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 language | English |
|---|---|
| Journal | PLoS Pathogens |
| Volume | 3 |
| Issue number | 3 |
| DOIs | |
| Publication status | Published - Mar 2007 |
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ASJC Scopus subject areas
- Microbiology
- Parasitology
- Virology
- Immunology
- Genetics
- Molecular Biology
Cite this
Conversion of the BASE prion strain into the BSE strain : The origin of BSE? / Capobianco, Raffaella; Casalone, Cristina; Suardi, Silvia; Mangieri, Michela; Miccolo, Claudia; Limido, Lucia; Catania, Marcella; Rossi, Giacomina; Di Fede, Giuseppe; Giaccone, Giorgio; Bruzzone, Maria Grazia; Minati, Ludovico; Corona, Cristiano; Acutis, Pierluigi; Gelmetti, Daniela; Lombardi, Guerino; Groschup, Martin H.; Buschmann, Anne; Zanusso, Gianluigi; Monaco, Salvatore; Caramelli, Maria; Tagliavini, Fabrizio.
In: PLoS Pathogens, Vol. 3, No. 3, 03.2007.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Conversion of the BASE prion strain into the BSE strain
T2 - The origin of BSE?
AU - Capobianco, Raffaella
AU - Casalone, Cristina
AU - Suardi, Silvia
AU - Mangieri, Michela
AU - Miccolo, Claudia
AU - Limido, Lucia
AU - Catania, Marcella
AU - Rossi, Giacomina
AU - Di Fede, Giuseppe
AU - Giaccone, Giorgio
AU - Bruzzone, Maria Grazia
AU - Minati, Ludovico
AU - Corona, Cristiano
AU - Acutis, Pierluigi
AU - Gelmetti, Daniela
AU - Lombardi, Guerino
AU - Groschup, Martin H.
AU - Buschmann, Anne
AU - Zanusso, Gianluigi
AU - Monaco, Salvatore
AU - Caramelli, Maria
AU - Tagliavini, Fabrizio
PY - 2007/3
Y1 - 2007/3
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=34047207529&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=34047207529&partnerID=8YFLogxK
U2 - 10.1371/journal.ppat.0030031
DO - 10.1371/journal.ppat.0030031
M3 - Article
VL - 3
JO - PLoS Pathogens
JF - PLoS Pathogens
SN - 1553-7366
IS - 3
ER -