title: Prion seeded conversion and amplification assays.
abstract: The conversion of the normal prion protein (PrP(C)) into its misfolded, aggregation-prone and infectious (prion) isoform is central to the progression of transmissible spongiform encephalopathies (TSEs) or prion diseases. Since the initial development of a cell free PrP conversion reaction, striking progress has been made in the development of much more continuous prion-induced conversion and amplification reactions. These studies have provided major insights into the molecular underpinnings of prion propagation and enabled the development of ultra-sensitive tests for prions and prion disease diagnosis. This chapter will provide an overview of such reactions and the practical and fundamental consequences of their development.
authors.affiliation: Laboratory of Persistent Viral Diseases, Rocky Mountain Laboratories, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Hamilton, MT 59840, USA.
authors.forename: Christina D
authors.initials: CD
authors.lastname: Orrú
authors.forename: Byron
authors.initials: B
authors.lastname: Caughey
mesh_terms: D000818:Animals; D001681:Biological Assay / Q000379:methods*; D035843:Biomedical Research / Q000639:trends; D005821:Genetic Techniques; D006801:Humans; D018621:PrPC Proteins / Q000378:metabolism; D018620:PrPSc Proteins / Q000378:metabolism; D017096:Prion Diseases / Q000378:metabolism*; D011328:Prions / Q000737:chemistry*; D017510:Protein Folding; D011994:Recombinant Proteins / Q000737:chemistry; D013997:Time Factors
chemical_list: D018621:PrPC Proteins; D018620:PrPSc Proteins; D011328:Prions; D011994:Recombinant Proteins