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Prion detection by an amyloid seeding assay.

David W Colby¹, Qiang Zhang, Shuyi Wang

¹Institute for Neurodegenerative Diseases [corrected], University of California, San Francisco, CA 94143, USA.

Proceedings of the National Academy of Sciences of the United States of America

|December 22, 2007

Summary

A new amyloid seeding assay (ASA) detects prion diseases by observing the polymerization of recombinant prion protein (recPrP) into amyloid fibers. This method identifies PrP(Sc) in human and animal samples, offering a protease-independent detection approach.

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Area of Science:

Neuroscience
Biochemistry
Molecular Biology

Background:

Prion diseases are fatal neurodegenerative disorders.
Prion infectivity is linked to the polymerization of recombinant prion protein (recPrP) into amyloid fibers.
The prion protein exists in different forms, including protease-sensitive (sPrP(Sc)) and protease-resistant PrP(Sc).

Purpose of the Study:

To develop and validate a novel amyloid seeding assay (ASA) for prion detection.
To assess the sensitivity and strain-typing capability of the ASA.
To demonstrate the ASA's utility in detecting both protease-sensitive and protease-resistant PrP(Sc) without relying on protease digestion or immunodetection.

Main Methods:

Utilized Thioflavin T fluorescence to detect recPrP polymerization into amyloid.

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Applied the ASA to brain samples from humans with sporadic Creutzfeldt-Jakob disease and rodents with experimental prion disease.

Tested the ASA's sensitivity with various prion strains, including hamster Sc237 prions.

Main Results:

The ASA successfully seeded recPrP polymerization, indicating the presence of prions.
PrP(Sc) was detected in human and rodent prion disease samples.
The ASA demonstrated high sensitivity, with a detection limit of approximately 1 fg for hamster Sc237 prions.
The assay effectively detected various prion strains, including those composed of protease-sensitive PrP(Sc).

Conclusions:

The amyloid seeding assay (ASA) is a sensitive and versatile method for detecting prion diseases.
ASA provides an alternative to traditional protease digestion and immunodetection methods for identifying PrP(Sc).
This assay has significant potential for prion diagnostics and research.