Alzheimer’s An Infectious Disease

Alzheimer’s A Transmissible Disease

If you think that you and your family are immune to the surging epidemic of neurodegenerative disease, think again. Neurodegenerative disease, including Alzheimer’s disease, is the fastest-growing cause of death in the world. It’s getting worse every day thanks to mismanagement and misinformation.

Infectious proteins known as prions are involved with most forms of neurodegenerative disease. Prion disease is known in neurology as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” The global epidemic has more to do with the prion contagion than age. In fact, it appears that the autism epidemic has more in common with Alzheimer’s disease than previously thought.

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. Prusiner claims that all TSEs, including Alzheimer’s disease, are caused by prions.

Alzheimer's disease 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 are a spectrum disease. Creutzfeldt-Jakob disease, which is extremely aggressive and extremely transmissible, is at the extreme end of the spectrum. Unfortunately, Prusiner’s science is being ignored and we are facing a public health disaster because of the negligence.

Neurologists are just guessing when they make a diagnosis on the prion spectrum. If the patient exhibits memory problems, they are labeled with Alzheimer’s disease. If they have a movement disorder, they are diagnosed with Parkinson’s disease. If the person exhibits extreme symptoms of both, they are diagnosed with Creutzfeldt-Jakob disease (CJD). It’s far from a science.

prion disease spectrum

According to neuroscientist Laura Manuelidis, at least 25 percent of Alzheimer’s diagnoses are wrong. These misdiagnoses are actually CJD, which is further up the prion spectrum. CJD, without dispute, is extremely infectious to caregivers and loved ones.

Neurologists don’t know where along the spectrum the disease becomes transmissible. The entire spectrum could represent a transmissible disease. Unfortunately, neurologists are not warning these patients and their caregivers about the risks of exposure. Even those with Creutzfeldt-Jakob disease are not quarantined. They are sent home, where they can infect friends, family, caregivers, clinics, dental offices, restaurants and entire communities.

“There has been a resurgence of this sort of thinking, because there is now real evidence of the potential transmissibility of Alzheimer’s,” 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 study published in the journal Nature renews concern about the transmissibility of Alzheimer’s disease between people. A second study released in early 2016 by the same scientist adds to the stack of evidence.

Studies confirm that people and animals dying of prion disease contaminate the environment around them with prions because prions are in the urine, feces, blood, mucus and saliva of each victim. Each victim becomes an incubator and a distributor of the Pandora-like pathogen. Victims are contagious long before they exhibit clinical symptoms.

Alzheimer's disease epidemic

At the personal level, this is very bad news for caregivers, especially spouses, who are 600 percent more likely to contract neurodegenerative disease from patients (Duke University and Utah State University). A cough, sneeze, utensils and drinking glasses all become lethal pathways. Once an item is contaminated, it’s impossible to sterilize. The human prion is resistant to both heat and chemicals. It’s reported that prions released from people are up to a hundred thousand times more difficult to deactivate than prions from most animals. Prions are not alive, so they can’t be killed.

Wastewater treatment plants are collecting points for prions from infected humans. The sewage treatment process can’t stop prions from migrating, mutating and multiplying before being discharged into the environment where they can kill again. The bad news is that the prions are being released back into the environment and dumped openly on land. The wastewater is being reclaimed and used for irrigating crops, parks, golf courses. It’s even being recycled as drinking water.

Claudio Soto, PhD, professor of neurology at the University of Texas Medical School in Houston, and his colleagues confirmed the presence of prions in urine. Soto also confirmed that plants uptake prions and are infectious and deadly to those who consume the infected plants. Therefore, humans, wildlife and livestock are vulnerable to prion disease via plants grown on land treated with sewage sludge and reclaimed sewage water.

Prion researcher Dr. Joel Pedersen, from the University of Wisconsin, found that prions become 680 times more infectious in certain soils. Pedersen also found that sewage treatment does not inactivate prions. Therefore, prions are lethal, mutating, migrating and multiplying everywhere sewage is dumped.

“Our results suggest that if prions enter municipal wastewater treatment systems, most of the agent would bond to sewage sludge, survive anaerobic digestion, and be present in treated biosolids,” Pedersen said.

prion research Joel Pedersen

“Land application of biosolids containing prions represents a route for their unintentional introduction into the environment. Our results emphasize the importance of keeping prions out of municipal wastewater treatment systems. Prions could end up in sewage treatment plants via slaughterhouses, hospitals, dental offices and mortuaries just to name a few of the pathways. The disposal of sludge represents the greatest risk of spreading prion contamination in the environment. Plus, we know that sewage sludge pathogens, pharmaceutical residue and chemical pollutants are taken up by plants and vegetables.”

Thanks to more and more people dying from TSEs, wastewater treatment systems are more contaminated with prions than ever. Wastewater treatment plants are now prion incubators and distributors. The prion problem is getting worse every day.

land application sewage sludge

The U.S. Environmental Protection Agency (EPA) has confirmed that prions are in sewage and that there has been no way to detect them or stop them. As such, the EPA has never issued guidance on prion management within wastewater treatment plants. Unfortunately, the EPA’s risk assessment on sewage sludge and biosolids were prepared before the world of science knew about prions. The agency continues to cling to its antiquated sludge rule crafted back in the dark ages. It does, however, consider prions a “contaminant of emerging concern.” Meanwhile, its outdated risk assessments are promoting a public health disaster.

“Since it’s unlikely that the sewage treatment process can effectively deactivate prions, adopting measures to prevent the entry of prions into the sewer system is advisable,” — Toronto Department of Health, November 2004.

Exposing crops and livestock to prions is a very bad idea. Plants absorb prions from the soil along with water and nutrient uptake, which makes the prions even more bioavailable and infectious to humans, wildlife and livestock.

chronic wasting disease caused by prions

Unfortunately, the damage is real. Deer, elk, moose and reindeer are contracting an unstoppable prion disease now. In deer, the government calls prion disease chronic wasting disease. In cattle, prion disease is called bovine spongiform encephalopathy (they might as well call it what it is—transmissible spongiform encephalopathy). Mad cow disease is the term that most of us know. The government pretends that there is a specific prion responsible for each of these diseases. The fact is that there are thousands of mutations of prions spreading in the environment and food chain now. Some kill quickly, while some are less lethal. The only thing that we need to know is that a deadly prion is a deadly prion. Prions shed from humans are the most aggressive and the most deadly. There is no species barrier.

If prion disease is killing these animals, livestock are not immune. Beef and dairy cattle are consuming these infected crops and the infected water supplies, too. Since humans are at the top of the food chain, and since we are often downstream from these infected farms, ranches and forests, our food and water supplies are being compromised. Wind and tornadoes transport the infectious waste even further.

So, is Alzheimer’s disease transmissible? There is absolutely no evidence to the contrary. The truth is your best defense against neurodegenerative disease.

Alzheimer's disease treatment

Preview and order the eBook now. Learn how to avert exposure to the Alzheimer’s disease contagion. Answers begin with the truth.

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Infectious Waste Spreading Brain Disease To Wildlife

Chronic Wasting Disease Caused By Dumping Of Infectious Waste

Alzheimer’s disease, Parkinson’s disease and other forms of neurodegenerative disease are collectively becoming the leading cause of death around the world. Brain disease also continues to expand in wildlife. Is there a connection?

Prions and Prusiner win Nobel Prize

Keep reading to find out why:

  • Alzheimer’s disease is an infectious prion disease;
  • Prion infectivity is in the bodily fluids of those with prion disease;
  • Wastewater treatment plants are spreading deadly prions via sewage sludge, biosolids and reclaimed wastewater.They also spread nuclear waste and toxic waste;
  • Wildlife are contracting prion disease from people because of this contamination. So are people. So are sea mammals.
  • Caregivers are in harm’s way because of widespread denial and mismanagement.
  • It’s time for several reforms. It’s time to reclassify biosolids and reclaimed wastewater as infectious waste. Prions are unstoppable. It’s time to enforce the Bioterrorism Preparedness and Response Act of 2002.

The Brain Disease Epidemic

Alzheimer’s disease alone is killing 50-100 million people now. Millions more will contract the disease this year, while just as many will go undiagnosed and misdiagnosed.

transmissible spongiform encephalopathy

Thanks to misinformation and the mismanagement of infectious waste and bodily fluids, people of all ages are now exposed to an expanding spectrum of brain disease. So are other mammals.

The most common forms of neurodegenerative disease include Alzheimer’s disease, Parkinson’s disease, ALS and Creutzfeldt-Jakob disease–the most aggressive and infectious of them all. According to Nobel Prize Laureate Stanley Prusiner, these brain diseases are part of the same disease spectrum—prion disease. It’s also known as transmissible spongiform encephalopathy (TSE). The operative word is transmissible.

prion disease epidemic

Prion disease also includes chronic wasting disease among cervids (deer) and mad cow disease among cattle. It’s been found in dozens of mammals.

Pandora’s Lunchbox

Many factors are contributing to the epidemic. Unfortunately, it appears that Alzheimer’s disease and Parkinson’s are just as infectious as Creutzfeldt-Jakob disease (CJD). The bodily fluids of people with prion disease are infectious. Prions are the X factor in the global epidemic.

biosolids land application disease

Prion disease is a spectrum disease that varies in severity. It also varies depending on which region of the brain is impacted first. It affects most, if not all, mammals. Prion disease causes memory loss, impaired coordination, and abnormal movements. Prions are an infectious form of glycoprotein that can propagate throughout the body. TSE surveillance is important for public health and food safety because TSEs have the potential of crossing from animals to humans, as seen with the spread of mad cow disease. TSEs also have the potential of being transmitted from humans to animals. The most common example is chronic wasting disease (CWD) among deer species.

CWD was first detected in deer in North America. Then it was detected in a variety of other animals, including an elephant at the Oakland zoo. It’s been found in a variety of animals across the United States and Canada. All hypotheses seem to center around contaminated feed and deer farmers. Then the deer spread the disease via nose-to-nose contact. Those theories were just rocked by the discovery of CWD in Norway in moose and reindeer. The disease didn’t jump the Atlantic from the Americas. However, Norway dumps tons of infectious waste on land every year–infectious waste from people with prion disease.

chronic wasting disease caused by prions

It’s not known which patients with brain disease become infectious or when. The medical community prefers to ignore the topic. The legal industry is about to have a bonanza because negligence is the rule and not the exception regarding Alzheimer’s disease and the mismanagement of infectious waste. Savvy neurologists won’t touch patients with these symptoms because of the risks. Unfortunately, caregivers aren’t warned accordingly.

“There is now real evidence of the potential transmissibility of Alzheimer’s,” 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).”

Prions are unstoppable. The pathogen spreads through the bodily fluids and cell tissue of its victims. The blood, saliva, mucus, milk, urine and feces of victims are infectious. Wastewater treatment doesn’t touch prions. In fact, these facilities are now helping incubate and distribute prions via solids and wastewater released. Once unleashed on the environment, prions remain infectious. They migrate, mutate and multiply as they infect crops, water supplies and more.

biosolids land application and disease

When the U.S. government enacted the Bioterrorism Preparedness and Response Act of 2002, it classified prions as select agents that pose an extreme risk to food, water and much more. Unfortunately, the CDC quietly took prions off the list because the regulation criminalized entire industries and several reckless practices.

Unfortunately, prions linger in the environment, homes, hospitals, nursing homes, dental offices and beyond infinitely. Prions defy all attempts at sterilization and inactivation.

Prions shed from humans are the most deadly. They demand more respect than radiation. They’re being ignored by regulators and industry alike. As such, food and water sources are being contaminated with the deadliest forms of prions. Municipal water systems can’t stop them from reaching water taps in millions of homes. Filtration doesn’t phase them.

Alzheimer's disease prevention

Scientists have shown that infected tissues can transmit prion disease between animals. There is no species barrier. 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. There is no evidence that Alzheimer’s disease is not infectious.

Although there are many causes and pathways contributing to prion disease, many pathways are being mismanaged around the globe. Not only are homes and hospitals exposed to the prion pathogen, so are entire sewage treatment systems. Wastewater treatment plants are prion incubators. Sewage sludge and wastewater pumped out spread the disease.

The risk assessments prepared by the U.S. EPA for wastewater treatment and sewage sludge are flawed. Many risks are not addressed, including prions and radioactive waste. They don’t mention prions or radiation because there is no answer. Most nations are making the same mistake. Failure to account for known risks is negligent. Crops for humans and livestock grown grown in sewage sludge absorb prions and become infectious. We’re all vulnerable to Alzheimer’s and other forms of prion disease right now due to widespread denial and mismanagement.

land application sewage sludge

Sewage treatment plants can’t detect or stop prions. Just ask the U.S. EPA. If sick deer are serving as a canary in a coal mine, what is this infectious sewage sludge doing to livestock and humans?

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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 Stop prion disease.

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Sewage Sludge Spreading Brain Disease

Biosolids Spreading Brain Disease Among Mammals

In 1972, world leaders realized that dumping millions of tons of sewage sludge into the oceans killed entire underwater ecosystems. Some nations stopped the dumping immediately, while others did not.

The U.S., for example, finally passed the Ocean Dumping Ban Act of 1988. It required dumping all municipal sewage sludge and industrial waste on land. That meant dumping it into landfills or dumping it openly on land, including farms, ranches, national forests, city parks, golf courses, playgrounds, sport fields and beyond. The Act went into effect in 1992 and it sparked a public health disaster. The practice is spreading pathogens to people, livestock, wildlife and beyond every day.

Landfills designed to handle this toxic soup are extremely expensive. So, the dumpers hired a public relations firm to convince unsuspecting citizens that neurotoxins are fertilizer. The PR firm called this toxic waste biosolids. It’s even sold in bags at your local home and garden store as soil for your garden and potting plants. It should be called death dirt.

biosolids management land application

Since then, millions of tons of sewage sludge have been given to farmers as fertilizer every year. Those farmers and ranchers who don’t believe that “fertilizer” bullshit are being paid to dump it on their land and shut up. The farmers are held harmless if the infectious waste causes damage to people or property.

“There is now real evidence of the potential transmissibility of Alzheimer’s,” 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).”

Unfortunately, the practice of dumping extreme quantities of sewage sludge on land has created an even bigger public health problem. It’s now killing wildlife and it still kills sea mammals. Livestock are not immune to the threat.

chronic wasting disease caused by prions

Prions are the protein-based infectious agents responsible for a group of diseases called transmissible spongiform encephalopathy (TSE). The operative word is transmissible. TSEs are more commonly known as:

  • bovine spongiform encephalopathy (mad cow disease) in cattle;
  • scrapie in sheep;
  • Creutzfeldt-Jakob disease (CJD) and Alzheimer’s disease in humans; and
  • chronic wasting disease (CWD) in deer, elk, moose and reindeer.

According to Nobel Laureate Stanley Prusiner, Alzheimer’s disease, ALS and Huntington’s disease also are on the TSE spectrum. All are fatal, neurodegenerative brain diseases.

Prions and Prusiner win Nobel Prize

Infectious prions are in the bodily fluids of its victims, including blood, urine, mucus, saliva and feces. These victims send prions to the municipal sewage treatment plant where they remain untouched. Wastewater effluent and sewage sludge recycles prions into the environment. Once dumped on open land, they remain infectious. Irrigation, precipitation and wind carry the prions into groundwater, streams, lakes, oceans and airways, including homes, offices and beyond.

Alzheimer's disease epidemic

Reckless wastewater treatment policies and practices are now fueling a global epidemic of neurodegenerative disease among people, wildlife and livestock. The risk assessments are based on fraud and outdated information. The risk assessments for the land application of sewage sludge (LASS) were developed back in the 1970s and 1980s–before we knew about prions and other killers in modern sewage streams, including many forms of infectious medical waste.

The risk assessments were questionable then and they are total failures now. Plus, these risk assessments do not account for the possibility of sewage sludge dumped on land going airborne. It’s much more than a possibility–airborne sewage sludge is killing people and animals. It’s dumping the toxins and infectious waste everywhere.

land application sewage sludge

Unfortunately, the U.S. exported these ridiculous ideas to other nations who proceeded to contaminate their food and water supplies with sewage. If hospitals can’t stop prions, neither can the brain surgeons at wastewater treatment plants.

The legislation banning ocean dumping was very explicit about the need to stop dumping potentially infectious medical waste into the oceans. Ironically, the current policy that promotes LASS ignores the risk of infectious medical waste and many other threats. It also ignores radionuclides, endocrine disruptors, birth control pills, antibiotics, flame-retardants and other toxins and superbugs. This toxic waste belongs in a lined landfill not our watersheds and food supplies. It’s time for immediate reforms.

The same sewage-borne toxins and pathogens are still contaminating our oceans. Now, they’re dumped in further upstream. Entire watersheds are now being infected—including the oceans. The body count among people, livestock and wildlife has been stacking up ever since ocean dumping began phasing out. Biosolids and other forms of sewage mismanagement are now fueling a global epidemic of neurological disease, including Alzheimer’s disease, Parkinson’s disease, autism, mad cow disease, chronic wasting disease, microcephaly and more. Industry and governments are scrambling to blame the global epidemic on anything but contaminated soil, water, food and air. They are playing dumb in the face of fraud and scientific suppression. Negligence is too kind of a word for these public servants.

biosolids land application and disease

Sewage also contaminates our food with listeria, e-coli, salmonella and other killers. In fact, scientists are scrambling to come up with new names for the growing list of sewage-related ailments, including Zika virus, West Nile virus, epizoic hemorrhagic fever, equine herpes, valley fever and others. Industrial disease is a more accurate label.

Crops contaminated by sewage sludge can uptake prions and deliver them throughout the plant. Plants then deliver the deadly prions to mammals that consume the plant. In fact, infected plants are spreading prion diseases to several species. When hamsters consumed infected wheat grass, the animals were infected with prion disease. Researchers also found deadly prions in plants exposed to infected urine and feces. The concept of a species barrier is a myth. A deadly prion is a deadly prion. They don’t discriminate among victims.

