Observing fibrillar assemblies on scrapie-infected cells
Publikation: Beitrag in Fachzeitschrift › Forschungsartikel › Beigetragen › Begutachtung
Beitragende
Abstract
The infectious agent in prion diseases is an aberrant-folded isoform of the cellular prion protein (PrPC). This scrapie-related prion protein (PrPSc) has an increased β-sheet content, is detergent insoluble and proteinase K resistant, and accumulates in prion-infected organisms and cells. In vitro, PrPSc self-aggregates into amyloid fibrils. However, there is no direct experimental proof for the occurrence of PrP Sc-containing fibrils in vivo or in cell cultures. Applying atomic force microscopy (AFM) to scrapie-infected mouse neuroblastoma (ScN2a) cells, we discovered growing patch-like assemblies of amyloid-like fibrillar structures on the cell surfaces. Immunofluorescence and AFM images showed heterogeneous accumulation and aggregation of PrPSc in ScN2a cell cultures. The percentage of cells having characteristic fibrils on their surface increased with time after scrapie infection. These endogeneous fibrils had lengths from 0.5 to 3 μm and protruded from the cell surface by 108±30 nm, and thus resembled the heterogeneous shapes and networks of in vitro prepared amyloid fibrils.
Details
Originalsprache | Englisch |
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Seiten (von - bis) | 83-93 |
Seitenumfang | 11 |
Fachzeitschrift | Pflugers Archiv European Journal of Physiology |
Jahrgang | 456 |
Ausgabenummer | 1 |
Publikationsstatus | Veröffentlicht - Apr. 2008 |
Peer-Review-Status | Ja |
Externe IDs
PubMed | 18175144 |
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Schlagworte
ASJC Scopus Sachgebiete
Schlagwörter
- Amyloid, Atomic force microscopy, Fibrils, Immunofluorescence, Mouse neuroblastoma (N2a) cells, Prion protein, Scrapie