Prion Disease

Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing deadly prions and prion disease. President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research.

Alzheimer’s disease (AD) is the most common neurodegenerative disease in humans and will pose a considerable challenge to healthcare systems in the coming years,” Prusiner said. “Aggregation of the β-amyloid (Aβ) peptide within the brain is thought to be an initiating event in AD pathogenesis. Many recent studies in transgenic mice have provided evidence that Aβ aggregates become self-propagating (infectious) during disease, leading to a cascade of protein aggregation in the brain, which may underlie the progressive nature of AD. The ability to self-propagate and the existence of distinct strains reveals that Aβ aggregates exhibit many properties indistinguishable from those of prions composed of PrPSc proteins. The evidence that Aβ can become a prion during disease, Aβ prions may be important for understanding the pathobiology of AD.”

prion disease

In June 2012, Prusiner confirmed that Alzheimer’s disease, Parkinson’s disease, Huntington’s and even ALS are prion diseases. Other prion diseases include Creutzfeldt-Jakob disease (CJD) in people, mad cow disease in livestock and chronic wasting disease (CWD) in wildlife. The variations in disease progression could be due to genetics in the patients or mutations in the prion, not different diseases entirely.

The scientific name for prion disease is Transmissible Spongiform Encephalopathy (TSE). The operative word is “transmissible.”

“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.”

Additional research has determined that the prion pathogen spreads through feces, saliva, blood, mucus, 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.

prions disease and Alzheimer's disease and Creutzfeldt-Jakob disease

The urine and sewage connection helps explain why the global epidemic is exploding. More than 50 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 sludge and wastewater–and that there is 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.

land application sewage sludge and biosolids

Read More About The Cause and Spread Of Alzheimer’s Disease.

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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.

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