Advertisement

< Back to Article

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

Fig 5

RT-QuIC analysis of mWTD brain homogenates using deer and mouse substrates.

(a) The curves depict a representative RT-QuIC response of serially diluted (2x10-2 to 2x10-7) mWTD-wt (left panels) and -116AG (right panels) using rPrP deer or mouse substrate. Fluorescence signal was 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, c) The RT-QuIC responses of mWTD-wt and -116AG were quantified by calculating lag phase (b), and log phase (c). Mean values of 7 experiments with 4 replicates each were used and statistically evaluated using log-rank (Mantel-Cox) test for the lag phase (b) and unpaired t-test for the log phase (c). *P <0.05, **P <0.01 and ***P <0.005 refers to differences between mWTD isolates (GraphPad Prism software).

Fig 5

doi: https://doi.org/10.1371/journal.ppat.1006553.g005