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Human transmissible spongiform encephalopathies: historic view.

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Human transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases. Research has shown these conditions, including Creutzfeldt-Jakob disease, are transmissible and linked to abnormal prion proteins.

Keywords:
Creutzfeldt–Jakob diseaseGerstmann–Sträussler–Scheinker syndromefatal familial insomniahistoric viewkuruprionscrapietransmissible spongiform encephalopathy

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Area of Science:

  • Neuroscience
  • Infectious Diseases
  • Protein Chemistry

Background:

  • Human transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases.
  • Early research in 1959 noted similarities between sheep scrapie and human kuru.
  • Subsequent studies linked kuru and Creutzfeldt-Jakob disease (CJD) to transmissible agents.

Observation:

  • Kuru, Creutzfeldt-Jakob disease (CJD), Gerstmann-Sträussler-Scheinker syndrome, and fatal familial insomnia were transmitted to non-human primates and other animals.
  • Iatrogenic CJD was transmitted via contaminated human pituitary-derived hormones and tissue grafts.
  • A new variant of CJD (vCJD) emerged, linked to bovine spongiform encephalopathy and spread through blood transfusions.

Findings:

  • The scrapie agent exhibited resistance to inactivation, suggesting an unconventional pathogen.
  • Stanley Prusiner identified misfolded prion proteins in TSE-affected tissues, proposing the prion hypothesis.
  • Prion protein expression is essential for TSE infection, and mutations correlate with familial TSEs.

Implications:

  • The prion hypothesis provides a framework for understanding TSE pathogenesis and diagnosis.
  • Further research is needed to explore potential environmental sources for sporadic TSE cases.
  • Understanding prion diseases is crucial for public health, particularly concerning iatrogenic and foodborne transmission.