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BSE infection in bovine PrP transgenic mice leads to hyperphosphorylation of tau-protein.

Bautista, MJ, Gutiérrez, J, Salguero, FJ, Fernández de Marco, MM, Romero-Trevejo, JL and Gómez-Villamandos, JC (2006) BSE infection in bovine PrP transgenic mice leads to hyperphosphorylation of tau-protein. Vet Microbiol, 115 (4). pp. 293-301.

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We observed the changes in the central nervous system (CNS) of transgenic mice expressing bovine prion protein (Bo-PrP) as a contribution to our knowledge of the pathogenesis of bovine spongiform encephalopathy (BSE). The main result was the detection of hyperphosphorylated tau. This protein was detected for the first time, using immunohistochemical techniques, in the neurons and glial cells of mice experimentally infected with BSE. The results highlighted the involvement of tau protein in the pathogenesis of BSE and the close link between hyperphosphorylated tau deposits and prion protein. Ultrastructural examination revealed a novel arrangement of intraneuronal tau deposits not hitherto reported.

Item Type: Article
Authors :
Bautista, MJ
Gutiérrez, J
Salguero, FJ
Fernández de Marco, MM
Romero-Trevejo, JL
Gómez-Villamandos, JC
Date : 20 July 2006
DOI : 10.1016/j.vetmic.2006.02.017
Uncontrolled Keywords : Animals, Brain, Cattle, Encephalopathy, Bovine Spongiform, Female, Immunohistochemistry, Mice, Mice, Inbred CBA, Mice, Transgenic, Microscopy, Electron, Transmission, Phosphorylation, Prions, tau Proteins
Related URLs :
Depositing User : Symplectic Elements
Date Deposited : 17 May 2017 10:08
Last Modified : 17 May 2017 10:08

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