title: Prion Strain Diversity.
abstract: Prion diseases affect a wide range of mammal species and are caused by a misfolded self-propagating isoform (PrPSc) of the normal prion protein (PrPC). Distinct strains of prions exist and are operationally defined by differences in a heritable phenotype under controlled experimental transmission conditions. Prion strains can differ in incubation period, clinical signs of disease, tissue tropism, and host range. The mechanism by which a protein-only pathogen can encode strain diversity is only beginning to be understood. The prevailing hypothesis is that prion strain diversity is encoded by strain-specific conformations of PrPSc; however, strain-specific cellular cofactors have been identified in vitro that may also contribute to prion strain diversity. Although much progress has been made on understanding the etiological agent of prion disease, the relationship between the strain-specific properties of PrPScand the resulting phenotype of disease in animals is poorly understood.
authors.affiliation: Department of Medical Microbiology and Immunology, School of Medicine, Creighton University, Omaha, Nebraska 68178.
authors.forename: Jason C
authors.initials: JC
authors.lastname: Bartz
mesh_terms: D000818:Animals; D001921:Brain / Q000473:pathology*; D002417:Cattle; D006801:Humans; D010641:Phenotype; D018620:PrPSc Proteins / Q000737:chemistry* / Q000235:genetics; D017096:Prion Diseases / Q000145:classification*; D011487:Protein Conformation; D012756:Sheep; D013045:Species Specificity
chemical_list: D018620:PrPSc Proteins