Abstract

Prion diseases are a group of neurodegenerative, transmissible, and fatal disorders that affect several animal species. They are characterized by the conformational conversion of the cellular prion protein (PrPC) into the pathological prion protein (PrPSc). In 2016, chronic wasting disease (CWD) gained great importance at European level due to the first disease detection in a wild reindeer (Rangifer tarandus) in Norway. The subsequent intensive CWD surveillance launched in cervids resulted in the detection of CWD in moose (Alces alces), with 11 cases in Norway, 3 in Finland and 4 in Sweden. These moose cases differ considerably from CWD cases in North American and reindeer in Norway, as PrPSc was detectable in the brain but not in lymphoid tissues. These facts suggest the occurrence of a new type of CWD. Here, we show some immunohistochemical features that are clearly different from CWD cases in North American and Norwegian reindeer. Further, the different types of PrPSc deposits found among moose demonstrate strong variations between the cases, supporting the postulation that these cases could carry multiple strains of CWD.

Keywords

CWD; moose; prion disease; chronic wasting disease; prions; transmissible spongiform encephalopathy; Norway; Finland; Sweden

Published in

Veterinary Research
2023, Volume: 54, number: 1, article number: 74
Publisher: BMC

SLU Authors

• Gavier Widén, Dolores

  • Department of Animal Biosciences, Swedish University of Agricultural Sciences
    
  • National Veterinary Institute (SVA)

UKÄ Subject classification

Pathobiology


Publication identifier

DOI: https://doi.org/10.1186/s13567-023-01208-3

Permanent link to this page (URI)

https://res.slu.se/id/publ/126557