The Impact of Vp-Porin, an Outer Membrane Protein, on the Biological Characteristics and Virulence of Vibrio Parahaemolyticus

文献类型： 外文期刊

第一作者： Che, Jinyuan

作者： Che, Jinyuan;Wang, Lei;Fang, Qitong;Hu, Shaojie;Liu, Binghong;Bao, Baolong;Fang, Xiu;Li, Lekang;Luo, Tuyan

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关键词： Vibrio parahaemolyticus; Vp-porin; antimicrobial resistance; motility; virulence

期刊名称：BIOLOGY-BASEL （ 影响因子：3.6； 五年影响因子：3.8 ）

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年卷期： 2024 年 13 卷 7 期

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收录情况： SCI

摘要： The increasing antibiotic resistance of Vibrio parahaemolyticus (V. parahaemolyticus), a critical halophilic pathogen, has become a significant concern, highlighting the need for a deeper understanding of the molecular mechanisms governing bacterial drug resistance in V. parahaemolyticus. Porins, essential proteins located in the outer membrane, play a direct role in influencing antimicrobial resistance mechanisms in bacteria. This study aimed to characterize a novel porin and evaluate its role in antimicrobial resistance by constructing a deletion mutant (triangle Vp-porin). The results showed that triangle Vp-porin exhibited impaired membrane integrity and increased susceptibility to certain antibiotics. Furthermore, the motility of triangle Vp-porin was impaired, and its virulence was attenuated, as assessed by Tetrahymena. These findings demonstrate the significant role of Vp-porin in modulating antimicrobial resistance and bacterial virulence. Porins are crucial proteins located in the outer membrane that directly influence antimicrobial resistance mechanisms and virulence in bacteria. In this study, a porin gene (Vp-porin) was cloned in V. parahaemolyticus, and the function of Vp-Porin in biological characteristics and virulence was investigated. The results of sequence analysis showed that Vp-Porin is highly conserved in Vibrio spp., and the predicted 3D structure showed it could form a 20-strand transmembrane beta-barrel domian. Membrane permeabilization provides evidence that the membrane integrity of triangle Vp-porin was damaged and the sensitivity to tetracycline, polymyxin B, rifampicin and cephalothin of triangle Vp-porin obviously increased. In addition, loss of Vp-porin damaged motility due to downregulated flagellar synthesis. In addition, triangle Vp-porin exhibited attenuated cytotoxicity to Tetrahymena. The relative survival rate of Tetrahymena infection with triangle Vp-porin was 86%, which is much higher than that with WT (49%). Taken together, the results of this study indicate that Vp-Porin in V. parahaemolyticus plays various roles in biological characteristics in membrane integrity, antimicrobial resistance and motility and contributes to virulence.

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