Disease-associated prion protein in the dental tissue of mice infected with scrapie

H Okada1, M Sakurai, T Yokoyama

  • 1Prion Disease Research Center, National Institute of Animal Health, Tsukuba, Ibaraki, Japan. okadahi@affrc.go.jp

Insights

Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases. This study found disease-associated prion protein (PrP(Sc)) in mouse dental tissues, suggesting a potential route for horizontal disease transmission.

Area of Science:

  • Neuroscience
  • Pathology
  • Veterinary Medicine

Background:

  • Transmissible spongiform encephalopathies (TSEs) are fatal neurodegenerative diseases affecting humans and animals.
  • Prion diseases are characterized by the accumulation of abnormal prion protein (PrP(Sc)).

Purpose of the Study:

  • To investigate the presence and potential role of disease-associated prion protein (PrP(Sc)) in dental tissues during scrapie infection.
  • To explore the pathway of PrP(Sc) spread from the brain to dental tissues.

Main Methods:

  • Immunohistochemistry was used to detect PrP(Sc) in the epithelial cell rests of Malassez (ERM) in mice infected with ME7 scrapie.
  • Mouse bioassay was performed on scrapie-infected dental tissue to determine infectivity.

Main Results:

  • Disease-associated prion protein (PrP(Sc)) was detected immunohistochemically in the ERM of experimentally infected mice.
  • Mouse bioassays of dental tissue showed prolonged incubation periods compared to brain tissue.
  • These findings suggest PrP(Sc) can spread from the brain to ERM via cranial nerves.

Conclusions:

  • The epithelial cell rests of Malassez in dental tissues harbor PrP(Sc) following scrapie infection.
  • Dental tissue may serve as a potential reservoir for the horizontal transmission of TSEs.
  • PrP(Sc) likely spreads from the brain to dental tissues along neural pathways.