Molecular mechanism of emodin in inhibiting the activity of Aeromonas hydrophila via AtpE

Author:

Zhang Huimin1,Zhou Jun1,Li Xuguang1,Deng Yanfei1,Ge Xianping2,Liu Bo2

Affiliation:

1. Freshwater Fisheries Research Institute of Jiangsu Province Nanjing China

2. Key Laboratory of Freshwater Fisheries and Germplasm Resources Utilization Ministry of Agriculture, Freshwater Fisheries Research Center, Chinese Academy of Fishery Sciences Wuxi China

Abstract

AbstractObjectiveAeromonas hydrophila, a leading pathogen of aquatic organisms, poses a significant challenge in terms of effective and safe inhibition.MethodsThrough the method of experiments and molecular simulations, we discovered that emodin effectively inhibits the A. hydrophila via the binding of emodin with AtpE (ATP synthase subunit C). Bacterial inhibition experiments show that emodin effectively inhibits the activity and growth of A. hydrophila.ResultFurther molecular docking and molecular dynamics simulation revealed that emodin binds directly to AtpE. More specifically, it binds to certain residues of AtpE, including TYR73, LEU70, ALA13, TYR10, MET17, and ALA14, ultimately leading to inhibition of activity.ConclusionConsequently, our discovery sheds new light on exploring the molecular mechanism through which emodin displays antimicrobial activity against A. hydrophila.

Funder

Jiangsu Agriculture Research System

National Natural Science Foundation of China

Publisher

Wiley

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