Underglycosylated prion protein modulates plaque formation in the brain

Research output: Contribution to journalReview articlepeer-review


The prion agent is unique in biology and is comprised of prion protein scrapie (PrPSc), a self-templating conformational variant of the host encoded prion protein cellular (PrPC). The deposition patterns of PrPSc in the CNS can vary considerably from a diffuse synaptic pattern to large plaque-like aggregates. Alterations of PrPC posttranslational processing can change PrPSc deposition patterns; however, the mechanism underlying these observations is unclear. In this issue of the JCI, Sevillano and authors determined that parenchymal PrPSc plaques of the mouse brain preferentially incorporated underglycosylated PrPC that had been liberated from the cell surface by the metalloproteinase, ADAM-10, in combination with heparan sulfate. These results provide mechanistic insight into the formation of PrPSc plaques and suggest that PrP posttranslational modifications direct pathogenicity as well as the rate of disease progression.

Original languageEnglish (US)
Pages (from-to)1087-1089
Number of pages3
JournalJournal of Clinical Investigation
Issue number3
StatePublished - Mar 2 2020

All Science Journal Classification (ASJC) codes

  • Medicine(all)


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