1755 and all that: a historical primer of transmissible spongiform encephalopathy

Brown, Paul; Bradley, R.

doi:10.1136/bmj.317.7174.1688

Cited by 92 publications

(41 citation statements)

References 11 publications

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“…While at the time of discovery it was a new disease in cows, a similar disease in sheep, namely scrapie, has been known for hundreds of years [7,24]. Therefore, scrapie is regarded as the prototype in a group of diseases called TSEs or prion diseases.…”

Section: Introductionmentioning

confidence: 99%

Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

Polak

Zmudzinski

Jacobs³

et al. 2007

Arch Virol

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SummaryThe aim of this study was to analyze molecular features of protease-resistant prion protein (PrP res ) in Western blots of BSE cases diagnosed in Poland with respect to a possible atypical status. Confirmed cases were analyzed by Western blotting with several monoclonal antibodies directed at N-terminal and core epitopes of prion protein (PrP). Most cases showed the classical glycoprofile characterized by the dominance of the di-over the monoglycosylated PrP res band, yielding di-=mono-ratios well above 2 and by reactivity with antibodies having their epitopes in bovine PrP region 110-242 (Ctype cases). Surprisingly, seven cases of BSE were atypical. Six were classified as L-type based on a slightly lower molecular mass (M r ) of the nonglycosylated band with respect to C-types and a conspicuously low di-=mono-ratio of glycosylated PrP res bands approaching unity. One case was classified as H-type because of a higher M r of PrP res bands on the blot when compared with C-type cases. A characteristic epitope of H-type PrP res occurred in the 101-110 region of PrP for which only antibody 12B2 had a sufficient affinity. The occurrence of atypical cases only in animals 9 years of age and older raises questions about the mechanisms of prion diseases and the origin of BSE.

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Section: Introductionmentioning

confidence: 99%

Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

Polak

Zmudzinski

Jacobs³

et al. 2007

Arch Virol

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“…PrP C is a ubiquitously expressed sialoglycoprotein normally attached to the outer leaflet of the plasma membrane via a glycosylphosphatidyl-inositol (GPI) anchor. Although the primary function of PrP C remains obscure, evidence suggests roles in copper regulation (4,28), antioxidant activity (3), and intracellular signaling (32). During normal expression, PrP C is translocated into the endoplasmic reticulum (ER) lumen, where it undergoes several posttranslational modifications, including the addition of the GPI anchor, disulfide bond formation, and core glycosylation at two asparagines, before it passes to the Golgi apparatus for further sugar modification and sialation en route to the plasmalemma (7).…”

mentioning

confidence: 99%

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation

Norstrom

Ciaccio²,

Rassbach³

et al. 2007

J Virol

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“…Transmissible spongiform encephalopathies (TSE) are fatal neurological diseases that occur in farmed and free-ranging animals, including scrapie in sheep and goats, transmissible mink encephalopathy, bovine spongiform encephalopathy in cattle, and chronic wasting disease in deer and elk (4,52). Sheep scrapie is the prototypic animal TSE and has been investigated for many years in the form of rodent-adapted isolates that have given rise to distinct stable laboratory strains (6).…”

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confidence: 99%

Distinct Stability States of Disease-Associated Human Prion Protein Identified by Conformation-Dependent Immunoassay

Choi

Peden

Gröner

et al. 2010

J Virol

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The phenotypic and strain-related properties of human prion diseases are, according to the prion hypothesis, proposed to reside in the physicochemical properties of the conformationally altered, disease-associated isoform of the prion protein (PrP Sc ), which accumulates in the brains of patients suffering from CreutzfeldtJakob disease and related conditions, such as Gerstmann-Straussler-Scheinker disease. Molecular strain typing of human prion diseases has focused extensively on differences in the fragment size and glycosylation site occupancy of the protease-resistant prion protein (PrP res ) in conjunction with the presence of mutations and polymorphisms in the prion protein gene (PRNP). Here we report the results of employing an alternative strategy that specifically addresses the conformational stability of PrP Sc and that has been used previously to characterize animal prion strains transmitted to rodents. The results show that there are at least two distinct conformation stability states in human prion diseases, neither of which appears to correlate fully with the PrP res type, as judged by fragment size or glycosylation, the PRNP codon 129 status, or the presence or absence of mutations in PRNP. These results suggest that conformational stability represents a further dimension to a complete description of potentially phenotype-related properties of PrP Sc in human prion diseases.

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1755 and all that: a historical primer of transmissible spongiform encephalopathy

Cited by 92 publications

References 11 publications

Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

Atypical status of bovine spongiform encephalopathy in Poland: a molecular typing study

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation

Distinct Stability States of Disease-Associated Human Prion Protein Identified by Conformation-Dependent Immunoassay

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