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Fig. 8 | Microbial Cell Factories

Fig. 8

From: Soluble polymorphic bank vole prion proteins induced by co-expression of quiescin sulfhydryl oxidase in E. coli and their aggregation behaviors

Fig. 8

rBVPrP-109M and rBVPrP-109I used as substrates for RT-QuIC analysis of hamster 263 K and mouse139A. a RT-QuIC spectra of 263 K and 139A in the presence of rBVPrP109I or rBVPrP109M as a substrate, respectively. 2 µL of brain homogenate diluted at 10−3 from either 263 K-infected hamster brain or 139A-infected mouse brain was added into each well of the 96-well plates as seeds. Each well contained 98 µL RT-QuIC reaction solution [10 mM phosphate buffer at pH 7.4, 300 mM NaCl, 10 µM thioflavin T (ThT), 1 mM EDTA, and 0.1 mg/mL of either rBVPrP109I (top four rows) or rBVPrP109M (bottom four rows)]. Negative controls were the samples without PrPSc seeds. b Comparison of ThT fluorescence intensity of RT-QuIC prion seeding activity of rBVPrP with 109I or 109M polymorphism seeded by 263 K or 193A strains. The ThT fluorescence intensity is plotted as a function of reaction time (hours). c Comparison of the lag phase of the RT-QuIC seeding activity of rBVPrP with 109I or 109M polymorphism seeded by 263 K and 193A stains. Percentage of maximal ThT fluorescence is plotted as a function of reaction time (hours)

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