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Destabilizing polymorphism in cervid prion protein hydrophobic core determines prion conformation and conversion efficiency

Fig 6

Efficiency of amyloid fibril formation using rPrP-116G substrate in RT-QuIC.

(a) The curves depict a representative RT-QuIC response of serially diluted (2x10-2 to 2x10-7) wt (upper panels) and 116AG (lower panels) WTD brain homogenates using rPrP-wt (right panels) or rPrP-116G (left panels) as substrates. Fluorescence signals were measured every 15 min. The x-axis represents the reaction time (hours), the y-axis represents the relative fluorescence units. Mean values of four replicates were used for each dilution. The cut-off is indicated at app. 50,000 RFU and is based on the average fluorescence values of negative controls +5SD. (b) The RT-QuIC responses of wt- and 116AG-prions were quantified by calculating the log phase for each isolate amplified using rPrP-wt or rPrP-116G. Mean values of 3 experiments with 4 replicates each were used for each isolate and statistical analyses were done using unpaired t-test for the log phase (b).

Fig 6