title: Intraspecies transmission of BASE induces clinical dullness and amyotrophic changes.
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.
authors.affiliation: Istituto Zooprofilattico Sperimentale della Lombardia e dell' Emilia Romagna, Brescia, Italy.
authors.forename: Guerino
authors.initials: G
authors.lastname: Lombardi
authors.forename: Cristina
authors.initials: C
authors.lastname: Casalone
authors.forename: Antonio
authors.initials: A
authors.lastname: D' Angelo
authors.forename: Daniela
authors.initials: D
authors.lastname: Gelmetti
authors.forename: Gloria
authors.initials: G
authors.lastname: Torcoli
authors.forename: Ilaria
authors.initials: I
authors.lastname: Barbieri
authors.forename: Cristiano
authors.initials: C
authors.lastname: Corona
authors.forename: Elisa
authors.initials: E
authors.lastname: Fasoli
authors.forename: Alessia
authors.initials: A
authors.lastname: Farinazzo
authors.forename: Michele
authors.initials: M
authors.lastname: Fiorini
authors.forename: Matteo
authors.initials: M
authors.lastname: Gelati
authors.forename: Barbara
authors.initials: B
authors.lastname: Iulini
authors.forename: Fabrizio
authors.initials: F
authors.lastname: Tagliavini
authors.forename: Sergio
authors.initials: S
authors.lastname: Ferrari
authors.forename: Maria
authors.initials: M
authors.lastname: Caramelli
authors.forename: Salvatore
authors.initials: S
authors.lastname: Monaco
authors.forename: Lorenzo
authors.initials: L
authors.lastname: Capucci
authors.forename: Gianluigi
authors.initials: G
authors.lastname: Zanusso
mesh_terms: D000682:Amyloid / Q000378:metabolism; D000818:Animals; D015415:Biomarkers / Q000378:metabolism; D001921:Brain / Q000378:metabolism / Q000473:pathology; D002417:Cattle; D016643:Encephalopathy, Bovine Spongiform / Q000473:pathology* / Q000635:transmission*; D005904:Glial Fibrillary Acidic Protein / Q000378:metabolism; D007150:Immunohistochemistry; D051379:Mice; D008822:Mice, Transgenic; D018482:Muscle, Skeletal / Q000378:metabolism / Q000473:pathology; D018621:PrPC Proteins / Q000302:isolation & purification / Q000378:metabolism / Q000472:pathogenicity*
chemical_list: D000682:Amyloid; D015415:Biomarkers; D005904:Glial Fibrillary Acidic Protein; D018621:PrPC Proteins