Glycosylation and prion protein.
Recent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycoforms" as a diagnostics tool has been discussed. The possibility exists that the glycans may play a role in the location of the prion protein on the neuronal cell surface. Alternative topologies and tethering of the prion glycoprotein on the cell membrane affect glycan site occupancy and may play a role in disease pathogenesis.
Rudd
Pauline M
PM
Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. pmr@glycob.ox.ac.uk
Merry
Anthony H
AH
Wormald
Mark R
MR
Dwek
Raymond A
RA
D006031:Glycosylation; D008958:Models, Molecular; D011328:Prions / Q000737:chemistry / Q000378:metabolism*; D017510:Protein Folding; D020033:Protein Isoforms / Q000737:chemistry / Q000378:metabolism; D017433:Protein Structure, Secondary
D011328:Prions; D020033:Protein Isoforms