Analyses of protease resistance and aggregation state of abnormal prion protein across the spectrum of human prions

Daniela Saverioni, Silvio Notari, Sabina Capellari, Ilaria Poggiolini, Armin Giese, Hans A. Kretzschmar, Piero Parchi

Research output: Contribution to journalArticlepeer-review

Abstract

Background: Protease resistance and aggregation state, two fundamental properties of abnormal prion protein (PrPSc), remain significantly unexplored. Results: Prion isolates show differences in PrPSc PK digestion profile that are only partially explained by differences in aggregate size. Conclusion: Molecular factors, likely acting on aggregate stability, significantly influence PrPSc PK sensitivity. Significance: The study provides insight into prion strain variability with respect to PrPSc PK sensitivity and aggregation state.

Original languageEnglish
Pages (from-to)27972-27985
Number of pages14
JournalJournal of Biological Chemistry
Volume288
Issue number39
DOIs
Publication statusPublished - Sep 27 2013

ASJC Scopus subject areas

  • Biochemistry
  • Cell Biology
  • Molecular Biology

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