Breech-birth prions
Article Abstract:
It has been established that CtmPrP, a transmembrane form of the abnormal plasma-membrane protein PrPSc, could be a neurotoxic molecule common to both the genetic and the acquired forms of prion diseases. This research involved investigating the effect of mutations on the cell-membrane topography and stability of prion protein, PrPC, in vitro and in vivo. The researchers took brain homogenates from a line of transgenic mice that expresses high levels of a hamster CtmPrP. A panel of transgenic mice and hamsters was innoculated with the brain homogenates, and it was found that CtmPrP-associated prion disease is not transmissible.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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Molecular assessment of the potential transmissibilities of BSE and scrapie to humans
Article Abstract:
Fears about the transmission of bovine spongiform encephalopathy (BSE) to man were raised with the emergence of cases of of Creutzfeldt-Jakob disease (CJD), a human transmissible spongiform encephalopathy (TSE) in the UK. Experiments show a link between in vitro conversion efficiencies and and known BSE, sheep scrapie and CJD transmissibilities. An in vitro system was used to assess the possible transmissibility of BSE and scrapie to man, and a limited conversion of human PrP-sen to PrP-res was found. It was concluded that transmission to man following equivalent exposure is finite but low.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1997
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Prion phylogeny revisited
Article Abstract:
The suggestion that the similarity in the amino-acid substitutions in cattle and human prion (PrP) proteins makes humans susceptible to bovine spongiform encephalopathy (BSE) is inaccurate. The susceptibility of sheep to BSE and scrapie is similar although the PrP sequence is identical in all sheep but different from that of cattle. This indicates that sequence similarity has no effect on susceptibility. The computation of all PrP sequences would change the prion phylogenetic tree and increase the probability of similar substitutions having occurred by chance.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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