Abstract
The scrapie (PrP Sc) and cellular (PrP C) prion proteins are encoded by the same gene, and their different properties are thought to arise from posttranslational modifications. We have found a phosphatidylinositol glycolipid on both PrP C and PrP 27–30 (derived from PrP Sc by limited proteolysis at the amino terminus). Ethanolamine, myo-inositol, phosphate, and stearic acid were identified as glycolipid components of gelpurified PrP 27–30. PrP 27–30 contains 2.8 moles of ethanolamine per mole. Incubation of PrP 27–30 with a bacterial phosphatidylinositol-specific phospholipase C (PIPLC) releases covalently bound stearic acid, and allows PrP 27–30 to react with antiserum specific for the PIPLC-digested glycolipid linked to the carboxyl terminus of the trypanosomal variant surface glycoprotein. PIPLC catalyzes the release of PrP C from cultured mammalian cells into the medium. These observations indicate that PrP C is anchored to the cell surface by the glycolipid.
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