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ARS Home » Midwest Area » Ames, Iowa » National Animal Disease Center » Virus and Prion Research » Research » Publications at this Location » Publication #356018
Research Project: Pathobiology, Genetics, and Detection of Transmissible Spongiform Encephalopathies

Location: Virus and Prion Research

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

Author
item Hwang, Soyoun
item Tatum, Trudy
item Lebepe Mazur, Semakaleng
item Nicholson, Eric

Submitted to: BMC Research Notes
Publication Type: Peer Reviewed Journal
Publication Acceptance Date: 12/4/2018
Publication Date: 12/14/2018
Citation: Hwang, S., Tatum, T., Lebepe-Mazur, S., Nicholson, E.M. 2018. Preparation of lyophilized recombinant prion protein for TSE diagnosis by RT-QuIC. BMC Research Notes. 11:895. https://doi.org/10.1186/s13104-018-3982-5.
DOI: https://doi.org/10.1186/s13104-018-3982-5

Interpretive Summary: Prion disease diagnostic advances include methods to amplify the amount of the infectious agent, in a sample. One such method, known as RT-QuIC, requires a study supply of freshly purified prion protein which necessitates an ongoing effort to produce in a manner that is not sustainable in a diagnostic laboratory setting. In this study we develop a method to dry and preserve the prion protein for long term storage allowing for production of the protein and storage for months or years prior to use and room temperature shipping to appropriate diagnostic laboratory destinations facilitating widespread use of RT-QuIC as a diagnostic method.

Technical Abstract: Transmissible spongiform encephalopathy (TSE) is a group of fatal neurodegenerative diseases, often referred as prion diseases, and the disorder is resulted from the misfolding of the cellular prion protein (PrPC) into a pathogenic form (PrPSc) that accumulates in the brain and lymphatic tissue. Amplification based assays such as real-time quaking induced conversion (RT-QuIC) allow us to assess the conversion of PrPC to PrPSc. RT-QuIC can be used for the detection of PrPSc in a variety of biological tissues from humans and animals. However, RT-QuIC requires a continuous supply of freshly purified 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 appropriate diagnostic laboratory destinations facilitating widespread use of RT-QuIC as a diagnostic method.