Fig. 1
From: Potent prion-like behaviors of pathogenic α-synuclein and evaluation of inactivation methods
Seed-dependent α-syn aggregation induced by serial dilutions of synthetic α-syn fibrils in SH-SY5Y cells. a Electron microscopy of human α-syn fibrils after sonication for 180 s. Negatively stained short fibrils less than 100 nm in size were observed. Scale bar, 100 nm. b Serial 10-fold dilutions of human α-syn fibrils (2 μl) were introduced into SH-SY5Y cells transiently expressing human WT α-syn in the presence of the transfection reagent. Immunoblot analysis of sarkosyl-insoluble fractions (ppt) and sarkosyl-soluble fractions (sup) extracted from mock-transfected cells or cells transfected with human α-syn fibrils in the range of 2 μg (1) to 0.2 pg (10− 7) are shown. Phosphorylated α-syn was detected with anti-phosphorylated α-syn PSer129 antibody. α-Syn was detected with anti-syn 131–140 antibody c Quantification of phosphorylated α-syn accumulated in SH-SY5Y cells exposed to serial dilutions of synthetic human α-syn fibrils. Band intensities from the immunoblot analyses shown in b were measured. The results are expressed as means ± SEM (n = 3).