Fig. 6: SoLs bear structural similarity to both lipid A and sulfatide and bind with MD-2 to block LPS binding. | Nature Communications

Fig. 6: SoLs bear structural similarity to both lipid A and sulfatide and bind with MD-2 to block LPS binding.

From: Biosynthetic enzyme analysis identifies a protective role for TLR4-acting gut microbial sulfonolipids in inflammatory bowel disease

Fig. 6: SoLs bear structural similarity to both lipid A and sulfatide and bind with MD-2 to block LPS binding.

a Chemical structures of immunogenic lipid A (derived from LPS), sulfatide, SoL A, and SoL B illustrating structural similarity in multiple acyl chains and negatively charged head groups. b Molecular docking of lipid A (red), sulfatide (magenta), SoL A (blue), and SoL B (orange) into the hydrophobic pocket of MD-2 in complex with TLR4. Three molecules of SoLs A and B were used in molecular docking experiments to mimic the six acyl chains of lipid A as inspired by sulfatides58. c ELISA displacement assay used to measure the binding behavior of SoLs A and B in competition with 1 ng/mL LPS, a natural ligand of the TLR4/MD-2 complex. Compounds were added either simultaneously (blue), LPS first (green), or SoL first (red). Bars indicate mean ± standard deviation. Experiments were independently repeated three times. For each treatment, n = 3 individual wells. Source data are provided in the Source Data file.

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