Fig 2: Potential interaction between ApoM and E.coli LPS revealed by docking simulations. A: Top-ranked model of ApoM-E coli LPS complex; ApoM is shown as a grey van der Waals surface, while E. coli LPS is presented as a red ball-and-stick model. B: Top-ranked model with ApoM in ribbon representation (green) and E. coli LPS shown as a red ball-and-stick model. C: A closer view of the ApoM-E. coli LPS binding interface. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig 3: ITC measurements of ApoM and E. coli LPS interactions. (Upper Panel) Change of power supply to the calorimetric cell during the titration of 100 μM of LPS solution into 10 μM of ApoM in PBS buffer at 25 °C, after the subtraction of the appropriate reference experiments. Negative values indicate exothermic peaks. (Lower Panel) Integration of the area under each injection, normalized per mol of injectant and plotted as a function of the [LPS]/[ApoM] ratio at each point of the titration. Solid red line represent the non-linear least-square fit of the ITC data to a single-set-of-sites binding model. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)

Fig 4: ApoM neutralized E. coli LPS and reduced nitric oxide release from macrophages in vitro. Freshly grown RAW264 macrophages were transferred to 96-well plate (0.25 × 106 cell/well) then induced with E. coli LPS (100 and 50 ng/ml) pre-incubated with or without ApoM (10 μg/ml) for 30 min. LL37 was used as a control due to its ability to neutralize endotoxin. Plates were incubated overnight and nitrite accumulation was measured using the Greiss reaction method.