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Authors: Christina D. Orrù, Jason M. Wilham, Sarah Vascellari, Andrew G. Hughson and Byron Caughey

Christina D. Orrù

Laboratory of Persistent Viral Diseases; Rocky Mountain Laboratories; National Institute of Allergy and Infectious Diseases; National Institutes of Health; Hamilton, MT USA

Jason M. Wilham

Laboratory of Persistent Viral Diseases; Rocky Mountain Laboratories; National Institute of Allergy and Infectious Diseases; National Institutes of Health; Hamilton, MT USA

Sarah Vascellari

Laboratory of Persistent Viral Diseases; Rocky Mountain Laboratories; National Institute of Allergy and Infectious Diseases; National Institutes of Health; Hamilton, MT USA

Andrew G. Hughson

Laboratory of Persistent Viral Diseases; Rocky Mountain Laboratories; National Institute of Allergy and Infectious Diseases; National Institutes of Health; Hamilton, MT USA

Byron Caughey

Corresponding author: bcaughey@nih.gov
Laboratory of Persistent Viral Diseases; Rocky Mountain Laboratories; National Institute of Allergy and Infectious Diseases; National Institutes of Health; Hamilton, MT USA

Abstract:
The ability of abnormal TSE-associated forms of PrP to seed the formation of amyloid fibrils from recombinant PrP^Sen has served as the basis for several relatively rapid and highly sensitive tests for prion diseases. These tests include rPrP-PMCA (rPMCA), standard quaking-induced conversion (S-QuIC), amyloid seeding assay (ASA), real-time QuIC (RT-QuIC) and enhanced QuIC (eQuIC). Here, we summarize recent improvements in the RT-QuIC-based assays that enhance the practicality, sensitivity and quantitative attributes of assays QuIC and promote the detection of prion seeding activity in dilute, inhibitor-laden fluids such as blood plasma.

Received: November 22, 2011; Accepted: January 20, 2012

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