Description:  We all produce prion protein. However, the misfolded protein can cause disease including sporadic, genetic, and acquired forms of prion disease; and this disease kills more than 400 individuals in the U.S. each year. Prion disease is universally and often rapidly fatal. Accurately identifying or ruling out prion disease premortem is diagnostically challenging, and until recently, clinical laboratory tests used to aid in the diagnosis of prion disease were generally limited to nonspecific protein markers of neurodegeneration. However, in the last decade, real-time quaking induced conversion (RT-QuIC) had been implemented and adopted worldwide as a novel diagnostic method that has proven to be both sensitive and specific in the detection of human prion disease. This novel method detects the pathogenic prion protein by amplifying and detecting the misfolded conformation in vitro. An overview of prion disease and relevant clinical laboratory tests will be explored.

Bio:  Daniel D. Rhoads, MD, D(ABMM), FCAP, began his laboratory medicine career as a medical laboratory scientist at the Hospital of the University of Pennsylvania. He subsequently moved to Texas and studied bacteriophage therapy, biofilm infections, and chronic wound microbiota before pursuing a doctorate of medicine at Texas Tech Health Sciences Center. He trained in Laboratory Medicine at the University of Pittsburgh Medical Center and trained in Medical Microbiology at the Cleveland Clinic. He recently served for three years as the Clinical Laboratory Director of the National Prion Disease Pathology Surveillance Center where he interpreted more than 10,000 RT-QuIC tests during his tenure. Currently, Dan is the Section Head of Microbiology at the Cleveland Clinic in Cleveland, Ohio. His academic interests include bacteriology antimicrobial resistance, clinical microbiology informatics, and novel diagnostics.