Creutzfeldt-Jakob Test Available
An Israeli hospital has become the first in the country to introduce a new test to detect Creutzfeldt-Jakob disease (CJD)—a rare brain disorder caused by an infectious protein called a prion.
In addition to CJD, prion disease includes Alzheimer’s disease, amyotrophic lateral sclerosis (ALS), chronic traumatic encephalopathy (CTE), Gerstmann-Straussler-Scheinker disease (GSS), Huntington’s disease, Parkinson’s disease and others. Many of these diseases are related in terms of cause and pathology. The biggest difference between most of the different diseases is the region of the brain that’s under attack. Most forms of neurodegenerative disease will eventually spread throughout the brain, which increases the range of symptoms.
Prions are a deadly and unstoppable form of protein that migrates, mutates, multiplies and kills with unparalleled efficiency. Prions were first discovered in the late 1980s as a protein-containing biological agent that replicates itself in living cells without nucleic acid. Prions are not alive, which means that they can’t be killed. Neutralizing them is virtually impossible. With each mutation, they become deadlier and more resistant.
A variety of factors can trigger neurodegenerative disease, including genetics, head trauma and poor nutrition. Today, however, the greatest factor behind the explosive growth is a neurotoxin that is spreading through our food, water, health systems and beyond.
Abnormal protein deposits spread in the brain, causing widespread damage that progresses rapidly. Symptoms include loss of intellect and memory, slurred speech and personality changes.
The disease is incurable and usually kills the sufferer within a year of onset. But diagnosis is considered important, as it avoids subjecting patients to often-painful treatments that fit other degenerative diseases but not CJD, giving them false hope, and prompts relatives who are at genetic risk to take preventative steps like screening their embryos.
CJD is disproportionately found among Jews of Libyan and Tunisian origin. It is estimated that there are thousands of carriers of the CJD-causing E200K mutation living in Israel, and children with just one carrier-parent can develop the incurable disease. A small minority of children of carriers develop the fatal disease.
Diagnosis is complex, often relying on a combination of tests. Brain biopsies aren’t used on living patients because of the contagious nature of the disease and even an MRI scan is not fully conclusive.
And while people whose heritage raises the risk of being a carrier are encouraged to screen, many don’t. When somebody develops CJD but the family never learns the identity of their disease, family members fail to learn they are at risk themselves, and that they have the option of taking measures to screen embryos of their offspring.
Tel Aviv Sourasky Medical Center has now become one of a dozen hospitals internationally to run a test that gives high-accuracy diagnosis based on analysis of spinal fluid. It joins a few hospitals in the US, but is the first in Israel. “This method is the world’s first standalone test to give diagnoses of CJD with very high accuracy — sensitivity of 92 percent,” said Dr. Yifat Alkalai, director of Sourasky’s Clinical Immunology Laboratory.
She expects that her lab will now analyze hundreds of samples per year, using the method that was developed in Japan 11 years ago, but which hasn’t become widely used due to the high level of expertise needed to put it into practice.
As CJD is characterized by specific interactions between prions, testing can be carried out by observing a patient’s prions interacting with prions from another source. The real-time quaking-induced conversion (RT-QUIC) technique. The prions are observed in lab conditions for five days, and certain patterns of interaction, which mimic how the prions would behave on the brain, confirm CJD.
Dr. Atarashi and his colleagues developed the RT-QUIC assay. Quaking-induced refers to in vitro shaking, which researchers believe accelerates the reactions to produce results quickly. Atarashi developed the RT-QUIC assay as a researcher at the National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, in Montana. In 2008, his team successfully used it to screen cerebrospinal fluid taken from prion-infected hamsters.
CJD is a prion disease, in which a common protein known as a prion becomes an infectious variant. Prions cause fatal neurodegenerative disease in humans and other mammals by converting the cellular version of prion protein into a toxic form that erodes the brain and body. Prion disease often is described as a wasting disease that causes a loss of body mass and brain mass.
Since prion disease generates infectious waste, those infected are contagious—which is why the clinical term for the disease is transmissible spongiform encephalopathies (TSE). Alzheimer’s disease, Parkinson’s disease, ALS, mad cow disease, chronic wasting disease and other forms of neurodegenerative disease are better known as TSE.When we connect these dots, it’s easier to see several patterns emerging regarding the truth and public health. The connection between the rapid spread of TSE is right under our nose.
Byron Caughey, chief of prion/TSE research at the Rocky Mountain lab and a co-author of the two hamster studies, is encouraged by the application of the assay to human cerebrospinal fluid samples. “Of course it will also be important to detect prion diseases in other species, but human diagnosis is of pre-eminent importance,” Caughey says.
“The earlier you’re able to detect the presence of an infection in humans or animals, the more chance you have of preventing transmission to others and treating the disease in those who are infected,” Caughey says.
Most hospitals, neurologists, surgeons, coroners and even morticians are aware of the prion threat. Unfortunately, family members and caregivers are not being warned. Since deadly prions spread through the bodily fluids and tissue of those carrying prion disease (milk, blood, saliva, mucus, urine, feces, tissue and skin), that seems to be a problem. Prions shed from infected humans are highly transmissible.
Prion disease has killed millions of people around the world over the past century. It’s impacting more people and more families than ever today. It’s also killing livestock, wildlife and sea mammals. The connection is undeniable. Wastewater management, industrial agriculture and modern medicine are fueling the flames of this public health disaster.
Governments and industry are working diligently to keep prion disease off the public radar. The epidemic will persist. A cure does not exist. It’s virtually impossible to sterilize anything exposed to a person with prion disease. Hospital systems are now on high alert after several cases of prion exposure. Ignoring the truth about prions on a broader scale is making the pandemic worse. Since prion disease is a transmissible disease, prion contamination via bodily fluids and tissue is a public health threat. Food and water supplies are at risk. Unfortunately, prion disease is being grossly mismanaged around the world in people, wildlife and livestock.
Until recently, few have considered the possibility that Alzheimer’s disease is a transmissible disease.
This denial and misinformation has been fueling a public health crisis around the world for years.
Dr. Stanley Prusiner, an American neuroscientist from the University of California at San Francisco, earned a Nobel Prize in 1997 for discovering and characterizing prions and prion disease. President Obama awarded Prusiner the National Medal of Science in 2010 to recognize the importance of his research. Important reforms to policies to protect public health, however, have been elusive. Dr. Prusiner’s most recent study confirms that Alzheimer’s disease is a prion disease–also known as transmissible spongiform encephalopathy (TSEs). Once again, it demands reform on many levels to protect public health.
Learn more about Dr. Stanley Prusiner and the Nobel Prize for prion science and prion disease.
