Fig. 5: Induction of aggregation in cells. | Nature Communications

Fig. 5: Induction of aggregation in cells.

From: Exploiting the aggregation propensity of beta-lactamases to design inhibitors that induce enzyme misfolding

Fig. 5: Induction of aggregation in cells.The alternative text for this image may have been generated using AI.

A Brightfield and structured illumination microscopy (SIM) images of E. coli strain UZ_TEM104 treated with TEM3.2 at 12 μM for 120 min and stained with pFTAA. A single representative image is shown. B SIM image of E. coli strain UZ_TEM104 treated with 12 μM FITC-TEM 3.2 in PBS for 120 min and stained with the red-shifted oligothiophene HS169 to visualize aggregation. A single representative image is shown. C SIM and brightfield images as in A, but for E. coli ATCC strain. D SIM images of E. coli K12 MG1655 overexpressing GFP from a pBAD vectorn and treated with vehicle or peptide TEM3.2. A single representative image is shown. E Western blot and quantification for the TEM beta-lactamase in the inclusion body (IB) fraction of E. coli strain UZ_TEM104, treated with 12 μM of the indicated peptide in PBS or control for 120 min. A single representative blot is shown. The quantification is the result of the densitometric quantification of four independent experiments and shows the mean and the standard deviation. Statistical testing was done using one-way ANOVA with Dunnett’s pairwise comparison to control (ns non-significant, *P ≤ 0.05, **P ≤ 0.01, ***P ≤ 0.001, ****P ≤ 0.0001). The corrected P-values were 0.6091, 0.0029, 0.0027, <0.0001, and 0.9992, from left to right. F Western blot and quantification for the SHV beta-lactamase in the IB fraction of E. coli SHV-11, treated with 12 μM of the indicated peptide in PBS for 120 min or control. Statistics exactly as in E, but from 3 independent experiments. The corrected P-values were 0.8753, 0.9796, 0.0001, 0.0003, and 0.0003, from left to right. Source data are provided as a Source Data file.

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