Interactions between prion protein isoforms: the kiss of death?
Direct interactions between the normal and aberrant forms of prion protein appear to be crucial in the transmission and pathogenesis of transmissible spongiform encephalopathies (TSEs) or prion diseases. Recent studies of such interactions in vitro have provided mechanistic insight into how TSE-associated prion protein might promote its own propagation in a manner that is specific enough to account, at least in part, for TSE strains and species barriers.
Caughey
B
B
Laboratory of Persistent Viral Diseases, NIAID, NIH, Rocky Mountain Laboratories, 903 S. 4th St, 59840, Hamilton, MT, USA. bcaughey@nih.gov
D017096:Prion Diseases / Q000378:metabolism; D011328:Prions / Q000378:metabolism*; D011485:Protein Binding; D020033:Protein Isoforms / Q000378:metabolism*
D011328:Prions; D020033:Protein Isoforms