Brain Researchers Create Synthetic Prion

Infectious Proteins Cause Many Brain-Wasting Diseases

Prion research is still unfolding, but researchers have successfully created a synthetic version, which could help solve some riddles.

Neurodegenerative disease , including Alzheimer’s disease, is the fastest-growing cause of death in the world. Autism also continues to surge. Some parts of the world are impacted more than others.

A variety of factors can trigger neurodegenerative disease, including genetics, head trauma and neurotoxins. Exposure to deadly proteins, however, could be the greatest threat to your brain.

Brain-wasting diseases are a terrifying prospect, made all the more distressing because of the lack of effective treatments. While we know that such disorders, like Creutzfeldt-Jakob disease (CJD), mad cow disease and chronic wasting disease (deer) are caused by infectious proteins called prions, experts have struggled to decode these proteins. However, we know that they migrate, mutate, multiply and kill. We know that they aren’t alive, therefore, we can’t kill them. Neutralizing them with complete confidence in all conditions, including in vivo, is virtually impossible. So far, prion diseases are always incurable and fatal. They also are highly transmissible.

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing prions (PREE-ons) and prion disease, also known as transmissible spongiform encephalopathy (TSE). The operative word is “transmissible.”

Prion disease and Alzheimer's disease

President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. Unfortunately, Prusiner’s science is being ignored.

Prions are a deadly and unstoppable form of protein that migrates, mutates, multiplies and kills with unparalleled efficiency.

TSE is a spectrum disease. The spectrum includes Alzheimer’s disease, Parkinson’s disease and an extremely aggressive version known as Creutzfeldt-Jakob disease. Prusiner claims that all forms of TSE are caused by infectious prions. The prion spectrum varies in severity. It also varies depending on which region of the brain is impacted first. When the presenting symptom is memory loss, the diagnoses flow along the following chart.

prion disease spectrum

Prions cause fatal neurodegenerative diseases in humans and animals by converting the cellular version of prion protein into a toxic form that builds up in the brain.

Scientists at Case Western Reserve University School of Medicine (CWRU) have synthesized the world’s first artificial human brain prion in a lab. Case Western is a global leader on prion research. It hopes that its new development will help us better understand how these deadly, infectious proteins misfold, spread and kill mammals–and possibly other species.

“This accomplishment represents a watershed event,” said Jiri G. Safar, the study’s lead author. “Until now our understanding of prions in the brain has been limited. Being able to generate synthetic human prions in a test tube, as we have done, will enable us to achieve a much richer understanding of prion structure and replication.

“This is crucial for developing inhibitors of their replication and propagation throughout the brain, which is essential for halting prion-based brain disease.”

The better we understand prions, the closer we get to developing treatments. What we already know is that prions are proteins that have folded incorrectly, which can cause neighboring proteins to continue the deadly sequence until the neurodegeneration carves holes throughout the entire brain. Upon death, the brain looks like a sponge.

In Nature Communications, scientists describe an essential contributory cause of prion disease – a process known as ganglioside GM1. This process helps prions convert other proteins into a new mutation of prions.

We know that each mutation becomes more aggressive and lethal. There are likely thousands of mutations floating through the man-made and natural worlds. Prions shed from humans are the deadliest, since humans are at the top of the food chain, which makes us prion collectors, condensers and distributors.

The researchers also traced the infection of prions to an area on the molecule’s structure known as the C terminal domain.

“Our findings explain, at the structural level, the emergence of new human prions and provide a basis for understanding how seemingly subtle differences in misfolded protein structure and modifications affect their transmissibility, cellular targeting, and thus manifestation in humans,” said Safar.

Non-human prions have previously been synthesized, with studies carried out on mice and hamsters, but the research from CWRU is the first to involve an aggressive and “highly destructive” artificial human prion. They made the artificial prion from a human prion protein expressed in E. coli bacteria (yes, you should be concerned about all of the food-borne illnesses. Sewage is getting into the food chain and our water supplies. Sewage is a prion super-highway. If E.coli, listeria and other poisons are making it into grocery stores and restaurants, so are prions).

The results of the study could alter how we think about degenerative disorders. Sincee Parkinson’s and Alzheimer’s disease spread through the brain much like CJD spreads, the researchers hope to develop better treatments for these diseases.

Unfortunately, there is a growing stack of evidence that Alzheimer’s disease is a transmissible disease—prion disease. For example, millions of these people have the severe form of Alzheimer’s disease, which is Creutzfeldt-Jakob disease (CJD). CJD is clearly a prion disease. Prion disease is highly contagious, incurable and fatal. Victims should be quarantined, but they are not.

According to neuroscientists Dr. Laura Manuelidis, at least 25 percent of Alzheimer’s diagnoses are not Alzheimer’s disease. These misdiagnoses are actually CJD, which is further up the prion spectrum. CJD, without dispute, is extremely infectious to caregivers and loved ones, but it has not been declared a reportable disease in the U.S. and many other nations. Millions of cases of deadly CJD are being misdiagnosed as Alzheimer’s disease. Millions of patients and caregivers are being misinformed, misguided and exposed to an aggressive disease. Millions of people with prion disease have exposed us all to their infectious waste thanks to misinformation and mismanagement.

