文献类型： 外文期刊

作者： Che, Jinyuan ¹ ; Fang, Qitong ² ; Hu, Shaojie ² ; Liu, Binghong ² ; Wang, Lei ¹ ; Fang, Xiu ³ ; Li, Lekang ⁴ ; Luo, Tuyan ⁵ ; Bao, Baolong ² ;

作者机构： 1.Tongji Univ, Coll Environm Sci & Engn, Key Lab Yangtze River Water Environm, Minist Educ, Shanghai 200092, Peoples R China

2.Shanghai Ocean Univ, Natl Demonstrat Ctr Expt Fisheries Sci Educ, Key Lab Explorat & Utilizat Aquat Genet Resources, Minist Educ, Shanghai 201306, Peoples R China

3.Fujian Prov Key Lab Breeding Lateolabrax Japonicus, Fuding 355200, Peoples R China

4.Jiujiang Acad Fishery Sci, Jiujiang 332000, Peoples R China

5.Fujian Acad Agr Sci, Inst Qual Stand & Testing Technol Agroprod, Fuzhou 350003, Peoples R China

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 ）

ISSN：

年卷期： 2024 年 13 卷 7 期

页码：

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.