Abstract
Prion Diseases and Feline Spongiform Encephalopathy•First Described: Feline spongiform encephalopathy was first recognized in 1990, but prion diseases of sheep and goats have been recognized since the 1700s and 1800s.•Cause: Prions are small infectious agents that are resistant to inactivation by heat, formalin, glutaraldehyde, alcohol, and radiation. Infectivity is associated with a host-encoded protein, the prion protein (PrP). The mechanism of transmissible spongiform encephalopathy (TSE) involves a misfolding of the normal prion protein (PrPc) to a new heat-resistant protein.•Affected Hosts: Cats, humans, and a variety of other mammalian species.•Geographic Distribution: Primarily Europe, but cases have occurred sporadically worldwide.•Mode of transmission: The TSEs are transmissible to other animals, at least under experimental conditions. Routes of natural transmission of TSEs involve oral ingestion, skin scarification, or congenital transmission. For example, scrapie has been consistently found in the placentas of ewes. Infection has spread iatrogenically through contaminated biologic products and likely through other veterinary procedures or feeding practices.•Major Clinical Signs: Adult cats, slowly progressive neurologic signs, behavioral changes, gait abnormalities, hypersensitivity.•Differential Diagnoses: Degenerative diseases, neoplasia, other infectious and inflammatory diseases of the CNS.•Human Health Significance: During the outbreak of bovine spongiform encephalopathy (BSE) in the United Kingdom, a new variant of Creutzfeldt-Jakob disease (vCJD) occurred in humans. The disease has also been reported in other countries. vCJD affected primarily young adults and was suspected of being caused by ingestion of contaminated cattle products. Not all humans are equally susceptible to the development of spongiform encephalopathy. Transmission of the agent through blood transfusions or organ donation remains a concern.
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