The Inhibition Mechanism of Emodin to the Core Protein of Aeromonas Hydrophila at the Molecular Level

Aeromonas hydrophila is a main pathogen and is of great harm in aquaculture, but the effective methods to inhibit it is not clear. This study reveals that emodin inhibits the activity of A. hydrophila through experimental methods. Further proteomics analysis showed that atpE was the core protein of the inhibition. To disclose how emodin affects the inhibition mechanism, molecular docking and molecular dynamics simulations were carried out for A. hydrophila core protein binding with emodin. Comparing with these simulations of free atpE, this study uncovered that the inhibition of emodin involves emodin directly binding to core protein atpE with this simulations. The emodin engages with residues TYR10, ALA13, ALA14, MET17, LEU70 and TYR73 of atpE, which eventually leads to the inhibition of the activity of A. hydrophila . Additionally, this phenomenon was confirmed by the experimental results. The finding provides a novel insight for the study of the underlying mechanisms of emodin on antimicrobial activity of A. hydrophila at the molecular level.