NR AXZI
AU Yokoyama,T.; Masujin,K.; Shu,Y.; Iwamaru,Y.; Imamura,M.; Mohri,S.
TI Characterization of an Abnormal Isoform of Prion Protein (PrPsc) in the Bovine Spongiform Encephalopathy (BSE) Resistant Animals
QU International Conference - Prion 2007 (26.-28.9.2007) Edinburgh International Conference Centre, Edinburgh, Scotland, UK - Book of Abstracts: Natural and Experimental Strains P02.06
IA http://www.prion2007.com/pdf/Prion Book of Abstracts.pdf
PT Konferenz-Poster
AB The "species barrier" influences the susceptibility of a host that may be subject to the interspecies transmission of prions. Although the bovine spongiform encephalopathy (BSE) prion affects a wide range of host species, it is not transmitted to hamsters. To study the species barrier, the transmissibility of the BSE prion to several lines of transgenic (Tg) mice, including those expressing chimeric prion protein (PrP) of mouse and hamster (MH2M and MHM2) were examined. The BSE prion was transmitted to tga20, MHM2, and ICR mice and it had an incubation period of approximately 400 days; hence, these mice were classified as "susceptible mice". However, the BSE prion was not transmitted to MH2M and TgHaNSE mice; therefore, these were classified as "resistant mice". The BSE prion had been passaged once in wild-type mice, and it could also transmit to resistant mice with abnormal isoform of PrP (PrPsc) accumulation. The characterization of PrPsc in susceptible and resistant mice was examined by using western blotting. PrPsc in all the Tg mice exhibited a BSE-like glycoform pattern with the antibody pAb B103 that recognized the N-terminal end of PrP27-30 as an epitope. PrPsc in susceptible mice also displayed a BSE-like glycoform pattern with another antibody (mAb 44B1) that recognized the C-terminal end of PrP27-30 as an epitope. In contrast, a different PrPsc pattern and molecular weight of PrPsc was detected in resistant mice by using 44B1 analysis. Deglycosylation analysis demonstrated that in addition to PrP27-30, truncated PrP fragments exist in resistant mice. These heterologous fragments might be the defective PrPsc that are generated during the adaptation of the BSE prion in resistant mice.
AD T. Yokoyama, K. Masujin, Y. Shu, Y. Iwamaru, M. Imamura, S. Mohri, National Institute of Animal Health, Prion Disease Research Center, Japan
SP englisch
PO Schottland