The focus of the research is to characterize structural differences in human prions causing different disease pathologies. Human prion diseases can have a sporadic, genetic, or infectious origin and are known under a variety of names, for example Creutzfeldt-Jakob disease, Gerstmann-Sträussler-Scheinker syndrome etc.
The sporadic forms, which account for ~90% of cases, have no known origin. They may results from a spontaneous conversion of the cellular prion protein into the infectious state, or stem from a somatic mutation in one of the ~100 billion neurons of the human brain.
The genetic or familial forms are responsible for about 10% of human prion disease cases and are caused by a mutation in the human prion protein gene.
The infectious transmission of human prion diseases is rare (less than 1% of cases) and either based on medical procedures (blood transfusions, dura mater transplants, contaminated human growth hormone etc.) or contaminated food.
We are using a variety of experimental techniques to study the differences between the human prion diseases. We are employing electron microscopy and biophysical techniques to determine structural differences between human prions. Furthermore, we address the question of whether different human prion strains interact with specific cellular proteins and thereby impair cell function