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Case Western Reserve University School of Medicine researchers have synthesized the first artificial human prion, a dramatic development in efforts to combat a devastating form of brain disease that has so far eluded treatment and a cure. Prions are proteins that have folded incorrectly. They can bind to neighboring normal proteins in the brain, triggering a domino effect that causes microscopic holes, turning brains into sponge, resulting in progressive deterioration, dementia, and certain death.
There are numerous types of prion diseases in humans; the most common being Creutzfeldt-Jakob disease (CJD). Why and how human prion mis-folding occurs has been a mystery that the Case Western Reserve investigative team may have solved with its new findings.
Generate synthetic human prions in a test tube will enable researchers to have better 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.
They also discovered an essential cofactor known as Ganglioside GM1—a cell molecule which modulates cell-to-cell signaling in triggering infectious replication and transmission of prion-based disease. This finding raises the hope for new therapeutic strategies using analog medications with inhibitory or blocking effect on human prion replication.
They also demonstrated that the replication rate, infectivity, and targeting of specific brain structures by synthetic and naturally occurring prions is determined not by the presence of mis-folded prions per se but by particular variations and modifications in the molecule’s structure—specifically in an area known as the C terminal domain which control the growth rate of infectious prions.
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