Deposition patterns of disease-associated prion protein in captive mule deer brains with chronic wasting disease.
Chronic wasting disease (CWD) is a transmissible spongiform encephalopathy (TSE) in captive and free-ranging cervids in the USA; its origin is obscure. Archival formalin-fixed and paraffin-embedded specimens of 16 captive mule deer brains with CWD were analyzed using immunocytochemistry for the disease-associated prion protein (PrP). The most prominent pattern of PrP deposition were plaque-like structures, a substantial proportion of which were florid plaques surrounded by a rim of spongiform vacuoles. The percentage of florid plaques was highly variable according to region, ranging from 0% to 52.7%. The highest percentage was observed in the medulla and basal ganglia, the lowest in the cerebral cortex. Only three brains contained no florid plaques. There were also punctate synaptic-type and perivascular deposits, particularly in areas of severe spongiform change, and subpial and subependymal plaque-like deposits, whereas cerebellar involvement was mild. Thus, CWD brain pathology prominently features florid PrP plaques, as does variant Creutzfeldt-Jakob disease (vCJD), but differs in other characteristics from vCJD.
Liberski
P P
PP
Institute of Neurology, University of Vienna, Wien, Austria.
Guiroy
D C
DC
Williams
E S
ES
Walis
A
A
Budka
H
H
D000595:Amino Acid Sequence; D000818:Animals; D001921:Brain / Q000473:pathology*; D003670:Deer; D006801:Humans; D008969:Molecular Sequence Data; D017096:Prion Diseases / Q000662:veterinary*; D011328:Prions / Q000032:analysis*
D011328:Prions