Fig. 2: rPga59 aggregates display amyloid structures properties. | npj Biofilms and Microbiomes

Fig. 2: rPga59 aggregates display amyloid structures properties.

From: The Pga59 cell wall protein is an amyloid forming protein involved in adhesion and biofilm establishment in the pathogenic yeast Candida albicans

Fig. 2: rPga59 aggregates display amyloid structures properties.

HIS6-Pga59 and HIS6-Pga59V32,33N proteins were expressed in Escherichia coli and purified by affinity chromatography. rPga59 proteins were analysed with Coomassie blue staining (a) and western blot using an α-His antibody (b). Fractions loaded on the gel correspond to the flow through (FT), the wash (W) and the elution (E). (M): Molecular weight markers. Sizes are indicated on the left. c ThT fluorescence intensity of each recombinant proteins analysed at 496 nm. The histogram shows the quantification of data from three independent experiments. Values are displayed as the averages ± SD. (**) p < 0.01. The significance of the ThT fluorescence differences was tested using Student’s t-test. d Wild type (left) and mutated (right) rPga59 were negatively stained with uranyl acetate and analysed with transmission electron microscopy. An isolated amyloid fibre formed by the WT protein is pinpointed on the micrograph with an arrow. Scale bar: 100 nm. Source data are provided as a Source Data file.

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