“These findings demonstrate that plants can efficiently bind infectious prions and act as carriers of infectivity, suggesting a possible role of environmental prion contamination in the horizontal transmission of the disease,” said Claudio Soto, the lead investigator from the University of Texas at Houston.

Killer prions are impossible to stop. Prions are contributing to the death of millions of people now. Victims produce and spread prions daily because they’re in the bodily fluids of all victims. Millions of people with brain disease are contaminating their homes and communities, while exposing caregivers and family members to the contagion. The sewage from these victims is contaminating the local wastewater treatment plant and everything that enters or leaves these facilities, including reclaimed wastewater and sewage sludge. Once dumped on open land, these contagions remain infectious as they migrate, mutate and multiply forever.

biosolids land application LASS

Prions demand more respect than radiation. They require containment and isolation, not distribution and consumption through air, food and water. These toxins demand lined landfills not reckless dumping on our dinner tables. Prions migrate, mutate and multiply, so dilution is not a solution. Prions are a nightmare.

The world has never done an effective job of managing its sewage. It’s an industry that drives by looking in the rear view mirror. It only swerves when the road is buried in body bags. After enough people get sick and die, new alternatives emerge. Today is no different. The bodies are stacking up. The prion contamination grows stronger and spreads further every day. It’s time to stop dumping sewage sludge on land because of the prion risk and many others that are not accounted for in the antiquated and fraudulent risk assessments. It’s time for citizens to defend our land, water and air–not just our guns.

chronic wasting disease caused by prions

Today, the land application of sewage sludge is killing mammals and more around the world. Pathogens in sludge are causing brain disease, cancer and death. Let’s take a meaningful stand for food safety. Just say no to biosolids in our watersheds and food supplies.

Take a free preview of our new eBook to learn everything that you need to know about the epidemic and the mismanagement. The rest of the book explains how to defend yourself with aversion and targeted nutrition. Please join our campaign for truth and reform.

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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 Stop prion disease.

Alzheimer’s Disease Caused By Food, Water Contamination

Sewage Sludge Spreading Infectious Waste

More than 50 million people around the world have Alzheimer’s disease and other forms of dementia. It’s the fastest-growing cause of death in the world.

Alzheimer’s disease is a member of an unstoppable family of neurodegenerative diseases known as Transmissible Spongiform Encephalopathy (TSE). The operative word is “transmissible.” Related diseases are killing wildlife and livestock around the world. The TSE epidemic represents an environmental nightmare that threatens every mammal on Earth.

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. All sewage is infectious.

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.

treat Alzheimer's disease

Although there are many causes and pathways contributing to the prion disease epidemic, many pathways are being mismanaged around the globe. As such, we are recycling the pathogen that causes Alzheimer’s right back into our food and water. We’re dumping these killer proteins on crops, parks, golf courses, ski areas and school grounds. Rain and irrigation spread them throughout our communities and watersheds. We’re dumping prions into our food and water supplies with foolish sewage management practices.

Prions Found In All Bodily Fluids

A new study confirms that people and animals dying of prion disease are contaminating the environment around them with a deadly and unstoppable protein found in their bodily fluids. Claudio Soto, PhD, professor of neurology and director of the George and Cynthia W. Mitchell Center for Alzheimer’s Disease and Other Brain Related Illnesses at the University of Texas Medical School in Houston, and his colleagues recently found prions in urine. The study was published in the August 7 issue of the New England Journal of Medicine.

The research offers hope for earlier diagnosis among the millions of people impacted around the world, which means earlier intervention and better disease management. It also can help develop screens to protect our blood supplies from donors with prion disease.

The bad news is that prions in urine, mucus, feces and blood underscores the environmental nightmare associated with Alzheimer’s, Creutzfeldt-Jakob (CJD), Parkinson’s, Huntington’s and prion diseases among livestock and wildlife. Although there are many causes for prion disease, many people and animals are contracting it from environmental exposure (food, water and soil) and then contaminating the environment even more with their own bodily fluids. Once victims die, carcasses also contaminate soil and water.

“This is the first time that prions have been detected in human urine,” Dr. Soto told Neurology Today.

prions in sewage and urine

Soto failed to reference urine and blood studies performed earlier by Ruth Gabizon in 2001 and Reichl in 2002. These studies also detected prions in bodily fluids. Despite that detail, Soto’s findings can help focus global attention on the exploding prion problem.

Additional research has determined that the prion pathogen spreads through feces, saliva, blood, milk, soil, water and the tissue of infected animals and humans. If a single person with prion disease discharges bodily fluids or feces into a public sewer system, that sewage system is permanently infected and the amount of contamination will multiply and intensify daily. Everything discharged from that sewage system—reclaimed water and biosolids—can spread the contamination even further.

land application sewage sludge

Once a prion reaches the soil, that soil is permanently contaminated and the entire watershed (water) below that point is at risk forever. If your food and water is generated in that watershed, you have a higher risk of contracting prion disease with every sip of water or every bite of food produced locally.

With the help of weather, prions can migrate through wind and water. Rain and snow can rinse them into surface water, groundwater, streams, ponds, lakes, and oceans. Wildlife, livestock and humans can ingest prions from soil, water and food. We can’t afford to take the risk of further contaminating entire watersheds – increasing the pathway to humans, livestock, and wildlife downstream.

chronic wasting disease caused by prions

Because of these factors and others, we have an epidemic of prion disease exploding around the world right now. The epidemic is worse in some regions of the world than others. For example, the death rate for Alzheimer’s disease is higher in Finland than any other country in the world. Iceland and the United States are runners up. In fact, the death rate for Alzheimer’s is higher in Washington state than any other known region in the world. These vast discrepancies can only be explained by environmental factors, including food, water and air pathways. Sewage disposal that contaminates local food and water supplies is likely part of the problem.

The urine and sewage connection helps explain why the global epidemic is exploding. More than 44 million people around the world are known to have these neurodegenerative diseases today. Millions more have the disease, but don’t know it, yet. In addition to these people, millions of infected people around the world have used our sewage systems over the past century. Millions more are using them today. It’s impossible to neutralize or stop prions in even the most sterile environments, including hospitals. It’s ludicrous to think that treated sewage water or biosolids are prion-free. Especially since prions from people are much more infectious than those found in other species (prions become more aggressive as they work their way up the food chain).

The U.S. Environmental Protection Agency (EPA) has confirmed that prions are in sewage and that there has been no way to detect them or stop them. As such, the EPA has never issued guidance on prion management within sewage processing plants. This lack of directive allows budget-strapped states and counties to regulate the practices in a variety of ways that best suit local municipalities and industries.

Dr. Soto’s test changes that equation. Now, the EPA can’t plead ignorance to the dangers of prions in biosolids and reclaimed sewage water. Sewage dumped at sea must be reconsidered. Prions should be classified as a select agent again by the U.S. Department of Homeland Security and the Center for Disease Control. Similar measures should be enacted around the world immediately. Failure to act responsibly is suicide.

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Prions Not Stopped By Species Barriers

Prion Disease Killing Many Mammals

Prions are known to migrate, mutate and multiply. They become more voracious as they move from one host to another. New research adds to the bank of evidence that a deadly prion is a deadly prion and they know no borders between species. For years, food safety experts and wildlife managers have put people at ease by hiding behind the myth of species barriers. Blind faith can kill you when it comes to prion dynamics.

Canadian researchers recently discovered a slight change in prions’ makeup appears to give mad cow disease the ability to adapt and spread to other animals. Mutation still is likely a more accurate term, but “adaptation” is close enough for government work. I think the “adaptation” is the equivalent of a chemical reaction that takes place when prions are exposed to a new bank of proteins in a new host (victim).

prion disease epidemic

Neurologist Valerie Sim and her research team at the University of Alberta said the findings might explain how prion diseases, such as chronic wasting disease and mad cow disease, adapt in order to spread between various types of animals.

The prions’ makeup appears to give the disease the ability to adapt by mimicking and recreating new strains with which it comes into contact.

“Prion diseases don’t always successfully go from one animal to another, but when they do, the process is called adaptation. And we want to figure out what triggers that process to happen, what changes happen within prions to allow the disease to spread,” Sim said in a statement.

land application sewage sludge

“One of the important things researchers in this field have realized is that if you pass certain strains of prion disease through a number of different hosts, the disease can adapt along the way and increase the number of susceptible hosts. That’s the big concern right now.”

The findings were published in the Journal of Biological Chemistry.

Prions are associated with an entire family of neurological disorders that are killing people, wildlife and livestock around the world. These diseases are known as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.” TSEs include Alzheimer’s disease, Creutzfeldt-Jakob disease, Parkinson’s disease, Huntington’s disease, scrapie, chronic wasting disease and mad cow disease. The disease has killed many species of mammals including dolphins and likely is killing whales.

chronic wasting disease caused by prions

Read more:

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More Mismanagement of Deadly Mad Cow Disease

Prion Pathogen Highly Contagious

After eight years, the U.S. Food and Drug Administration (FDA) reopened the comment period for its rule on what cow parts may be used in human products Monday because research completed since the interim rule was published has revealed traces of bovine spongiform encephalopathy (BSE) and deadly prions in parts of the intestine currently allowed in human food and drugs.

mad cow disease

Since there is no way to ever sterilize the production line once infected with prions, just one infected animal part will contaminate the production line forever. Food, cosmetics, gel caps, lotions and other products could kill you and your family. Even our water supplies have been compromised due to prion mismanagement, including sewage mismanagement.

