NR AMCJ
AU Vorberg,I.; Priola,S.A.
TI Molecular basis of scrapie strain glycoform variation
QU The Journal of Biological Chemistry 2002 Sep 27; 277(39): 36775-81
PT journal article
AB Transmissible spongiform encephalopathies (TSE) are characterized by the conversion of a protease-sensitive host glycoprotein, prion protein or PrP-sen, to a protease-resistant form (PrPres). PrPres molecules that accumulate in the brain and lymphoreticular system of the host consist of three differentially glycosylated forms. Analysis of the relative amounts of the PrPres glycoforms has been used to discriminate TSE strains and has become increasingly important in the differential diagnosis of human TSEs. However, the molecular basis of PrPres glycoform variation between different TSE agents is unknown. Here we report that PrPres itself can dictate strain-specific PrPres glycoforms. The final PrPres glycoform pattern, however, can be influenced by the cell and significantly altered by subtle changes in the glycosylation state of PrP-sen. Thus, strain-specific PrPres glycosylation profiles are likely the consequence of a complex interaction between PrPres, PrP-sen, and the cell and may indicate the cellular compartment in which the strain-specific formation of PrPres occurs.
MH Animal; Blotting, Western; Brain/metabolism; Cell-Free System; *Glycosylation; Human; Mice; Phenotype; PrPsc Proteins/*chemistry/metabolism; Prion Diseases/*metabolism; Scrapie/*metabolism; Tumor Cells, Cultured
AD Laboratory of Persistent Viral Diseases, NIAID, National Institutes of Health, Rocky Mountain Laboratories, Hamilton, Montana 59840, USA
SP englisch
PO USA