Molecular basis of scrapie strain glycoform variation - PubMed (original) (raw)
. 2002 Sep 27;277(39):36775-81.
doi: 10.1074/jbc.M206865200. Epub 2002 Jul 23.
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- PMID: 12138171
- DOI: 10.1074/jbc.M206865200
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Molecular basis of scrapie strain glycoform variation
Ina Vorberg et al. J Biol Chem. 2002.
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Abstract
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 (PrP-res). PrP-res 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 PrP-res 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 PrP-res glycoform variation between different TSE agents is unknown. Here we report that PrP-res itself can dictate strain-specific PrP-res glycoforms. The final PrP-res 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 PrP-res glycosylation profiles are likely the consequence of a complex interaction between PrP-res, PrP-sen, and the cell and may indicate the cellular compartment in which the strain-specific formation of PrP-res occurs.
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