The report is alarming. Again, it shows that regulators are protecting the public health with blind faith, ignorance and incompetence. We must demand that deadly prions be regulated based on proven safety as opposed to one of a proven risk (ie. dead people). It took them eight years of status quo to raise this flag and countless products have been contaminated in the interim. As a result, we can only guess how many families have been exposed to this deadly and incurable prion disease. This is reckless, negligent and unforgivable. It’s criminal. It’s bioterrorism.

In 2005, FDA issued its interim final rule, “Use of Materials Derived From Cattle in Human Food and Cosmetics,” which stated that a cow’s small intestine was safe for use in human products as long as the portion called the distal ileum had been removed. At the time, the distal ileum was known to be a potential reservoir for BSE, also known as mad cow disease, but other parts of the small intestine were considered safe.

mad cow disease and prions

Since that time, studies have found low levels of BSE in other parts of the cow’s intestine, including the proximal ileum, jejunum, ileocecal junction, and colon, prompting concerns that perhaps the U.S. Department of Agriculture (which regulates meat safety) and FDA should also prohibit these parts from use in human foods and cosmetics. Of course, they should be kept out of rendering facilities, where they can be recycled back into products and animal feed (including pet food). In fact, we should demand answers about where the risky parts, such as the distal ileum, spinal cords, eyes, tonsils, and other specified risk material (SRM) are going now.

“The infectivity levels reported in these studies were much lower than the infectivity levels that were previously demonstrated in the distal ileum,” notes FDA. (It only takes one prion to kill you, so, I’m not feeling any safer despite this disclaimer.)

In light of these findings, FDA has reopened the comment period on its 2005 interim final rule in order to hear from anyone who has information on the topic. These are questions that should have been asked long ago.

When the FDA announced the reopened comment period, it stated that it believes that the trace levels of infectivity found in these other parts of the intestine don’t pose a risk of human exposure to BSE in the United States. That’s nonsense. Prions migrate, mutate and multiply. They can’t be stopped. So to say that the levels of infectivity are low further demonstrates the FDA’s and USDA’s incompetence or willingness to tolerate and unleash risks to the public.

“We want to hear from other people,” says Sebastian Cianci, spokesperson for FDA. “From what we’re seeing, we’ve concluded that there wouldn’t be a measurable reduction of risk from removing other parts. However, we want other people to weigh in before a final determination is made.”

In reaching its conclusion, FDA says it also considered a recent opinion from the European Union Food Safety Authority on the risk of BSE from parts of the small intestine other than the distal ileum. Why aren’t they actively seeking and sharing this information on a global basis? The bad news is that other prion risks remain unchecked and or mismanaged. The pathways to prion contamination in food, water, products and our healthcare systems are numerous.

A look at the opinion handed down from EFSA’s Panel on Biological Hazards shows that the group was unable to draw a conclusion about the safety of other parts of a cow’s intestine. Bullshit. It’s time to put all of the facts on the table and keep all risks off of our dinner table and out of our homes and hands. prions have been classified as a “select agent” by the U.S. Department of Homeland Security. Research is tightly controlled and extremely limited. Why are the USDA and FDA conducting chemistry experiments with them in our food, water, cosmetics and other products? What gives them the right to turn every human on the planet into a guinea pig? Any person or agency that violates the Bioterrorism Preparedness and Prevention Act of 2002 is, by definition, a terrorist.

“Due to limitations in the data currently available, an accurate quantification of the amount of infectivity in the intestinal parts other than ileum of Classical BSE infected cattle at different stages of the incubation period cannot be provided,” says the panel in its conclusion. Unfortunately, given the dangers of prions, it only takes one to multiply into millions. It only takes one prion to kill you. Quantification of this dynamic is very simple math.

The reopened comment period has been posted in the Federal Register. You can access it  here. Comments can be submitted by clicking the “Submit a Formal Comment” button.

Thanks to Gretchen Goetz and Food Safety News for their contribution to this article.

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Japan Will Ease Mad Cow Disease Restrictions on U.S. Beef

Pathogen Behind Mad Cow Disease Unstoppable

For only the second time in ten years, Japan will further ease restrictions on U.S. beef imports starting to allow entry of beef and beef products from cattle less than 30 months of age. They will implement the new regulation on February 1, 2013.Previously, a 2006 restriction limited U.S. beef imports to products from cattle under 20 months of age. Japan set that restriction when it allowed limited U.S. beef imports to resume after a cow with bovine spongiform encephalopathy (BSE) was found in a U.S herd in 2003.Japan’s easing of restrictions on U.S. beef imports is a sign that there is more product demand than fear in the Asian nation about BSE, popularly known as Mad Cow Disease.

mad cow disease and Japan imports of U.S. beef

Opening Japan’s market to more U.S. beef will result in “hundreds of million of dollars in exports of U.S. beef to Japan in coming years,” according to a statement by U.S. Trade Representative Ron Kirk and Secretary of Agriculture Tom Vilsack.

Kirk and Vilsack depicted the trade agreement as a “near normalization” of beef trade between the two nations. “This is great news for American ranchers and beef companies, who can now—as a result of this agreement—increase their exports of U.S. beef to their largest market for beef in Asia,” Ambassador Kirk said.

Kirk called it a “significant and historic step” that will grow American exports and jobs.

Japan banned U.S. beef in 2003 after the first cow with BSE was discovered near Mabton, WA. It took three years before it allowed some imports from the younger animals.

Japan’s independent Food Safety Commission (FSC) conducted a risk assessment in 2011 that found raising the age limit in conjunction of U.S. controls on specific risk materials (SRM) could address safety concerns.

land application sewage sludge

The expanded U.S. beef exports to Japan could reach the country by mid February and will likely put upward pressure on prices as American cattle numbers are at the lowest levels in 60 years. The drought affecting much of the U.S. has caused farmers and ranches to reduce their herds because dry lands aren’t producing enough to support the cattle.

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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

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


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 ( 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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Creutzfeldt-Jakob Disease Takes Teenager

Girl Died Rapidly From Neurological Disorder

When 15-year-old Claire McVey appeared reluctant to eat in front of her family, her mother Annie assumed she was just having teen wobbles about her weight. But Claire was showing the first signs of variant Creutzfeldt-Jakob disease (prion disease) or vCJD – a condition that would leave the bubbly teenager dead within six months. It’s the human form of mad cow disease and an overall prion epidemic that is spreading exponentially.

annie and claire mcvey

It was in 1996 that Annie, like all mothers, was horrified to learn that dozens of people had been infected with an incurable degenerative brain condition caught by eating beef from cattle infected with bovine spongiform encephalopathy or BSE (there are other vectors of concern).

“Being vegetarian, I always cooked meat-free dishes at home but my two children would occasionally eat meat elsewhere,” says Annie who lives in Kentisbury Ford in Devon. “When I heard about BSE being passed on to humans I was horrified. I wasn’t going to risk my children’s health so I immediately stopped Claire and her brother from eating all meat. What I didn’t know was that it was already too late.”

It was four years later, in July 1999, that Annie, who worked as a risk manager at their local district hospital, first noticed her daughter had become withdrawn and was behaving oddly.

“She stopped eating in front of us,” she recalls. “At first I thought she might be developing an eating disorder but it was more an anxiety about people seeing her eat. Then she started to have an issue about going to school and she didn’t want to wear her shoes. I couldn’t understand what had got into her.”

Worried, Annie took Claire to see their GP, who diagnosed the teenager with suspected depression. But still feeling uneasy about her daughter’s behavior, she arranged for Claire to see a pediatrician.

“After carrying out a neurological examination he told me that he suspected Claire had a brain tumor,” recalls Annie. “My world just fell apart.”

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Claire was immediately admitted to Frenchay Children’s Hospital in Bristol, 100 miles away, for more tests.

“Over the next week she was tested from head to toe,” says Annie. “She had MRI scans, a lumbar puncture, biopsies, neurological testing and seemingly every blood test going but the doctors couldn’t find anything.”

Yet Claire’s health was deteriorating rapidly. She had trouble with her balance, felt very weak and couldn’t walk.

“Eventually, they told me the news I’d dreaded the most,” recalls Annie. “Claire had suspected vCJD. It was like being punched in the stomach. I knew what it meant. Claire was being handed a death sentence.”

Since doctors are not able to confirm a patient had vCJD until a brain biopsy is conducted after their death, there were no more answers.

All Annie could do was take Claire back to the home they shared with Annie’s partner, Wayne, and Claire’s older brother.

“Back home, Claire asked me if she was going to die,” recalls Annie. “All I could say was that I didn’t know. She said she was scared that it would hurt, so I promised Claire that if there was any pain I would make sure it was relieved. She seemed eerily calm, like she’d accepted her fate. I could hardly believe what was happening.”

