Detection of the disease-associated form of the prion protein in biological samples. (January 2015)

• Record Type: Journal Article
• Authors: Nicholson, Eric M
• Is Part Of: Bioanalysis. Volume 7:Number 2(2015)
• Page Start: 253
• Page End: 261
• Publication Date: 2015-01
• Subjects: Drugs -- Analysis -- Periodicals; 615.19005
• DOI: 10.4155/bio.14.301
• Languages: English
• ISSNs: 1757-6180

Abstract

Transmissible spongiform encephalopathies (TSEs) are neurodegenerative diseases that occur in a variety of mammals. In TSEs, a chromosomally encoded protein (PrP C ) undergoes a conformational change to the disease-associated form (PrP d ). PrP d is capable of inducing a change in additional molecules of PrP C to the PrP d conformation. TSEs are inevitably fatal and cross-species transmission is known to occur, and there is potential for transmission via blood transfusion and organ transplantation in humans. Thus, there is interest in high-quality diagnostics for both humans and animals. This review summarizes methods of TSE detection currently in use in diagnostic settings and discusses recent advances in PrP d detection that afford substantial enhancements in sensitivity over currently approved methods for use in clinical settings.