Clinical Trials Expanding For PRN100
Neurodegenerative disease is the fastest-growing cause of death on earth. Unfortunately, there isn’t a cure, but a special form of immunotherapy continues to offer hope.
Preclinical studies have demonstrated that monoclonal antibodies are effective against various forms of prion disease, which includes Alzheimer’s disease, Parkinson’s disease, Creutzfeldt-Jakob disease (CJD), ALS and Huntington’s disease.
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. Today, neurodegenerative disease is killing teenagers.
Prions also cause scrapie in sheep, bovine spongiform encephalopathy in cattle (mad cow disease), and chronic wasting disease in cervids—deer, elk, moose and reindeer. It appears that all mammals are vulnerable. It’s more accurate and constructive to refer to the multiple forms as prion disease. There is no species barrier. There are thousands of mutations involved in the prion pandemic.
Prions are a deadly form of protein that accumulates in the bodies and brains of victims. Prions migrate, mutate, multiply and kill with unparalleled efficiency.
The clinical name for prion disease is transmissible spongiform encephalopathy (TSE). As the name implies, TSEs are transmissible because of the unstoppable prion protein. The key is to avoid prion disease.
A variety of factors can trigger neurodegenerative disease, including genetics, head trauma and high cholesterol. Today, however, the greatest factor behind the explosive growth is prion contamination in our food, water, health systems, and beyond.
The immune system recognizes foreign proteins as alien to the body. In response, the body produces specific antibodies to fight that infection. However, since prions are formed from the body’s own proteins, the immune system doesn’t produce lifesaving antibodies to stop them.
Once a person is infected, targeted nutrition offers the best hope for treatment. However, monoclonal antibody therapy shows a remarkable ability to purge prion proteins from the body and brain. PRN100 is an antibody specifically designed to bind to normal prion proteins. The intent is to prevent normal prions from being infected by pathogenic prions, which will hopefully stop the deadly prion infection. In theory, the process stimulates the patient’s immune system to join the battle. The treatment seems to slow disease progression, but it is unknown whether there is any hope for a cure.
Researchers treated six patients who had CJD with PRN100. Patients were treated intravenously with PRN100 every two weeks. Patients were treated for 7–260 days. Repeated dosing was well tolerated. No significant adverse reactions were seen. All patients showed progressive neurological decline on serial assessments with the MRC Scales.
“This is the first time a drug specifically designed to treat CJD has been used in humans and the results are very encouraging,” said Professor John Collinge, director of the MRC Prion Unit at UCL, who led the development of the PRN100 treatment. “This is an important step forward in targeting prion infections. The drug may have the potential to prevent the onset of symptoms in people at risk of prion disease due to genetic mutations or accidental prion exposure. It could contribute to the development of therapies for more common dementias, including Alzheimer’s disease.”
The treatment appeared to be safe and reached encouraging CSF and brain tissue concentrations. These findings justify the need for clinical trials in patients with CJD, Alzheimer’s disease and Parkinson’s disease.