Over the next four months, Claire grew weaker and weaker, rapidly becoming less and less mobile. She was on medication to ease her anxiety and painkillers for her muscle spasms. She needed help dressing herself and eating and drinking but as she didn’t want to go back to hospital, a place was arranged for Claire at Little Bridge House, a children’s hospice in Fremington near Barnstaple. There, staff doted on Claire and she was able to find peaceful moments, listening to music in their sensory room.

“As time went on she couldn’t move at all,” says Annie. “She began to slur her speech and I wondered if she’d remember me the next day.”

biosolids land application and disease

Claire spent Christmas at home, returning to the hospice a few days later. She had been excited about the millennium New Year’s Eve but, fading rapidly, she slept through all the celebrations.

“The next morning she couldn’t believe she’d missed it all,” says Annie. “When the nurse asked what she’d like for breakfast she requested Buck’s Fizz! Then she asked to be lifted into her chair so she could go around and say ‘Happy New Year’ to everyone. I think that was her way of saying goodbye – she died 10 days later on January 11. Her brother and I were sat by her side as Claire slipped away in her sleep.”

Over the following months the pain of losing her daughter took its toll and in November 2000 Annie began to experience problems with her own health. She was diagnosed with post-traumatic stress disorder, depression and chronic fatigue. She developed an autoimmune disorder, which left her weak and immobile. Too weak to get out of bed, Annie felt eaten up by grief.

“I was in a terrible place,” she says. “I was devastated, frustrated and unable to do anything. All I could think about was Claire and what had happened to her. I felt consumed by anger that the government compensation promised was taking so long, not just for me, but for the vCJD families still caring for people. These families were going through the worst time of their lives and finding the process of getting compensation very difficult. I wanted to do something to help but the legal process confused me. I needed to understand it, to make sense of it, so in 2004 I decided to study law through the Open University,” says Claire. “My aim was to support families so they could get a care package and be compensated fairly.”

Wheelchair-bound and still suffering from debilitating fatigue, Annie made it her mission to complete her degree.

During her six years of study with the OU she put her learning into practice, too, regularly fighting tooth and nail for the rights of other vCJD families (prion disease). Although Annie, now 54, did receive a payout in 2006, she was dismayed by the system that compensated families purely on the basis of how well they could express the severity of their suffering. So in 2010, she and other families took their case to the High Court, claiming the compensation scheme was flawed. Although their challenge and a subsequent Court of Appeal action failed, Annie was able to find peace in the fact she had done everything she could.

prion disease epidemic

“The judge said he sympathized with our case but he had to apply legal principles,” she says. “It was disappointing but we kept it in the public eye for a long time. We made our mark.”

Later that year, Annie graduated with a Bachelor of Law honors degree, which she dedicated to Claire’s memory during the ceremony. She now plans to take a masters degree in Medical Ethics.

“I cannot praise the Open University enough,” she says. “It allows people like me, who can’t go to university full time, to study for a degree. The quality of the courses and the support they have given me has been excellent.”

And Annie is still putting her studies to good use.

“There are so many downtrodden people out there because they don’t know where to start with the law,” she says. “I work for a couple of unions, looking at cases, giving them advice, assisting their members and helping them with personal injury claims.

“When you have a law degree in a small town, everyone comes for help. I’m very busy and quite content with that. I can’t think of anything more worthwhile.”

And despite the hardships she has endured, she remains upbeat.

“Losing Claire was the worst moment of my life,” she says. “I’m in a life that doesn’t feel real. I’m waiting for my girl to come back but she won’t. It is a physical pain. But what I went through was nothing compared to Claire.

“I’ve had a good life. I may be incapacitated but whenever I feel sorry for myself she pops into my head. Claire was interested in law and she might well have gone on to study it herself if she’d had the chance. She missed out on so many chances so I’m determined to make the most of mine.”

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Mad Cow Disease Related To Alzheimer’s Disease

Prions Link Mad Cow Disease, Chronic Wasting Disease and Alzheimer’s Disease

Prion disease is being mismanaged around the globe, which is contributing to the migration, mutation, and exponential growth in the deadly contagion. Our food, water and healthcare systems are now critical pathways that must be guarded much more closely.

Not surprisingly, mad cow disease, clinically known as bovine spongiform encephalopathy (BSE), has been rampant in the U.S. for decades. The human form of mad cow is Creutzfeldt-Jakob disease (CJD). The USDA and FDA have done a very good job of keeping this under wraps, as well as displaying a healthy disregard for human life by their neglect as well as their silence. The testing on cattle raised for food in the U.S. is ‘careless’ and ‘irresponsible’ according to The World Health Organization (WHO). The mismanagement goes much further than mad cow disease.

mad cow disease and prions

Testing one cow out of every 2,000 animals slaughtered is reckless, since the disease is unstoppable in soil, water and other areas infected by victims. Because of this fact, no one knows how many infected cattle enter the human food chain; however it is certain it leads to CJD and Alzheimer’s disease.

Food Safety and WHO Precautions

WHO has issued a warning stating that the U.S. is violating the guidelines set forth for the prevention of BSE or mad cow disease making its way into the human population. WHO states that the U.S. is inadequately testing the brains of human dementia victims and is likely missing hundreds of human cases of Creutzfeldt Jakob Disease (CJD), caused by the reckless management of prion pathways, including human sewage, sewage sludge and biosolids.

The warning goes on to state that the feeding of infected animals to other animals must be ceased immediately. The feeding of slaughterhouse waste (which also goes into the sewage systems around the world), including blood, feathers and excrement, to other farmed animals is causing major health risks to all who eat beef, or any other farmed animal. Deer, elk, sheep, pigs and chickens can all carry this disease in different forms.

Prions and Prusiner win Nobel Prize

Prions Connect Alzheimer’s CJD and Mad Cow Disease

CJD and Alzheimer’s disease are caused by an infectious prion, which is (not) a virus. A prion is a protein, but a mutated protein that is somewhat different in shape. These prions fold into an abnormal pattern, at which time they begin killing off brain cells by the millions.

Steven Strittmatter, Professor of Neurology at Yale University, comments, “It’s too bizarre that these two diseases would share this common protein.”

Further, a well-known physician said, “The most frequent misdiagnosis of CJD among the elderly is Alzheimer’s disease. Neither CJD nor Alzheimer’s can be conclusively diagnosed without a brain biopsy, and the symptoms and pathology of both diseases overlap,” said Michael Greger, M.D.

The gestation period for this prion can be years or even decades. The problem with this is that many people infected will not even show signs of the disease for years, and the final death toll may not show up until it’s too late to actually do something about the rest of the population. Also, since CJD is often mis-diagnosed, getting the true picture will be difficult.

Regrettably, the National Institute of Neurological Disorders indicates that there is not one single diagnostic test for detecting CJD. The only way to confirm a diagnosis of CJD is by brain biopsy or autopsy. The biopsy is a dangerous procedure because it means removing a part of a person’s brain, and getting the part that is infected is not likely. And, when testing in either autopsy or biopsy, surgeons performing the test have to take extreme care to be certain they don’t become infected themselves. Strict surgical and disinfection procedures must be followed to perform this kind of test.

I’d venture to say that most doctors would do just about anything BUT this, in order to avoid the risks involved, as well as the time and expense; hence – misdiagnosis.

Alzheimer's disease epidemic

Alzheimer’s Disease Epidemic

Today, Alzheimer’s disease is the 6th leading cause of death in the U.S. It is the only disease that causes certain death, because it cannot be prevented by medicine, or cured or even slowed down.

From 2000 to 2008, in the U.S. alone, deaths from Alzheimer’s disease have risen sixty-six percent (66%). An estimated 5.4 million people in the U.S. have Alzheimer’s in 2011.  This includes people over the age of 65, and younger people who have young-onset Alzheimer’s.

Scientists believe it is Mad Cow gone rampant and have found a possible link to this horrible brain-wasting disease – and most other types of dementia. A link to Parkinson’s, Huntington’s disease, Lou Gehrig’s disease, and others has also been made.

Dr. Greger explains, “Mad-Cow disease is caused by unconventional pathogens called prions–literally infectious proteins–which, because of their unique structure, are practically invulnerable, surviving even incineration at temperatures hot enough to melt lead.”   Sadly, pigs can also carry the disease and since they are slaughtered long before any symptoms can surface, it is difficult to diagnose.

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According to Dr. Greger: “Laboratory experiments show that pigs can indeed be infected by Mad-Cow brains– and hundreds of thousands of downer pigs, too sick or crippled by injury to even walk, arrive at U.S. slaughterhouses every year.”

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Prion Disease Described By Prusiner

Prions Cause Many Neurological Disorders

By Stanley B. Prusiner, Nobel-Prize Laureate, Prion Discovery and Research

Fifteen years ago I evoked a good deal of skepticism when I proposed that the infectious agents causing certain degenerative disorders of the central nervous system in animals and, more rarely, in humans might consist of protein and nothing else. At the time, the notion was heretical. Dogma held that the conveyers of transmissible diseases required genetic material, composed of nucleic acid (DNA or RNA), in order to establish an infection in a host. Even viruses, among the simplest microbes, rely on such material to direct synthesis of the proteins needed for survival and replication.

