title: The many shades of prion strain adaptation.
abstract: In several recent studies transmissible prion disease was induced in animals by inoculation with recombinant prion protein amyloid fibrils produced in vitro. Serial transmission of amyloid fibrils gave rise to a new class of prion strains of synthetic origin. Gradual transformation of disease phenotypes and PrP(Sc) properties was observed during serial transmission of synthetic prions, a process that resembled the phenomenon of prion strain adaptation. The current article discusses the remarkable parallels between phenomena of prion strain adaptation that accompanies cross-species transmission and the evolution of synthetic prions occurring within the same host. Two alternative mechanisms underlying prion strain adaptation and synthetic strain evolution are discussed. The current article highlights the complexity of the prion transmission barrier and strain adaptation and proposes that the phenomenon of prion adaptation is more common than previously thought.
authors: Center for Biomedical Engineering and Technology; Department of Anatomy and Neurobiology; University of Maryland School of Medicine; Baltimore, MD USA.
authors: Ilia V
authors: IV
authors: Baskakov
mesh_terms: D000222:Adaptation, Physiological; D006801:Humans; D019636:Neurodegenerative Diseases / Q000209:etiology; D011328:Prions / Q000145:classification / Q000502:physiology*; D013045:Species Specificity
chemical_list: D011328:Prions
keywords: deformed templating mechanism; neurodegenerative diseases; prion diseases; prion protein; species barrier; strain adaptation; synthetic prions