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Unaltered susceptibility to BSE in transgenic mice expressing human prion protein

J Collinge1, M S Palmer, K C Sidle

  • 1Department of Biochemistry and Molecular Genetics, Imperial College School of Medicine at St Mary's, London, UK.

Nature
|December 21, 1995
PubMed

Insights

Transmissible neurodegenerative diseases, known as prion diseases, can cross species barriers. Transgenic mice expressing human prion protein (PrP) did not shorten incubation periods for bovine spongiform encephalopathy (BSE) or produce human PrP(Sc).

Area of Science:

  • Neurodegenerative diseases
  • Prion biology
  • Transmissible spongiform encephalopathies

Background:

  • Prion diseases are fatal neurodegenerative conditions affecting humans and animals.
  • Prions are misfolded proteins (PrPSc) resistant to degradation.
  • A species barrier typically limits prion disease transmission between different species.

Purpose of the Study:

  • To investigate the potential for bovine spongiform encephalopathy (BSE) transmission to humans.
  • To develop a transgenic mouse model for studying the human prion disease species barrier.

Main Methods:

  • Transgenic mice expressing human prion protein (PrP) were challenged with BSE prions.
  • Incubation periods and prion protein (PrP) formation in challenged mice were analyzed.

Main Results:

  • Transgenic mice expressing human PrP did not exhibit shortened incubation periods when challenged with BSE.
  • Only mouse PrPSc was detected in the transgenic mice, not human PrPSc, following BSE challenge.

Conclusions:

  • The study suggests that human PrP expression in mice does not facilitate BSE prion replication or transmission.
  • These findings contribute to understanding the species barrier for BSE transmission to humans.

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