Prions and Prusiner win Nobel Prize

Later, many scientists were similarly dubious when my colleagues and I suggested that these “proteinaceous infectious particles”–or prions, as I called the disease-causing agents–could underlie inherited, as well as communicable, diseases. Such dual behavior was then unknown to medical science.

And we met resistance again when we concluded that prions (PREE-ons) multiply in an incredible way; they convert normal protein molecules into dangerous ones simply by inducing the benign molecules to change their shape. Today, however, a wealth of experimental and clinical data has made a convincing case that we are correct on all three counts.

Prions are indeed responsible for transmissible and inherited disorders of protein conformation. They can also cause sporadic disease, in which neither transmission between individuals nor inheritance is evident.

Moreover, there are hints that the prions causing the diseases explored thus far may not be the only ones. Prions made of rather different proteins may contribute to other neurodegenerative diseases that are quite prevalent in humans. They might even participate in illnesses that attack muscles.

The known prion diseases, all fatal, are sometimes referred to as spongiform encephalopathies. They are so named because they frequently cause the brain to become riddled with holes. These ills, which can brew for years (or even for decades in humans) are widespread in animals. A common form is scrapie, found in sheep and goats. Afflicted animals lose coordination and eventually become so incapacitated that they cannot stand. They also become irritable and, in some cases, develop an intense itch that leads them to scrape off their wool or hair (hence the name “scrapie”).

chronic wasting disease cause

The other prion diseases of animals go by such names as transmissible mink encephalopathy, chronic wasting disease of mule deer and elk, feline spongiform encephalopathy and bovine spongiform encephalopathy. The last, often called mad cow disease, is the most worrisome. They all are deadly and unstoppable. There might not be any difference between these diseases, except for the resistance of the victim.

mad cow disease and prions

Gerald A. H. Wells and John W. Wilesmith of the Central Veterinary Laboratory in Weybridge, England, identified the condition in 1986, after it began striking cows in Great Britain, causing them to became uncoordinated and unusually apprehensive. The source of the emerging epidemic was soon traced to a food supplement that included meat and bone meal from dead sheep. The methods for processing sheep carcasses had been changed in the late 1970s. Where once they would have eliminated the scrapie agent in the supplement, now they apparently did not. The British government banned the use of animal-derived feed supplements in 1988, and the epidemic has probably peaked. Nevertheless, many people continue to worry that they will eventually fall ill as a result of having consumed tainted meat.

The human prion diseases are more obscure. Kuru has been seen only among the Fore Highlanders of Papua New Guinea. They call it the “laughing death.” Vincent Zigas of the Australian Public Health Service and D. Carleton Gajdusek of the U.S. National Institutes of Health described it in 1957, noting that many highlanders became afflicted with a strange, fatal disease marked by loss of coordination (ataxia) and often later by dementia. The affected individuals probably acquired kuru through ritual cannibalism: the Fore tribe reportedly honored the dead by eating their brains. The practice has since stopped, and kuru has virtually disappeared.

Alzheimer's disease epidemic

Creutzfeldt-Jakob disease, in contrast, occurs worldwide and usually becomes evident as dementia. Most of the time it appears sporadically, striking one person in a million, typically around age 60. About 10 to 15 percent of cases are inherited, and a small number are, sadly, iatrogenic–spread inadvertently by the attempt to treat some other medical problem. Iatrogenic Creutzfeldt-Jakob disease has apparently been transmitted by corneal transplantation, implantation of dura mater or electrodes in the brain, use of contaminated surgical instruments, and injection of growth hormone derived from human pituitaries (before recombinant growth hormone became available).

The two remaining human disorders are Gerstmann-Straussler-Scheinker disease (which is (2) manifest as ataxia and other signs of damage to the cerebellum) and fatal familial insomnia (in which dementia follows difficulty sleeping). Both these conditions are usually inherited and typically appear in midlife. Fatal familial insomnia was discovered only recently, by Elio Lugaresi and Rossella Medori of the University of Bologna and Pierluigi Gambetti of Case Western Reserve University.

I first became intrigued by the prion diseases in 1972, when as a resident in neurology at the University of California School of Medicine at San Francisco, I lost a patient to Creutzfeldt-Jakob disease. As I reviewed the scientific literature on that and related conditions, I learned that scrapie, Creutzfeldt-Jakob disease and kuru had all been shown to be transmissible by injecting extracts of diseased brains into the brains of healthy animals. The infections were thought to be caused by a slow-acting virus, yet no one had managed to isolate the culprit (Prusiner later stated that he believes that Alzheimer’s disease is a prion disease).

In the course of reading, I came across an astonishing report in which Tikvah Alper and her colleagues at the Hammersmith Hospital in London suggested that the scrapie agent might lack nucleic acid, which usually can be degraded by ultraviolet or ionizing radiation. When the nucleic acid in extracts of scrapie-infected brains was presumably destroyed by those treatments, the extracts retained their ability to transmit scrapie. If the organism did lack DNA and RNA, the finding would mean that it was not a virus or any other known type of infectious agent, all of which contain genetic material. What, then, was it?

Investigators had many ideas–including, jokingly, linoleum and kryptonite–but no hard answers. I immediately began trying to solve this mystery when I set up a laboratory at U.C.S.F. in 1974. The first step had to be a mechanical one–purifying the infectious material in scrapie-infected brains so that its composition could be analyzed. The task was daunting; many investigators had tried and failed in the past. But with the optimism of youth, I forged ahead [see “Prions,” by Stanley B. Prusiner; SCIENTIFIC AMERICAN, October 1984].

Alzheimer's disease prevention

Amazing Prion Discovery

All our results pointed toward one startling conclusion: the infectious agent in scrapie (and presumably in the related diseases) did indeed lack nucleic acid and consisted mainly, if not exclusively, of protein. We deduced that DNA and RNA were absent because, like Alper, we saw that procedures known to damage nucleic acid did not reduce infectivity. And we knew protein was an essential component because procedures that denature (unfold) or degrade protein reduced infectivity.

I thus introduced the term “prion” to distinguish this class of disease conveyer from viruses, bacteria, fungi and other known pathogens. Not long afterward, we determined that scrapie prions contained a single protein that we called PrP, for “prion protein.” Now the major question became; Where did the instructions specifying the sequence of amino acids in PrP reside? Were they carried by an undetected piece of DNA that traveled with PrP, or were they, perhaps, contained in a gene housed in the chromosomes of cells?

The key to this riddle was the identification in 1984 of some 15 amino acids at one end of the PrP protein. My group identified this short amino acid sequence in collaboration with Leroy E. Hood and his co-workers at the California Institute of Technology. Knowledge of the sequence allowed us and others to construct molecular probes, or detectors, able to indicate whether mammalian cells carried the PrP gene. With probes produced by Hood’s team, Bruno Oesch, working in the laboratory of Charles Weissmann at the University of Zurich, showed that hamster cells do contain a gene for PrP. At about the same time, Bruce Cheseboro of the NIH Rocky Mountain Laboratories made his own probes and established that mouse cells harbor the gene as well. That work made it possible to isolate the gene and to establish that it resides not in prions but in the chromosomes of hamsters, mice, humans and all other mammals that have been examined. What is more, most of the time, these animals make PrP without getting sick.

One interpretation of such findings was that we had made a terrible mistake: PrP had nothing to do with prion diseases. Another possibility was that PrP could be produced in two forms, one that generated disease and one that did not. We soon showed the latter interpretation to be correct. The critical clue was the fact that the PrP found in infected brains resisted breakdown by cellular enzymes called proteases.

Most proteins in cells are degraded fairly easily. I therefore suspected that if a normal, (3) nonthreatening form of PrP existed, it too would be susceptible to degradation. Ronald A. Barry in my laboratory then identified this hypothetical protease-sensitive form. It thus became clear that scrapie-causing PrP is a variant of a normal protein. We therefore called the normal protein “cellular PrP” and the infectious (protease-resistant) form “scrapie PrP.” The latter term is now used to refer to the protein molecules that constitute the prions causing all scrapie-like diseases of animals and humans.

Alzheimers disease epidemic

Prion Diseases Can Be Inherited

Early on we had hoped to use the PrP gene to generate pure copies of PrP. Next, we would inject the protein molecules into animals, secure in the knowledge that no elusive virus was clinging to them. If the injections caused scrapie in the animals, we would have shown that protein molecules could, as we had proposed, transmit disease. By 1986, however, we knew the plan would not work. For one thing, it proved very difficult to induce the gene to make the high levels of PrP needed for conducting studies. For another thing, the protein that was produced was the normal, cellular form. Fortunately, work on a different problem led us to an alternative approach for demonstrating that prions could transmit scrapie without the help of any accompanying nucleic acid.

