Prions
Open Access
- 1 January 2011
- journal article
- review article
- Published by Cold Spring Harbor Laboratory in Cold Spring Harbor Perspectives in Biology
- Vol. 3 (1), a006833
- https://doi.org/10.1101/cshperspect.a006833
Abstract
The discovery of infectious proteins, denoted prions, was unexpected. After much debate over the chemical basis of heredity, resolution of this issue began with the discovery that DNA, not protein, from pneumococcus was capable of genetically transforming bacteria ( Avery et al. 1944). Four decades later, the discovery that a protein could mimic viral and bacterial pathogens with respect to the transmission of some nervous system diseases ( Prusiner 1982) met with great resistance. Overwhelming evidence now shows that Creutzfeldt–Jakob disease (CJD) and related disorders are caused by prions. The prion diseases are characterized by neurodegeneration and lethality. In mammals, prions reproduce by recruiting the normal, cellular isoform of the prion protein (PrPC) and stimulating its conversion into the disease-causing isoform (PrPSc). PrPC and PrPSc have distinct conformations: PrPC is rich in α-helical content and has little β-sheet structure, whereas PrPSc has less α-helical content and is rich in β-sheet structure ( Pan et al. 1993). The conformational conversion of PrPC to PrPSc is the fundamental event underlying prion diseases. In this article, we provide an introduction to prions and the diseases they cause.Keywords
This publication has 96 references indexed in Scilit:
- Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion DiversityScience, 1996
- Rescue of neurophysiological phenotype seen in PrP null mice by transgene encoding human prion proteinNature Genetics, 1995
- Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteinsCell, 1994
- Segregation of a missense mutation in the amyloid precursor protein gene with familial Alzheimer's diseaseNature, 1991
- Scrapie and cellular prion proteins differ in their kinetics of synthesis and topology in cultured cells.The Journal of cell biology, 1990
- Pro→Leu change at position 102 of prinon protein is the most common but not the sole mutation related to Gerstmann-Sträussler syndromeBiochemical and Biophysical Research Communications, 1989
- Fatal Familial Insomnia and Dysautonomia with Selective Degeneration of Thalamic NucleiThe New England Journal of Medicine, 1986
- Creutzfeldt–Jakob Disease in a Young Adult with Idiopathic HypopituitarismThe New England Journal of Medicine, 1985
- Alzheimer's disease: Initial report of the purification and characterization of a novel cerebrovascular amyloid proteinBiochemical and Biophysical Research Communications, 1984
- Some Speculations about Prions, Amyloid, and Alzheimer's DiseaseThe New England Journal of Medicine, 1984