Abstract:
:The disease phenotype of bovine spongiform encephalopathy (BSE) and the molecular/ biological properties of its prion strain, including the host range and the characteristics of BSE-related disorders, have been extensively studied since its discovery in 1986. In recent years, systematic testing of the brains of cattle coming to slaughter resulted in the identification of at least two atypical forms of BSE. These emerging disorders are characterized by novel conformers of the bovine pathological prion protein (PrP(TSE)), named high-type (BSE-H) and low-type (BSE-L). We recently reported two Italian atypical cases with a PrP(TSE) type identical to BSE-L, pathologically characterized by PrP amyloid plaques and known as bovine amyloidotic spongiform encephalopathy (BASE). Several lines of evidence suggest that BASE is highly virulent and easily transmissible to a wide host range. Experimental transmission to transgenic mice overexpressing bovine PrP (Tgbov XV) suggested that BASE is caused by a prion strain distinct from the BSE isolate. In the present study, we experimentally infected Friesian and Alpine brown cattle with Italian BSE and BASE isolates via the intracerebral route. BASE-infected cattle developed amyotrophic changes accompanied by mental dullness. The molecular and neuropathological profiles, including PrP deposition pattern, closely matched those observed in the original cases. This study provides clear evidence of BASE as a distinct prion isolate and discloses a novel disease phenotype in cattle.
journal_name
PLoS Pathogjournal_title
PLoS pathogensauthors
Lombardi G,Casalone C,D' Angelo A,Gelmetti D,Torcoli G,Barbieri I,Corona C,Fasoli E,Farinazzo A,Fiorini M,Gelati M,Iulini B,Tagliavini F,Ferrari S,Caramelli M,Monaco S,Capucci L,Zanusso Gdoi
10.1371/journal.ppat.1000075subject
Has Abstractpub_date
2008-05-23 00:00:00pages
e1000075issue
5eissn
1553-7366issn
1553-7374journal_volume
4pub_type
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