Prion protein in exosomes: partnering A peptides and driving fibrilization

This Editorial highlights a study by Falker and coworkers in which the authors expanded the notion of how prion protein (PrPC) can be involved with the neurotoxicity promoted by A oligomers, the most toxic component in Alzheimer's Disease. While confirming that PrPC is secreted from cells in exosomes, they showed that at the surface of these vesicles PrPC is capable of binding to dimeric up to pentameric, oligomeric A(42), and A(42) fibrils. In addition, by binding to diverse oligomeric A(42) components, exosomal PrPC accelerated A(42) fibrilization leading to decrease in the neurotoxicity mediated by A(42) as well as A(42) internalization. These data suggest an opportunity to design new therapeutic compounds for Alzheimer's disease. Read the highlighted article Exosomal cellular prion protein drives fibrillization of amyloid beta and counteracts amyloid beta-mediated neurotoxicity' on page88.