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Updated: Jul 16, 2026

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain
11:29

Isolation of Soluble and Insoluble PrP Oligomers in the Normal Human Brain

Published on: October 3, 2012

Identification of prion amyloid filaments in scrapie-infected brain

S J DeArmond, M P McKinley, R A Barry

    Cell
    |May 1, 1985
    PubMed

    Insights

    Abnormal prion protein filaments, forming amyloid plaques, were found in the brains of scrapie-infected hamsters. These protein filaments, composed of PrP 27-30, accumulate extracellularly, offering insights into prion disease pathology.

    Area of Science:

    • Neuroscience
    • Biochemistry
    • Pathology

    Background:

    • Prion diseases are characterized by the accumulation of misfolded prion proteins.
    • The exact structure and formation of these aggregates in vivo remain incompletely understood.

    Purpose of the Study:

    • To investigate the ultrastructural morphology of prion protein aggregates in the brain of scrapie-infected hamsters.
    • To determine the composition of these aggregates and compare them to purified prion preparations.

    Main Methods:

    • Immunoelectron microscopy was employed to visualize and characterize extracellular filaments in hamster brains.
    • Affinity-purified antibodies against PrP 27-30 were used for compositional analysis.

    Main Results:

    • Extracellular filaments, 16 nm in diameter and up to 1500 nm in length, were identified in scrapie-infected hamster brains.
    • These filaments, composed of PrP 27-30, exhibited limited twisting, suggesting possible flattened cylinder or helical protofilament structures.
    • The ultrastructure of these prion filaments closely resembles amyloid structures found in other tissues.

    Conclusions:

    • This study provides the first direct evidence of prion protein assembly into filaments within the brain.
    • These filaments accumulate extracellularly, forming amyloid plaques, a hallmark of prion diseases.
    • The findings contribute to understanding the structural basis of prion pathogenesis and amyloid formation.

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