Researchers at the University of Alberta, led by Dr. Holger Wille, have developed a novel strategy for the creation of vaccines and specific antigens for prion protein diseases. Applying a structure-based, rationally designed approach, the researchers modified a non-infectious protein scaffold to mimic both the structural elements and surface markers that are uniquely characteristic of the misfolded prion protein (PrPSc). By more accurately presenting conserved epitopes from PrPSc, these vaccines are expected to stimulate a more effective immune response against it. When used to immunize animals, the resulting antiserum contained high quantities of antibodies that very specifically recognize PrPSc and high-specificity monoclonal anti-PrPSc antibodies have been generated, as verified by ELISA assays. In vivo animal experiments to evaluate the efficacy of the vaccines are currently underway.
Diseases linked to accumulation and aggregation of misfolded prion protein include scrapie in sheep and goats, chronic wasting disease in deer and elk, bovine spongiform encephalopathy in cattle, and Creutzfeldt-Jakob disease in humans. Most attempts to create prophylactic vaccines for prion diseases have generally relied on full-length proteins or short peptides derived from the non-disease related form of the prion protein. In contrast to the present technology, these prior vaccines are unlikely to adopt an appropriate three-dimensional structure when administered in vivo and to this point have offered limited protection against disease. The present technology aims to overcome such barriers. The monoclonal anti-PrPSc antibodies described herein can selectively detect the misfolded PrPSc in animal tissues without requiring any pretreatment. These anti-PrPSc antibodies have the potential to simplify the high-throughput post-mortem diagnostics for prion diseases that are already common in the food industry.
Technology Management Group
TEC Edmonton – University of Alberta