Misfolded cell-surface glycoproteins {Proteinaceous Infectious Particle} {prion}| can be in vertebrates [Prusiner, 1982].
gene
All vertebrates have protease-resistant protein (PrP) genes, whose sequence controls transmissibility.
prion protein
PrP proteins can have normal forms {cellular prion protein} (PrPC), which are in neurons. PdPSc refolds PrPC and makes clumps. PrPC can change into sticky clumps if affected by other prions, especially in B cells and brain.
amyloid
Prion proteins of size 27 to 30 kilodaltons, PrP 27-30, polymerize into amyloid fibrils. Prion-disease amyloid plaques have PrP.
radiation
Prions are more stable than anthrax spores. Irradiation does not end them.
diseases
Prion brain diseases {chronic wasting disease} (CWD) can be in sheep {scrapie}, Papua New Guinea Kore tribeswomen {kuru} {laughing sickness}, people {Creutzfeldt-Jakob disease} (CJD), and cows {spongiform encephalopathy} {bovine spongiform encephalopathy} (BSE) {mad-cow disease}. Prion diseases are sporadically infectious and can inherit.
Scrapie is in sheep and so is ovine neurodegenerative disease. Scrapie PrP has altered cellular PrP.
Chronic Wasting Disease affects deer and elk herds in west USA and Canada.
Mad Cow disease caused 1990s new-variant Creutzfeldt-Jakob disease (nvCJD) outbreak. Europe and Japan screen cattle for BSE.
Inherited CJD is 10% to 15% of human prion-disease cases. Altered cellular PrP causes human Gerstmann-Sträussler-Scheinker syndrome and familial CJD. Typical cases have no sequence changes or chemical differences between normal PrP and disease PrP, but they fold into different shapes. Proteinase K digests normal PrP completely, but aggregated disease PrP resists digestion. Disease PrP prompts normal PrP refolding into disease PrP.
Disease PrP can be protease-sensitive precursors in blood, unlike normal PrP [Safar et al., 1998].
Biological Sciences>Medicine>Disease>Kinds>Protein
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Date Modified: 2022.0224