London.– Prions cause neurodegenerative diseases in humans and animals like cows, sheep, or deer. In most cases, humans or animals get sick sporadically, when, for unknown reasons, normal proteins in the brain called PrPc change to harmful prions (called PrPSc).  

The PrPSc proteins then cause severe degeneration of the brain that kills the victims within a matter of months. There are no cures or therapies for prion diseases. The most common human prion disease is sporadic Creutzfeld-Jacob Disease, or sCJD. Scientists still understand little about why and how in some cases normal proteins change to prions and destroy the brain.  

All patients die, most of them within a few months, but there are differences between individual cases. The hope is that understanding the differences between individual cases might eventually provide some insight into the causes of the disease and suggest ways to treat it.  

To catalogue and examine those differences, it is important to come up with standard assays that allow meaningful comparisons. Markus Glatzel (Hamburg University) and colleagues have developed such an assay.  

Applying it to 50 postmortem samples from patients with sCJD reveals substantial differences in molecular pathology, suggesting that this approach could indeed help to understand this mysterious and devastating disease.