Pathology of SSLOW, a transmissible and fatal synthetic prion protein disorder, and comparison with naturally occurring classical transmissible spongiform encephalopathies.

ABSTRACT:

Aims

Naturally occurring transmissible spongiform encephalopathies (TSEs) accumulate disease-specific forms of prion protein on cell membranes in association with pathognomonic lesions. We wished to determine whether synthetic prion protein disorders recapitulated these and other subcellular TSE-specific changes.

Methods

SSLOW is a TSE initiated with refolded synthetic prion protein. Five terminally sick hamsters previously intracerebrally inoculated with third passage SSLOW were examined using light and immunogold electron microscopy.

Results

SSLOW-affected hamsters showed widespread abnormal prion protein (PrP(SSLOW) ) and amyloid plaques. PrP(SSLOW) accumulated on plasma lemmas of neurites and glia without pathological changes. PrP(SSLOW) also colocalized with incr

SUBMITTER: Jeffrey M 

PROVIDER: S-EPMC3783560 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature