For years, scientists have known the mechanisms underlying normal, as well as the disease-causing (pathogenic) versions, of prions. But according to a recent article published in Sci-Tech Daily, no one knew how the normal protein version, which is located on the surface of many cells, transforms into the pathogenic version.
Prion Diseases are a Public Health Concern
Prion diseases, in a manner similar to viruses or bacteria, can spread from animals to people, or they may be transmitted among humans through blood transfusions, hormone injections, or surgery with contaminated instruments.
Most noteworthy is that prions are misfolded proteins that can transmit their abnormal shape onto normal versions of the same protein. Diseases associated with protein misfolding are Lewy body dementia, Parkinson’s, and Alzheimer’s diseases.
Thus far, there have been no therapies available to treat these often fatal diseases.
However, in a recent first-in-human study, patients with Creutzfeldt-Jakob’s disorder that is known to be the most common prion disease in humans, have been treated with anti-prion antibodies.
About the Discovery
The recent discovery by researchers from the Zurich University and London’s Imperial College identified the critical missing step during which normal prions change into pathogenic forms.
The researchers then went a step further and are now able to block the prions before they can transition. This discovery may lead to the development of new drugs that can combat fatal brain diseases.
About Prion Diseases
Prion diseases are caused by an infectious agent called a prion. The prion manifests from a misfolded prion protein.
Brain damage occurs when normal prion becomes abnormal and forms clumps on the brain causing personality changes, and problems with memory and movement. Prion diseases may take decades to surface, but when they do they progress rapidly and are fatal.
This is the first time scientists have isolated an abnormal (mutant) prion protein. The protein can be found in individuals who have inherited prion disorders. The scientists used nuclear magnetic resonance spectroscopy to identify how the intermediate step was structured. Then they were able to observe the molecular mechanism in real-time while the prion was misfolding.
According to the researchers, the study has provided new insights into what causes prions to become infectious.