BMC Research Notes (Dec 2021)

RT-QuIC detection of pathological prion protein in subclinical goats following experimental oral transmission of L-type BSE

  • Alessandra Favole,
  • Maria Mazza,
  • Antonio D’Angelo,
  • Guerino Lombardi,
  • Claudia Palmitessa,
  • Luana Dell’Atti,
  • Giulia Cagnotti,
  • Elena Berrone,
  • Marina Gallo,
  • Tiziana Avanzato,
  • Erika Messana,
  • Loretta Masoero,
  • Pier Luigi Acutis,
  • Daniela Meloni,
  • Franco Cardone,
  • Maria Caramelli,
  • Cristina Casalone,
  • Cristiano Corona

DOI
https://doi.org/10.1186/s13104-021-05859-3
Journal volume & issue
Vol. 14, no. 1
pp. 1 – 6

Abstract

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Abstract Objective The spread of bovine spongiform encephalopathy (BSE) agent to small ruminants is still a major issue in the surveillance of transmissible spongiform encephalopathies (TSEs). L-type bovine spongiform encephalopathy (L-BSE) is an atypical form of BSE with an unknown zoonotic potential that is transmissible to cattle and small ruminants. Our current knowledge of bovine atypical prion strains in sheep and goat relies only on experimental transmission studies by intracranial inoculation. To assess oral susceptibility of goats to L-BSE, we orally inoculated five goats with cattle L-BSE brain homogenates and investigated pathogenic prion protein (PrPsc) distribution by an ultrasensitive in vitro conversion assay known as Real-Time Quaking Induced Conversion (RT-QuIC). Results Despite a prolonged observation period of 80 months, all these animals and the uninfected controls did not develop clinical signs referable to TSEs and tested negative by standard diagnostics. Otherwise, RT-QuIC analysis showed seeding activity in five out of five examined brain samples. PrPsc accumulation was also detected in spinal cord and lymphoreticular system. These results indicate that caprine species are susceptible to L-BSE by oral transmission and that ultrasensitive prion tests deserve consideration to improve the potential of current surveillance systems against otherwise undetectable forms of animal prion infections.

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