Prions are in the urine, feces, blood, saliva, mucus, skin and cell tissue of all victims–all human byproducts that are washed, dumped, or flushed down sinks and toilets. One can assume that the waste is extra infectious when it comes from funeral homes, nursing homes, hospitals, dental offices, veterinarians, slaughterhouses and some laboratories.

land application sewage sludge and biosolids

Wastewater treatment plants can’t detect or stop prions. Therefore, they ignore them. So does the EPA. So do various other government agencies around the world. Wastewater reclamation and reuse spreads prions back into our world, our watersheds and our food supplies. Applying sewage sludge to open land is insane. It’s time to stop growing our food in this toxic soup of carcinogens, nerve agents and endocrine disruptors. Allowing rains and runoff to rinse these toxins into our rivers, streams, lakes and oceans is taking its toll on public health and marine life. Ironically, this public health disaster began when global leaders realized that dumping sewage in our oceans killed entire underwater ecosystems and spoiled our beaches. Now, we’re being told that sewage sludge should be reclassified as biosolids and sold as fertilizer. Good thinking.

Suffice it to say, prion science is still unfolding. However, we know enough to say that prion pathways and prion diseases are being mismanaged.

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Conference Investigates Prion Diseases

Prion Epidemic Striking Mammals Globally

Editor’s Note: According to Nobel-Prize winner Stanley Prusiner, Alzheimer’s, Parkinson’s Creutzfeldt-Jakob, Chronic Wasting, and Mad Cow disease all are forms of prion disease. One could argue that we have epidemics in Alzheimer’s and Chronic Wasting disease. Those incubating various forms of prion disease are very infectious. We should assume that they all are very contagious and reform prion management policies accordingly around the world.

What does chronic wasting disease – a killer neurological disease in deer, elk, and moose – have in common with human brain disorders, such as Alzheimer’s and Parkinson’s disease?

The diseases are caused by protein misfolding that starts a degenerative chain reaction in the nervous system, ultimately leading to death. In the case of chronic wasting disease (CWD), a distorted protein called a prion triggers the neurodegeneration.

The mysteries and fatal effects of prions, as well as the insights they hold for well-known neurological diseases in people, are the focus of a three-day scientific meeting called “Expanding Prion Horizons” at Colorado State University this week. The Prion Research Center, a CSU Program of Research and Scholarly Excellence, is hosting the conference.

CSU researchers have investigated the puzzling properties of prions for decades, since they first identified CWD in deer in northern Colorado, and this week they will host national and international colleagues to consider new scientific questions related to these rogue proteins. This includes what scientists might learn from prion diseases to better understand protein misfolding disorders in people, including Alzheimer’s, Parkinson’s, Lou Gehrig’s and Huntington’s diseases.

Prions and Alzheimer's disease

Nobel laureate Dr. Stanley Prusiner, director of the Institute for Neurodegenerative Diseases at the University of California – San Francisco, will headline the meeting. His keynote talk, “A Unifying Role for Prions in Neurodegenerative Diseases,” will start at 8 a.m. Thursday at the University Center for the Arts. It is free and open to the public.

“It’s an honor to have Dr. Prusiner visit CSU,” said Sue VandeWoude, associate dean for research in the CSU College of Veterinary Medicine and Biomedical Sciences. “Participation of a scientist of his caliber in this conference highlights the decades-long research focus on prion diseases in Fort Collins, and puts the spotlight on CSU as a leader in this intriguing research area.”

Prusiner, a neurologist and biochemist, won the Nobel Prize in Physiology or Medicine in 1997 for prion research. He is credited with first proposing that misfolded proteins with infectious properties cause the family of degenerative neurological diseases now known as prion diseases, or transmissible spongiform encephalopathies.

Prion diseases include: chronic wasting disease, which affects deer, elk, and moose; bovine spongiform encephalopathy, or mad cow disease; scrapie, which affects sheep; and Creutzfeldt-Jakob disease, the fatal prion disorder seen in humans.

Prusiner labored in the laboratory for years to prove that these degenerative diseases are caused by infectious proteins, not by a virus, as scientists widely believed for many years. The maverick scientist even gave the infectious agents their name: prions, from “proteinaceous infectious particles.”

biosolids land application sewage sludge

These agents, Prusiner showed, can arise spontaneously, can be inherited, can be transmitted like other infectious pathogens (from contamination in food, water, medical and dental devices) and can cause other proteins to change shape. The “prion paradigm,” used to describe the activity of these misfolded proteins, since has formed a basis for better understanding other neurodegenerative diseases that plague people, and has led to Prusiner’s investigation of novel therapies to stop neurodegeneration.

“Dr. Prusiner provides us with a compelling story about the emergence of a new scientific paradigm and the importance of basic scientific research,” said Glenn Telling, director of the CSU Prion Research Center.

Prion investigators at CSU are themselves internationally recognized for their expertise in transmissible spongiform encephalopathies that pose a risk for human and animal health. In fact, CSU scientists first identified CWD as a fatal wasting syndrome in mule deer, and then discovered it is a prion disorder.

chronic wasting disease

CWD “continues to spread with alarming efficiency among wild and captive animals” and continues to demand scientific attention, Telling said. Mad-cow disease prions have clearly caused a new form of prion disease in humans, while there is conflicting scientific evidence about the risks that CWD prions pose to people.

This remains an important issue for CSU prion researchers working in the endemic region, where CWD infection rates reach 15 percent to 20 percent in some wild elk, and deer populations, Telling said. CWD has spread from its epicenter in northern Colorado to at least 20 other states, two Canadian provinces, and South Korea, scientific surveillance has found.

“This is an emerging epidemic,” Telling said. “CWD is the only recognized prion disease in wild animals, which means it’s very difficult to control, and it’s extremely contagious. It’s important that we understand prion diseases so we can better assess risk to public health.”