Conversion of the BASE prion strain into the BSE strain: The origin of BSE?

Raffaella Capobianco, Cristina Casalone, Silvia Suardi, Michela Mangieri, Claudia Miccolo, Lucia Limido, Marcella Catania, Giacomina Rossi, Giuseppe Di Fede, Giorgio Giaccone, Maria Grazia Bruzzone, Ludovico Minati, Cristiano Corona, Pierluigi Acutis, Daniela Gelmetti, Guerino Lombardi, Martin H. Groschup, Anne Buschmann, Gianluigi Zanusso, Salvatore MonacoMaria Caramelli, Fabrizio Tagliavini

Research output: Contribution to journalArticlepeer-review

Abstract

Atypical neuropathological and molecular phenotypes of bovine spongiform encephalopathy (BSE) have recently been identified in different countries. One of these phenotypes, named bovine "amyloidotic" spongiform encephalopathy (BASE), differs from classical BSE for the occurrence of a distinct type of the disease-associated prion protein (PrP), termed PrP Sc, and the presence of PrP amyloid plaques. Here, we show that the agents responsible for BSE and BASE possess different biological properties upon transmission to transgenic mice expressing bovine PrP and inbred lines of nontransgenic mice. Strikingly, serial passages of the BASE strain to nontransgenic mice induced a neuropathological and molecular disease phenotype indistinguishable from that of BSE-infected mice. The existence of more than one agent associated with prion disease in cattle and the ability of the BASE strain to convert into the BSE strain may have important implications with respect to the origin of BSE and spongiform encephalopathies in other species, including humans.

Original languageEnglish
JournalPLoS Pathogens
Volume3
Issue number3
DOIs
Publication statusPublished - Mar 2007

ASJC Scopus subject areas

  • Microbiology
  • Parasitology
  • Virology
  • Immunology
  • Genetics
  • Molecular Biology

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