In many cases, the scrapie-like illnesses of humans seemed to occur without having been spread from one host to another, and in some families they appeared to be inherited. (Today researchers know that about 10 percent of human prion diseases are familial, felling half of the members of the affected families.) It was this last pattern that drew our attention. Could it be that prions were more unusual than we originally thought? Were they responsible for the appearance of both hereditary and transmissible illnesses? In 1988 Karen Hsiao in my laboratory and I uncovered some of the earliest data showing that human prion diseases can certainly be inherited. We acquired clones of a PrP gene obtained from a man who had Gerstmann-Straussler-Scheinker disease in his family and was dying of it himself. Then we compared his gene with PrP genes obtained from a healthy population and found a tiny abnormality known as a point mutation.

To grasp the nature of this mutation, it helps to know something about the organization of genes. Genes consist of two strands of the DNA building blocks called nucleotides, which differ from one another in the bases they carry. The bases on one strand combine with the bases on the other strand to form base pairs: the “rungs” on the familiar DNA “ladder.” In addition to holding the DNA ladder together, these pairs spell out the sequence of amino acids that must be strung together to make a particular protein. Three base pairs together–a unit called a codon–specify a single amino acid. In our dying patient, just one base pair (out of more than 750) had been exchanged for a different pair. The change, in turn, had altered the information carried by codon 102, causing the amino acid leucine to be substituted for the amino acid proline in the man’s PrP protein.

With the help of Tim J. Crow of Northwick Park Hospital in London and Jurg Ott of Columbia University and their colleagues, we discovered the same mutation in genes from a large number of patients with Gerstmann-Straussler-Scheinker disease, and we showed that the high incidence in the affected families was statistically significant. In other words, we established genetic linkage between the mutation and the disease–a finding that strongly implies the mutation is the cause. Over the past six years work by many investigators has uncovered 18 mutations in families with inherited prion diseases; for five of these mutations, enough cases have now been collected to demonstrate genetic linkage. The discovery of mutations gave us a way to eliminate the possibility that a nucleic acid was traveling with prion proteins and directing their multiplication.

We could now create genetically altered mice carrying a mutated PrP gene. If the presence of the altered gene in these “transgenic” animals led by itself to scrapie, and if the brain tissue of the transgenic animals then caused scrapie in healthy animals, we would have solid evidence that the protein encoded by the mutated gene had been solely responsible for the transfer of disease. Studies I conducted with Hsiao, Darlene Groth in my group and Stephen J. DeArmond, head of a separate laboratory at U.C.S.F., have now shown that scrapie can be generated and transmitted in this way [see BOX at end of this article]. These results in animals resemble those obtained in 1981, when Gajdusek, Colin L. Masters and Clarence J. Gibbs, Jr., all at the National Institutes of Health, transmitted apparently inherited Gerstmann-Straussler-Scheinker disease to monkeys. They also resemble the findings of Jun Tateishi and Tetsuyuki Kitamoto of Kyushu University in Japan, who transmitted inherited Creutzfeldt-Jakob disease to mice.

Together the collected transmission studies persuasively argue that prions do, after all, (4) represent an unprecedented class of infectious agents, composed only of a modified mammalian protein. And the conclusion is strengthened by the fact that assiduous searching for a scrapie-specific nucleic acid (especially by Detlev H. Riesner of Heinrich Heine University in Dusseldorf) has produced no evidence that such genetic material is attached to prions. Scientists who continue to favor the virus theory might say that we still have not proved our case. If the PrP gene coded for a protein that, when mutated, facilitated infection by a ubiquitous virus, the mutation would lead to viral infection of the brain. Then injection of brain extracts from the mutant animal would spread the infection to another host. Yet in the absence of any evidence of a virus, this hypothesis looks to be untenable.

In addition to showing that a protein can multiply and cause disease without help from nucleic acids, we have gained insight into how scrapie PrP propagates in cells. Many details remain to be worked out, but one aspect appears quite clear: the main difference between normal PrP and scrapie PrP is conformational. Evidently, the scrapie protein propagates itself by contacting normal PrP molecules and somehow causing them to unfold and flip from their usual conformation to the scrapie shape. This change initiates a cascade in which newly converted molecules change the shape of other normal PrP molecules, and so on. These events apparently occur on a membrane in the cell interior.

We started to think that the differences between cellular and scrapie forms of PrP must be conformational after other possibilities began to seem unlikely. For instance, it has long been known that the infectious form often has the same amino acid sequence as the normal type. Of course, molecules that start off being identical can later be chemically modified in ways that alter their activity. But intensive investigations by Neil Stahl and Michael A. Baldwin in my laboratory have turned up no differences of this kind.

treat Alzheimer's disease


The Protein Pathogen

How, exactly, do the structures of normal and scrapie forms of PrP differ? Studies by Keh-Ming Pan in our group indicate that the normal protein consists primarily of alpha helices, regions in which the protein backbone twists into a specific kind of spiral; the scrapie form, however, contains beta strands, regions in which the backbone is fully extended. Collections of these strands form beta sheets. Fred E. Cohen, who directs another laboratory at U.C.S.F., has used molecular modeling to try to predict the structure of the normal protein based on its amino acid sequence. His calculations imply that the protein probably folds into a compact structure having four helices in its core.

Less is known about the structure, or structures, adopted by scrapie PrP. The evidence supporting the proposition that scrapie PrP can induce an alpha-helical PrP molecule to switch to a beta-sheet form comes primarily from two important studies by investigators in my group. Maria Gasset learned that synthetic peptides (short strings of amino acids) corresponding to three of the four putative alpha-helical regions of PrP can fold into beta sheets. And Jack Nguyen has shown that in their beta-sheet conformation, such peptides can impose a beta-sheet structure on helical PrP peptides. More recently Byron W. Caughey of the Rocky Mountain Laboratories and Peter T. Lansbury of the Massachusetts Institute of Technology have reported that cellular PrP can be converted into scrapie PrP in a test tube by mixing the two proteins together.

PrP molecules arising from mutated genes probably do not adopt the scrapie conformation as soon as they are synthesized. Otherwise, people carrying mutant genes would become sick in early childhood. We suspect that mutations in the PrP gene render the resulting proteins susceptible to flipping from an alpha-helical to a beta-sheet shape. Presumably, it takes time until one of the molecules spontaneously flips over and still more time for scrapie PrP to accumulate and damage the brain enough to cause symptoms. Fred Cohen and I think we might be able to explain why the various mutations that have been noted in PrP genes could facilitate folding into the beta-sheet form.

Many of the human mutations give rise to the substitution of one amino acid for another within the four putative helices or at their borders. Insertion of incorrect amino acids at those positions might destabilize a helix, thus increasing the likelihood that the affected helix and its neighbors will refold into a beta-sheet conformation. Conversely, Hermann Schatzel in my laboratory finds that the harmless differences distinguishing the PrP gene of humans from those of apes and monkeys affect amino acids lying outside of the proposed helical domains–where the divergent amino acids probably would not profoundly influence the stability of the helical regions.

No one knows exactly how propagation of scrapie PrP damages cells. In cell cultures, the conversion of normal PrP to the scrapie form occurs inside neurons, after which scrapie PrP accumulates in intracellular vesicles known as lysosomes. In the brain, filled lysosomes could conceivably burst and damage cells. As the diseased cells died, creating holes in the brain, their prions would be released to attack other cells. We do know with certainty that cleavage of scrapie PrP is what produces PrP fragments that accumulate as plaques in the brains of some patients. Those aggregates resemble plaques seen in Alzheimer’s disease, although the Alzheimer’s clumps consist of a different protein. The PrP plaques are a useful sign of prion infection, but they seem not to be a major cause of impairment. In many people and animals with prion disease, the plaques do not arise at all.

Even though we do not yet know much about how PrP scrapie harms brain tissue, we can foresee that an understanding of the three-dimensional structure of the PrP protein will lead to therapies. If, for example, the four-helix-bundle model of PrP is correct, drug developers might be able to design a compound that would bind to a central pocket that could be formed by the four helices. So bound, the drug would stabilize these helices and prevent their conversion into beta sheets.

Another idea for therapy is inspired by research in which Weissmann and his colleagues applied gene-targeting technology to create mice that lacked the PrP gene and so could not make PrP. By knocking out a gene and noting the consequences of its loss, one can often deduce the usual functions of the gene’s protein product. In this case, however, the animals missing PrP displayed no detectable abnormalities. If it turns out that PrP is truly inessential, then physicians might one day consider delivering so-called antisense or antigene therapies to the brains of patients with prion diseases. Such therapies aim to block genes from giving rise to unwanted proteins and could potentially shut down production of cellular PrP [see “The New Genetic Medicines,” by Jack S. Cohen and Michael E. Hogan; SCIENTIFIC AMERICAN, December 1994].

They would thereby block PrP from propagating itself. It is worth noting that the knockout mice provided a welcomed opportunity to challenge the prion hypothesis. If the animals became ill after inoculation with prions, their sickness would have indicated that prions could multiply even in the absence of a preexisting pool of PrP molecules. As I expected, inoculation with prions did not produce scrapie, and no evidence of prion replication could be detected.

The enigma of how scrapie PrP multiplies and causes disease is not the only puzzle starting to be solved. Another long-standing question–the mystery of how prions consisting of a single kind of protein can vary markedly 2n their effects–is beginning to be answered as well. Lain H. Pattison of the Agriculture Research Council in Compton, England, initially called attention to this phenomenon. Years ago he obtained prions from two separate sets of goats. One isolate made inoculated animals drowsy, whereas the second made them hyperactive. Similarly, it is now evident that some prions cause disease quickly, whereas others do so slowly.

