Prions are now the X factor. Industry and government are not accounting for them or regulating them. They are ignoring the threat completely, which violates the Bioterrorism Preparedness and Response Act of 2002 in the United States. Other nations also are ignoring laws developed to protect food, air and water.

“There is now real evidence of the potential transmissibility of Alzheimer’s disease,” says Thomas Wiesniewski M.D. a prion and Alzheimer’s researcher at New York University School of Medicine. “In fact, this ability to transmit an abnormal conformation is probably a universal property of amyloid-forming proteins (prions).”

A new study published in the journal Nature renews concern about the transmissibility of Alzheimer’s disease between people. A second study by the same scientist in early 2016 adds to the stack of evidence.

The first symptoms of CJD typically include memory loss and difficulty keeping balance and walking. As the disease destroys the brain, patients rapidly progress in a matter of months to difficulty with movement, an inability to talk and swallow and, finally, death.

Clusters of CJD have been reported in various areas of the United States — Pennsylvania in 1993, Florida in 1994, Oregon in 1996, New York in 1999-2000 and Texas in 1996. In addition, several people in New Jersey developed CJD in recent years, including a 56-year-old woman who died on May 31, 2003. Although in some instances, a mad cow link was suspected, all of the cases ultimately were classified as sporadic. The common thread is more likely sewage sludge, also known as biosolids, dumped on land.

land application sewage sludge

People who develop CJD from eating prion-contaminated beef have been thought to develop a specific form of the disorder called variant CJD. But new research, released last December, indicates the mad cow pathogen can cause both sporadic CJD and the variant form. A deadly prion is a deadly prion and there are now hundreds, if not thousands, of mutations.

“Now people are beginning to realize that because something looks like sporadic CJD they can’t necessarily conclude that it’s not linked to mad cow disease,” said Laura Manuelidis, section chief of surgery in the neuropathology department at Yale University, who conducted a 1989 study that found 13 percent of Alzheimer’s patients actually had CJD.

Several studies, including the one by Manuelidis, have found autopsies reveal 3-percent-to-13-percent of patients diagnosed with Alzheimer’s or dementia actually suffered from CJD. Those numbers might sound low, but there are 4-million Alzheimer’s cases and hundreds of thousands of dementia cases in the United States. A small percentage of those cases could add up to 120,000 or more CJD victims going undetected and not included in official statistics.

biosolids land application

Experiences in England and Switzerland — two countries that discovered mad cow disease in their cattle — have heightened concerns about the possibility some cases of sporadic CJD are due to consuming mad-cow-tainted beef. Both countries have reported increases in sporadic CJD since mad cow was first detected in British herds in 1986.

Switzerland discovered last year its CJD rate was twice that of any other country in the world. Switzerland had been seeing about eight to 11 cases per year from 1997 to 2000. Then the incidence more than doubled, to 19 cases in 2001 and 18 cases in 2002.

The CDC says the annual rate of CJD in the United States is one case per million people, but the above studies suggest the true prevalence of CJD is not known, Manuelidis told UPI.

Diagnosing CJD or Alzheimer’s disease is difficult because no test exists that can identify either disease in a living patient with certainty. So physicians must rely on the patient’s symptoms to determine which illness might be present. Sometimes, however, the symptoms of one disease can appear similar to the other disorder. The only way to determine the disease conclusively is to perform an autopsy on the brain after death.

Unfortunately, although autopsies once were performed on approximately half of all corpses, the frequency has dropped to 15 percent or less in the United States. The National Center for Health Statistics — a branch of the CDC — stopped collecting autopsy data in 1995.

“If we don’t do autopsies and we don’t look at people’s brains, we have no idea about what is the general prevalence of these kinds of infections and (whether) it is changing,” Manuelidis said.

At the same time autopsies have been declining, the number of deaths attributed to Alzheimer’s disease has increased more than 50-fold since 1979, going from 857 deaths then to nearly 50,000 in 2000. Though it is unlikely the dramatic increase in Alzheimer’s is due entirely to misdiagnosed CJD cases, it “could explain some of the increase we’ve seen,” Manuelidis said.

“Neurodegenerative disease and Alzheimer’s disease have become a wastebasket” for mental illness in the elderly that is difficult to diagnose conclusively, she said. “In other words, what people call Alzheimer’s now is more broad than what people used to call it, and that has the possibility of encompassing more diseases — including CJD.”

The autopsy studies that found undiagnosed CJD cases raise the question of whether the United States “already has an undetected epidemic here,” Jeff Nelson, director of vegsource.com, a vegetarian advocacy Web site, told UPI.

“What’s the source of that?” Nelson asked. “Could it be the same source of encephalopathy we saw in mink?”

Nelson referred to an outbreak of a mad-cow-type disorder in mink in Wisconsin in the 1980s. The origin was traced back to the animals’ diet, which included parts of so-called downer cattle — sick cows that are unable to stand, which often indicates a neurological disease, including mad cow. The mink disease raised concerns about whether U.S. cattle were carrying a mad-cow-like pathogen even prior to the U.K. epidemic that began in 1986.

Andrew Monjan, chief of the neuropsychology of aging program at the National Institute of Aging — part of the National Institutes of Health in Bethesda, Md. — acknowledged there has been an increase in U.S. Alzheimer’s cases. However, he told UPI, this probably is due to the aging of the population — as people grow older, they develop a higher risk of developing Alzheimer’s (bullshit).

