Preparation of lyophilized recombinant prion protein for TSE diagnosis by RT-QuIC

April 9, 2019

Title

Preparation of lyophilized recombinant prion protein for TSE diagnosis by RT-QuIC

Author

Soyoun Hwang, Trudy Tatum, Semakaleng Lebepe‑Mazur, Eric M. Nicholson

Year

2018

Journal

BMC Research Notes

Abstract

Transmissible spongiform encephalopathies (TSEs) are a group of fatal neurodegenerative diseases, often referred as prion diseases. TSEs result from the misfolding of the cellular prion protein (PrPC ) into a pathogenic form (PrPSc) that accumulates in the brain and lymphatic tissue. Amplifcation based assays such as real-time quaking induced conversion allow us to assess the conversion of PrPC to PrPSc. Real-time quaking induced conversion (RTQuIC) can be used for the detection of PrPSc in a variety of biological tissues from humans and animals. However, RTQuIC requires a continuous supply of freshly purifed prion protein and this necessity is not sustainable in a diagnostic
laboratory setting. In this study, we developed a method to dry and preserve the prion protein for long term storage allowing for production of the protein and storage for extended time prior to use and room temperature shipping to appropri‑ ate diagnostic laboratory destinations facilitating widespread use of RT-QuIC as a diagnostic method.

Instrument

J-815

Keywords

Circular dichroism, Secondary structure, Protein folding, Thermal stability, Thermodynamics, Biochemistry