NDLI: Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation.

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Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation.

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Acquisition of protease resistance by prion proteins in scrapie-infected cells does not require asparagine-linked glycosylation.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Taraboulos, A. Mckinley, M. P. Prusiner, S. B. Rogers, M. Scott, M. Borchelt, D. R. Serban, D.
Description	Author Affiliation: Taraboulos A ( Department of Neurology, University of California, San Francisco 94143.);
Abstract	The scrapie and cellular isoforms of the prion protein (PrPSc and PrPC) differ strikingly in a number of their biochemical and metabolic properties. The structural features underlying these differences are unknown, but they are thought to result from a posttranslational process. Both PrP isoforms contain complex type oligosaccharides, raising the possibility that differences in the asparagine-linked glycosylation account for the properties that distinguish PrPC and PrPSc. ScN2a and ScHaB cells in culture produce several PrP molecules with relative molecular masses of 26-35 kDa and proteinase K-resistant cores of 19-29 kDa. When the cells were treated with tunicamycin, this heterogeneity was eliminated and a single PrP species of 26 kDa was observed. Several hours after its synthesis, a fraction of this protein became insoluble in detergents and acquired a proteinase K-resistant core, thus displaying two of the biochemical hallmarks of PrPSc. Synthesis in the presence of tunicamycin restricted the proteinase K-resistant cores of PrP to a single species of 19 kDa. No proteinase K-resistant PrP was found in uninfected cells. Expression of a mutated PrP gene lacking both asparagine-linked glycosylation sites in ScN2a cells resulted in the synthesis of 19-kDa proteinase K-resistant PrP molecules. We conclude that asparagine-linked glycosylation is not essential for the synthesis of proteinase K-resistant PrP and that structural differences unrelated to asparagine-linked oligosaccharides must exist between PrPC and PrPSc. Whether unglycosylated PrPSc molecules are associated with scrapie prion infectivity remains to be established.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	21
Volume Number	87
Language	English
Publisher	National Academy of Sciences
Publisher Date	1990-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Transformation, Viral Prions Genetics Serine Endopeptidases Metabolism Viral Proteins Amino Acid Sequence Asparagine Endopeptidase K Glycosylation Kinetics Molecular Sequence Data PrPSc Proteins Protein Processing, Post-Translational Drug Effects Tunicamycin Pharmacology Isolation & Purification Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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