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Published on: November 19, 2010
Observing fibrillar assemblies on scrapie-infected cells
Susanne Wegmann1, Margit Miesbauer, Konstanze F Winklhofer
1Center of Biotechnology, University of Technology, Dresden, Germany.
Pflugers Archiv : European Journal of Physiology
|January 5, 2008
Summary
Researchers discovered amyloid-like prion protein fibrils on the surface of scrapie-infected cells using atomic force microscopy. This provides the first direct evidence of these structures in cell cultures, advancing prion disease research.
Area of Science:
- Neuroscience
- Biochemistry
- Cell Biology
Background:
- Prion diseases involve aberrant-folded prion proteins (PrPSc) that are insoluble and resistant to degradation.
- In vitro studies show PrPSc self-aggregates into amyloid fibrils, but in vivo evidence is lacking.
Purpose of the Study:
- To investigate the presence and morphology of PrPSc aggregates in scrapie-infected cells.
- To provide direct experimental proof of PrPSc-containing fibrils in cell cultures.
Main Methods:
- Utilized atomic force microscopy (AFM) on scrapie-infected mouse neuroblastoma (ScN2a) cells.
- Combined AFM with immunofluorescence imaging to analyze PrPSc accumulation.
Main Results:
- Discovered growing, patch-like, amyloid-like fibrillar structures on the surfaces of ScN2a cells.
- Observed heterogeneous accumulation and aggregation of PrPSc, with fibril presence increasing over time post-infection.
- Characterized endogenous fibrils: 0.5–3 µm in length, protruding ~108 nm from the cell surface.
Conclusions:
- Provides the first direct experimental evidence for PrPSc-containing amyloid fibrils on the surface of infected cells.
- These endogenous fibrils resemble in vitro-formed amyloid structures, suggesting similar aggregation mechanisms.
- This finding enhances understanding of prion pathogenesis and potential therapeutic targets.
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03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
03:03Amyloid Fibrils
Amyloid fibrils are aggregates of misfolded proteins. Under most circumstances, misfolded proteins are either refolded by chaperone proteins or degraded by the proteasome. However, in the case of a mutation or a disease, these proteins can accumulate to form large clusters and often further assemble to form elongated fibers, called fibrils.
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...
Amyloid deposits were observed as early as 1639 in the liver and the spleen. In 1854, Rudolph Virchow performed iodine staining, normally used to...