Prion Mutations

Alan G. Dickinson, Hugh Fraser and Moira E. Bruce of the Institute for Animal Health in Edinburgh, who have examined the differential effects of varied isolates in mice, are among those who note that only pathogens containing nucleic acids are known to occur in multiple strains. Hence, they and others assert, the existence of prion “strains” indicates the prion hypothesis must be incorrect; viruses must be at the root of scrapie and its relatives. Yet because efforts to find viral nucleic acids have been unrewarding, the explanation for the differences must lie elsewhere. One possibility is that prions can adopt multiple conformations. Folded in one way, a prion might convert normal PrP to the scrapie form highly efficiently, giving rise to short incubation times. Folded another way, it might work less efficiently. Similarly, one “conformer” might be attracted to neuronal populations in one part of the brain, whereas another might be attracted to neurons elsewhere, thus producing different symptoms. Considering that PrP can fold in at least two ways, it would not be surprising to find it can collapse into other structures as well.

Since the mid-1980s we have also sought insight into a phenomenon known as the species barrier. This concept refers to the fact that something makes it difficult for prions made by one species to cause disease in animals of another species. The cause of this difficulty is of considerable interest today because of the epidemic of mad cow disease in Britain. We and others have been trying to find out whether the species barrier is strong (6) enough to prevent the spread of prion disease from cows to humans.


There Is No Species Barrier

The barrier was discovered by Pattison, who in the 1960s found it hard to transmit scrapie between sheep and rodents. To determine the cause of the trouble, my colleague Michael R. Scott and I later generated transgenic mice expressing the PrP gene of the Syrian hamster–that is, making the hamster PrP protein. The mouse gene differs from that of the hamster gene at 16 codons out of 254. Normal mice inoculated with hamster prions rarely acquire scrapie, but the transgenic mice became ill within about two months. We thus concluded that we had broken the species barrier by inserting the hamster genes into the mice. Moreover, on the basis of this and other experiments, we realized that the barrier resides in the amino acid sequence of PrP: the more the sequence of a scrapie PrP molecule resembles the PrP sequence of its host, the more likely it is that the host will acquire prion disease.

In one of those other experiments, for example, we examined transgenic mice carrying the Syrian hamster PrP gene in addition to their own mouse gene. Those mice make normal forms of both hamster and mouse PrP. When we inoculated the animals with mouse prions, they made more mouse prions. When we inoculated them with hamster prions, they made hamster prions. From this behavior, we learned that prions preferentially interact with cellular PrP of homologous, or like, composition. The attraction of scrapie PrP for cellular PrP having the same sequence probably explains why scrapie managed to spread to cows in England from food consisting of sheep tissue: sheep and bovine PrP differ only at seven positions. In contrast, the sequence difference between human and bovine PrP is large: the molecules diverge at more than 30 positions. Because the variance is great, the likelihood of transmission from cows to people would seem to be low.

Consistent with this assessment are epidemiological studies by W. Bryan Matthews, a professor emeritus at the University of Oxford. Matthews found no link between scrapie in sheep and the occurrence of Creutzfeldt-Jakob disease in sheep-farming countries. On the other hand, two farmers who had “mad cows” in their herds have recently died of Creutzfeldt-Jakob disease. Their deaths may have nothing to do with the bovine epidemic, but the situation bears watching. It may turn out that certain parts of the PrP molecule are more important than others for breaking the species barrier.

If that is the case, and if cow PrP closely resembles human PrP in the critical regions, then the likelihood of danger might turn out to be higher than a simple comparison of the complete amino acid sequences would suggest. We began to consider the possibility that some parts of the PrP molecule might be particularly important to the species barrier after a study related to this blockade took an odd turn. My colleague Glenn C. Telling had created transgenic mice carrying a hybrid PrP gene that consisted of human codes flanked on either side by mouse codes; this gene gave rise to a hybrid protein. Then he introduced brain tissue from patients who had died of Creutzfeldt-Jakob disease or Gerstmann-Straussler-Scheinker disease into the transgenic animals.

Oddly enough, the animals became ill much more frequently and faster than did mice carrying a full human PrP gene, which diverges from mouse PrP at 28 positions. This outcome implied that similarity in the central region of the PrP molecule may be more critical than it is in the other segments. The result also lent support to earlier indications–uncovered by Shu-Lian Yang in DeArmond’s laboratory and Albert Taraboulos in my group–that molecules made by the host can influence the behavior of scrapie PrP. We speculate that in the hybrid-gene study, a mouse protein, possibly a “chaperone” normally involved in folding nascent protein chains, recognized one of the two mouse-derived regions of the hybrid PrP protein. This chaperone bound to that region and helped to refold the hybrid molecule into the scrapie conformation. The chaperone did not provide similar help in mice making a totally human PrP protein, presumably because the human protein lacked a binding site for the mouse factor.

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Prion Disease Spreading Through Sewage

An unforeseen story has recently emerged from studies of transgenic mice making unusually high amounts of normal PrP proteins. DeArmond, David Westaway in our group and George A. Carlson of the McLaughlin Laboratory in Great Falls, Mont., became perplexed when they noted that some older transgenic mice developed an illness characterized by rigidity and diminished grooming.

When we pursued the cause, we found that making excessive amounts of PrP can (7) eventually lead to neurodegeneration and, surprisingly, to destruction of both muscles and peripheral nerves. These discoveries widen the spectrum of prion diseases and are prompting a search for human prion diseases that affect the peripheral nervous system and muscles. Investigations of animals that overproduce PrP have yielded another benefit as well.

They offer a clue as to how the sporadic form of Creutzfeldt-Jakob disease might arise. For a time I suspected that sporadic disease might begin when the wear and tear of living led to a mutation of the PrP gene in at least one cell in the body. Eventually, the mutated protein might switch to the scrapie form and gradually propagate itself, until the buildup of scrapie PrP crossed the threshold to overt disease. The mouse studies suggest that at some point in the lives of the one in a million individuals who acquire sporadic Creutzfeldt-Jakob disease, cellular PrP may spontaneously convert to the scrapie form.

The experiments also raise the possibility that people who become afflicted with sporadic Creutzfeldt-Jakob disease overproduce PrP, but we do not yet know if, in fact, they do. All the known prion diseases in humans have now been modeled in mice. With our most recent work we have inadvertently developed an animal model for sporadic prion disease. Mice inoculated with brain extracts from scrapie-infected animals and from humans afflicted with Creutzfeldt-Jakob disease have long provided a model for the infectious forms of prion disorders. And the inherited prion diseases have been modeled in transgenic mice carrying mutant PrP genes.

These murine representations of the human prion afflictions should not only extend understanding of how prions cause brain degeneration, they should also create opportunities to evaluate therapies for these devastating maladies.

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No Difference Between TSEs

Ongoing research may also help determine whether prions consisting of other proteins play a part in more common neurodegenerative conditions, including Alzheimer’s disease, Parkinson’s disease and amyotrophic lateral sclerosis. There are some marked similarities in all these disorders. As is true of the known prion diseases, the more widespread ills mostly occur sporadically but sometimes “run” in families. All are also usually diseases of middle to later life and are marked by similar pathology: neurons degenerate, protein deposits can accumulate as plaques, and glial cells (which support and nourish nerve cells) grow larger in reaction to damage to neurons.

Strikingly, in none of these disorders do white blood cells–those ever present warriors of the immune system–infiltrate the brain. If a virus were involved in these illnesses, white cells would be expected to appear. Recent findings in yeast encourage speculation that prions unrelated in amino acid sequence to the PrP protein could exist. Reed B. Wickner of the NIH reports that a protein called Ure2p might sometimes change its conformation, thereby affecting its activity in the cell. In one shape, the protein is active; in the other, it is silent. The collected studies described here argue persuasively that the prion is an entirely new class of infectious pathogen and that prion diseases result from aberrations of protein conformation. Whether changes in protein shape are responsible for common neurodegenerative diseases, such as Alzheimer’s, remains unknown, but it is a possibility that should not be ignored.

Several studies have shown that prions composed only of PrP are able to convey infection from one animal to another. In one such experiment, the author and his colleagues created mice carrying many copies of a mutant PrP gene; these animals made high levels of mutant PrP, some of which appears to adopt the scrapie conformation. Eventually all the mice displayed symptoms of brain damage and died.

Then the workers injected brain tissue from the diseased animals into genetically altered mice making low levels of the same mutant PrP protein. (Such mice were chosen as recipients because scrapie PrP is most attracted to PrP molecules having the same composition.) Uninoculated mice did not become ill (indicating that making low levels of the aberrant protein was safe), but many of the treated ones did. Moreover, brain tissue transferred from the diseased recipients to their healthy counterparts caused illness once again. If the aberrant protein were unable to transmit infection, none of the inoculated animals would have sickened.


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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 special expertise. Please contact Gary Chandler to join our coalition for reform