Salt-responsive outer membrane proteins of Vibrio anguillarum serotype 01 as revealed by comparative proteome analysis

Salt-responsive outer membrane proteins of Vibrio anguillarum serotype 01 as revealed by comparative proteome analysis
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DOI:
10.1111/j.1365-2672.2009.04178.x
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发表时间:
2009-06-01
影响因子:
4
通讯作者:
Chen, W. -J.
Chen, W. -J.
中科院分区:
生物学3区
文献类型:
--
作者:
Kao, D. -Y.;Cheng, Y. -C.;Chen, W. -J.

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目的:鳗弧菌是一种引起弧菌病的普遍海洋病原体。鳗弧菌遇到海水和宿主之间不同的渗透压条件,其外膜蛋白(OMPs)在适应环境变化中发挥着至关重要的作用。本研究采用蛋白质组学方法研究鳗弧菌的盐响应性OMP。方法与结果:较低的盐度(0-85% NaCl)更适合细菌的生长、存活和游动。比较二维电泳(2-DE)分析显示在3个不同盐度下有6个差异表达蛋白点,成功鉴定出它们分别为OmpU、麦芽孔蛋白、鞭毛蛋白B、Omp26La、Omp26La和OmpW。结论:OmpW和OmpU在3-5%盐度下高表达,表明它们在NaCl有效流出中发挥作用。麦芽孔蛋白在较高盐度下下调,表明较高的渗透压抑制碳水化合物转运和细菌生长。 Omp26La 是 OmpV 的同源物,在低盐度下发挥盐胁迫响应蛋白的作用。 研究的意义和影响:据我们所知,这是第一篇利用蛋白质组学方法描述鳗鱼盐胁迫响应蛋白的报告。我们的结果为描述海洋病原体的渗透调节机制提供了有用的策略。
Aims: Vibrio anguillarum is a universal marine pathogen causing vibriosis. Vibrio anguillarum encounters different osmolarity conditions between seawater and hosts, and its outer membrane proteins (OMPs) play a crucial role in the adaptation to changes of the surroundings. In the present study, proteomic approaches were applied to investigate the salt-responsive OMPs of V. anguillarum.Methods and Results: Lower salinity (0-85% NaCl) is more suitable for growth, survival and swimming motility of the bacterium. Comparative two-dimensional electrophoresis (2-DE) analysis reveals six differentially expressed protein spots among three different salinities, which were successfully identified as OmpU, maltoporin, flagellin B, Omp26La, Omp26La and OmpW respectively.Conclusions: OmpW and OmpU were highly expressed at 3-5% salinity, suggesting their role in the efficient efflux of NaCl. Maltoporin was downregulated in higher salinity, indicating that higher osmolarity inhibits carbohydrate transport and bacterial growth. Omp26La, the homologue of OmpV, functions as a salt-responsive protein in lower salinity.Significance and Impact of the Study: To the best of our knowledge, this is the first report describing salt stress-responsive proteins of V. anguillarum using proteomic approaches. Our results provide a useful strategy for delineating the osmoregulatory mechanism of the marine pathogens.