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Updated: May 4, 2026
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Isolation of Cortical Microglia with Preserved Immunophenotype and Functionality From Murine Neonates
Published on: January 30, 2014
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Reactive microglia partially envelop viable neurons in prion diseases
Natallia Makarava1,2, Tarek Safadi1,2, Olga Bocharova1,2
1Center for Biomedical Engineering and Technology and.
The Journal of Clinical Investigation
|October 3, 2024
Summary
In prion disease, microglia initially clear prions but later partially envelop neurons, leading to rapid prion accumulation and neuronal dysfunction. This microglial shift impacts neurodegeneration in prion diseases.
Area of Science:
- Neuroscience
- Immunology
- Pathology
Background:
- Microglia are key immune cells in the central nervous system, primarily known for phagocytosis.
- Prion diseases are characterized by the accumulation of misfolded prion proteins (PrPSc).
Purpose of the Study:
- To investigate microglial activity and interaction with neurons during prion disease progression.
- To characterize the phenomenon of neuronal envelopment by microglia in prion disease.
Main Methods:
- Observation of microglial-neuronal interactions in prion-affected brain tissue.
- Analysis of prion (PrPSc) accumulation and neuronal markers.
- Investigation of the role of specific pathways (e.g., CD11b) in microglial-neuronal interactions.
Main Results:
- Microglia phagocytose PrPSc in early prion disease stages.
- A shift occurs in late preclinical stages, with microglia forming extensive contacts with neurons.
- Partial neuronal envelopment by microglia is observed, associated with neuronal functional decline but not apoptosis.
- This envelopment is independent of the CD11b pathway and occurs across various prion disease models and human sCJD.
Conclusions:
- Microglial activity changes dynamically during prion disease, shifting from prion clearance to neuronal envelopment.
- Partial neuronal envelopment by reactive microglia is a novel phenomenon in neurodegenerative disease.
- This microglial behavior contributes to prion propagation and neuronal dysfunction in prion diseases.
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