“There’s been no change in the number of CJD cases in the country and there has been clearly a tracking of the unusual cases of CJD” that could be due to mad cow disease, Monjan said. However, Terry Singletary, coordinator of CJD Watch — an organization founded to track CJD cases — says efforts to track the disease have been close to nonexistent. For example, only 12 states require such reports. Therefore, many cases might be going undetected, unreported or misdiagnosed.

mad cow disease

If more states made CJD a reportable illness, there would be more clusters detected across the United States, said Singletary, who became involved with CJD advocacy after his mother died from a form of CJD known as Heidenhain variant. In the 18-year period between 1979 and 1996, he noted, the country saw a jump from one case of sporadic CJD in people under the age of 30 — a warning sign for a link to mad cow because nearly all of the U.K. victims were 30 years of age or younger — to five cases in five years between 1997 and 2001. “That represents a substantial blip,” he told UPI.

Singletary also said there have been increases in sporadic CJD in France, Germany and Italy, all of which have detected mad cow disease in their cattle.

So far, the CDC has refused to impose a national requirement that physicians and hospitals report cases of the disease. The agency has not chosen to make CJD a reportable disease because “making it reportable is not necessarily directly helpful in surveillance because in some states where it’s reportable you may not get the physician to report it,” said Dr. Ermias Belay, CDC’s medical epidemiologist working on CJD.

Instead, the agency relies on other methods, including death certificates and urging physicians to send suspicious cases to the National Prion Disease Pathology Surveillance Center at Case Western Reserve University in Cleveland, which is funded by the CDC. However, because autopsies generally are not done, if a CJD case is misdiagnosed as Alzheimer’s or dementia, a correct diagnosis might never be determined and therefore the cause of death listed on a death certificate might be inaccurate.

Belay told UPI he discounted this possibility. It is unlikely to happen, he said, because it is easy to distinguish CJD from Alzheimer’s — the two conditions display different symptoms.

Manuelidis disagreed. It can be quite difficult to determine accurately if a patient has CJD, as evidenced by her study, in which respected and competent neurologists and psychiatrists at Yale originally diagnosed patients with Alzheimer’s, yet were wrong at least 13 percent of the time. Another study conducted at the University of Pennsylvania, which found 6 percent of dementia patients actually were suffering from CJD, supports the difficulty in distinguishing the illnesses correctly.

The U. Penn. researchers concluded: “These results show that in patients with a clinical diagnosis of dementia, the etiology (cause) cannot be accurately predicted during life.”

In addition, the NPDPSC sees less than half of all the CJD cases each year, so the CDC’s investigational system not only is missing many of the misdiagnosed CJD cases, it also is not conducting autopsies on most of the detected cases.

Belay said the CDC follows up on all cases of CJD that occur in people under age 55, as these could be linked to variant — mad-cow-related — CJD. But so far, all have turned out to be sporadic forms of the disease. About 30 cases of the disorder occur each year in the United States in this age group, while the remaining 270 or so are older.

The case of Carrie Mahan — a Philadelphia woman who developed a brain disorder that appeared to be CJD and died from it in 2000 at the age of 29 — illustrates just how difficult it can be to diagnose the disease.

Mahan’s physician, Dr. Peter Crinos of the University of Pennsylvania Medical Center, ruled out other disorders and felt certain the young woman had died of CJD, a concern that raised the possibility of a link to mad cow disease because of her young age. When neuropathologist Nicholas Gonatas, who had seen CJD before, examined Mahan’s brain after her death, he, likewise, was confident he detected the microscopic, sponge-like holes caused by the disease. But when he sent brain samples to the NPDPSC, the results came back negative. Gonatas, convinced the surveillance center’s finding was erroneous, sent off two more samples, only to have them both come back negative.

Subsequent research, however, has shown the test used by the surveillance center cannot rule out CJD, said Crinos, an assistant professor of neurology.

“There’s no question that Carrie had a spongiform encephalopathy,” Crinos said, but added although it appeared to be CJD, it is difficult if not impossible to say if it was due to mad cow disease.

Crinos told UPI until the CDC implements a better tracking system, a lot of questions will remain about CJD and cases like Carrie Mahan’s. One central question: Why are cases of what is presumed to be a rare disease popping up in clusters in certain areas of the country? Crinos said the clustering suggests an environmental or food-borne cause, but so far, “No one knows the answer to that.”

The Second Part Of The Prion Equation

We can split hairs about the diagnoses, misdiagnoses and causes of the prion disease forever, but the problem with prions is that the victims are infectious themselves and serve as prion incubators and distributors. The bodily fluids of victims are loaded with infectious prions. Blood, urine, feces, saliva and mucus transport the disease throughout the victims’ environments. Downstream, wastewater treatment plants, for example, are spreading this infectious waste far and wide because they are incapable of stopping prions. All by-products and discharges from wastewater treatment plants are infectious waste, which are contributing to the global epidemic of neurodegenerative disease among humans, wildlife and livestock. Sewage treatment plants can’t detect or stop prions. Just ask the U.S. EPA and the industry trade organization—the Wastewater Effluent Federation. Sewage sludge (biosolids) and wastewater reclamation are causing widespread contamination.

biosolids land application and disease

Once unleashed on the environment, prions remain infectious. They migrate, mutate and multiply as they infect crops, water supplies and more.

Deer, elk, moose and reindeer are now contracting prion disease from humans. To help cloak the epidemic, it’s called chronic wasting disease (CWD). Deer with CWD are proverbial canaries in a coal mine. They are being killed by government sharpshooters to help cover up the problem. It’s insane.

Alzheimer’s Disease News via http://www.organicconsumers.org/madcow/CJD122903.cfm

public relations firm and public affairs firm Denver and Phoenix

Crossbow Communications specializes in issue management and public affairs. Alzheimer’s disease, Creutzfeldt-Jakob disease, chronic wasting disease and the prion disease epidemic is an area of special expertise. Please contact Gary Chandler to join our coalition for reform gary@crossbow1.com.