J Vet Sci.  2019 Mar;20(2):e8. 10.4142/jvs.2019.20.e8.

Re-transmissibility of mouse-adapted ME7 scrapie strain to ovine PrP transgenic mice

• Babalola J
• Kim JM
• Lee YJ
• Park JH
• Choi HS
• Choi YG
• Choi EK
• Kim YS

• KMID: 2454011
• DOI: http://doi.org/10.4142/jvs.2019.20.e8

Abstract

Scrapie is a mammalian transmissible spongiform encephalopathy or prion disease that predominantly affects sheep and goats. Scrapie has been shown to overcome the species barrier via experimental infection of other rodents. To confirm the re-transmissibility of the mouse-adapted ME7 scrapie strain to ovine prion protein (PrP) transgenic mice, mice of an ovinized transgenic mouse line carrying the Suffolk sheep PrP gene that contained the A₁₃₆ R₁₅₄ Q₁₇₁/ARQ allele were intracerebrally inoculated with brain homogenates obtained from terminally ill ME7-infected C57BL/6J mice. Herein, we report that the mouse-adapted ME7 scrapie strain was successfully re-transmitted to the transgenic mice expressing ovine PrP. In addition, we observed changes in the incubation period, glycoform profile, and pattern of scrapie PrP (PrP(Sc)) deposition in the affected brains. PrP(Sc) deposition in the hippocampal region of the brain of 2nd-passaged ovine PrP transgenic mice was accompanied by plaque formation. These results reveal that the mouse-adapted ME7 scrapie strain has the capacity to act as a template for the conversion of ovine normal monomeric precursors into a pathogenic form in ovine PrP transgenic mice. The change in glycoform pattern and the deposition of plaques in the hippocampal region of the brain of the 2nd-passaged PrP transgenic mice are most likely cellular PrP species dependent rather than being ME7 scrapie strain encoded.

Keyword

Prion; prion diseases; scrapie; gliosis; amyloid plaque

MeSH Terms

Alleles
Animals
Brain
Gliosis
Goats
Humans
Mice
Mice, Transgenic*
Plaque, Amyloid
Prion Diseases
PrPSc Proteins
Rodentia
Scrapie*
Sheep
Terminally Ill
PrPSc Proteins