摘要
Acinetobacter baumannii infections are associated with a high mortality rate. Sulbactam, a beta-lactamase inhibitor, is commonly used to treat A. baumannii infections, but its underlying mechanisms are unclear. Two-component regulatory systems (TCSs) are important for bacterial adaptability and response ability. In this study, we focused on two TCSs, namely AdeSR and BaeSR, and identified a protein highly similar to the dimerization and histidine phosphotransfer (DHp) and catalytic ATP-binding (CA) domains of the TCSs by using Swiss-Model. Sulbactam and β-lactamase inhibitors, which are structurally similar to sulbactam, were docked with the selected sequence 4JAS using the simulation tools SwissDock and ArgusLab. Analysis with both these analytical tools showed that sulbactam can react on the active sites of 4JAS at a relatively steady level (ΔG -7 to −10 kcal/mol). Sulbactam likely interacts with the active sites of BaeSR and AdeSR, and owing to its smaller size and ability to form ionic bonds with Mg 2+ , it may potentially compete with ATP/ADP in BaeSR and AdeSR and consequently interfere with A. baumannii multiplication. This is the first study to investigate the association between sulbactam and TCSs in A. baumannii using molecular docking and simulation analyses.