title: Glycosylation and prion protein.
abstract: 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.
authors.affiliation: Oxford Glycobiology Institute, University of Oxford, South Parks Road, Oxford OX1 3QU, UK. pmr@glycob.ox.ac.uk
authors.forename: Pauline M
authors.initials: PM
authors.lastname: Rudd
authors.forename: Anthony H
authors.initials: AH
authors.lastname: Merry
authors.forename: Mark R
authors.initials: MR
authors.lastname: Wormald
authors.forename: Raymond A
authors.initials: RA
authors.lastname: Dwek
mesh_terms: 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
chemical_list: D011328:Prions; D020033:Protein Isoforms