Abstract
Atypical bovine spongiform encephalopathy (BSE) has recently been identified in Europe, North America, and Japan. It is classified as H-type and L-type BSE according to the molecular mass of the disease-associated prion protein (PrPSc). To investigate the topographical distribution and deposition patterns of immunolabeled PrPSc, H-type BSE isolate was inoculated intracerebrally into cattle. H-type BSE was successfully transmitted to 3 calves, with incubation periods between 500 and 600 days. Moderate to severe spongiform changes were detected in the cerebral and cerebellar cortices, basal ganglia, thalamus, and brainstem. H-type BSE was characterized by the presence of PrP-immunopositive amyloid plaques in the white matter of the cerebrum, basal ganglia, and thalamus. Moreover, intraglial-type immunolabeled PrPSc was prominent throughout the brain. Stellate-type immunolabeled PrPSc was conspicuous in the gray matter of the cerebral cortex, basal ganglia, and thalamus, but not in the brainstem. In addition, PrPSc accumulation was detected in the peripheral nervous tissues, such as trigeminal ganglia, dorsal root ganglia, optic nerve, retina, and neurohypophysis. Cattle are susceptible to H-type BSE with a shorter incubation period, showing distinct and distinguishable phenotypes of PrPSc accumulation.
Highlights
Bovine spongiform encephalopathy (BSE), which belongs to a group of diseases called transmissible spongiform encephalopathies (TSE), is a fatal neurodegenerative disorder of cattle
This study demonstrated successful intraspecies transmission of H-type BSE characterized by a shorter incubation period as compared with C-type BSE [19]
To the best of our knowledge, far, neuropathological and immunohistochemical data for H-type BSE have only been reported from the medulla oblongata at the obex in German, United States, and Swedish field cases [10,13,24]
Summary
Bovine spongiform encephalopathy (BSE), which belongs to a group of diseases called transmissible spongiform encephalopathies (TSE), is a fatal neurodegenerative disorder of cattle. The infectious agent responsible for TSE is the disease-associated prion protein (PrPSc), which is thought to be a post-translationally modified form of the host-encoded membrane glycoprotein (PrPC) [2]. The transmissibility of atypical H-type and L-type BSE to mice [13,14,15,16,17,18] and cattle [19,20,21,22] has been confirmed, and these forms clearly differ from Ctype BSE regarding incubation periods, PrPres profiles, protease susceptibility, and spatial distribution patterns of histopathological lesions and immunolabeled PrPSc [3,6,16,20,22]. C-type [23] and H-type [14,15] BSE isolates were transmissible to wild-type mice already in the first passage, whereas L-type BSE agent failed to transmit in the first passage but was successfully transmitted to wild-type mice in the second passage [17]
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