Intraspecies Transmission of BASE Induces Clinical Dullness and Amyotrophic Changes

PLoS Pathogens

Cristiano Corona¹  Maria Caramelli¹  Barbara Iulini¹  Cristina Casalone¹  Michele Fiorini²  Gianluigi Zanusso²  Sergio Ferrari²  Salvatore Monaco²  Elisa Fasoli²  Matteo Gelati²  Alessia Farinazzo²  Antonio D' Angelo³  Fabrizio Tagliavini⁴  Guerino Lombardi⁵  Daniela Gelmetti⁵  Gloria Torcoli⁵  Ilaria Barbieri⁵  Lorenzo Capucci⁵ 

[1] Centro di Referenza Nazionale per le Encefalopatie Animali, Istituto Zooprofilattico Sperimentale del Piemonte, Liguria e Valle D' Aosta, Turin, Italy;Department of Neurological and Visual Sciences, Section of Clinical Neurology, University of Verona, Verona, Italy;Dipartimento di Patologia Animale, Università degli Studi di Torino, Grugliasco, Italy;Fondazione IRCCS Istituto Nazionale Neurologico “Carlo Besta”, Milan, Italy;Istituto Zooprofilattico Sperimentale della Lombardia e dell' Emilia Romagna, Brescia, Italy

关键词: Cattle;    Bovine spongiform encephalopathy;    Veterinary diseases;    Animal prion diseases;    Motor neurons;    Muscle tissue;    Spinal cord;    Thalamus;   

DOI  :  10.1371/journal.ppat.1000075

学科分类：生物科学（综合）

来源: Public Library of Science

【 摘 要 】

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 (PrPTSE), named high-type (BSE-H) and low-type (BSE-L). We recently reported two Italian atypical cases with a PrPTSE 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.

【 授权许可】

CC BY