Proteomic analysis on the expression of outer membrane proteins of Vibrio alginolyticus at different sodium concentrations

Abstract

The ability of osmoregulation is crucial to marine pathogens that always face the change of osmotic pressure when they shift between natural marine water-bodies and hosts. Previous studies indicated that the expressional patterns of outer membrane proteins (OMPs) changed when Gram-negative bacteria were transferred in different environments. In the present study, proteomic methodologies were used to investigate the expressional pattern of OMPs of Vibrio alginolyticus, a universal marine pathogen, at different Na(+) concentrations. OmpW, OmpV, and Omp TolC were determined to be osmotic stress responsive proteins. Of the three proteins, importantly, OmpV and OmpW showed distinctly reverse changes to each other, indicating that the two proteins might be the two components varied with changed NaCl concentrations. In addition, our results suggest that closely related species of bacteria with available whole genomic databases should be applied after item microorganism species was used when proteins from a bacterium with unavailable whole genomic information were identified by PMF. Therefore, our results not only expand our knowledge on osmotic stress responsive proteins, but also provide valuable information for strategies on screening of these proteins.

Salinity and Temperature Effects on Physiological Responses of Vibrio fischeri from Diverse Ecological Niches

“…Studying the microbial growth of marine symbionts constantly experiencing shifts between marine free-living and host phases is critical since the osmotic pressure can change dramatically between these two environments [30,31]. This subject definitely needs to be addressed with the remarkable illumination in recent years that virulence and osmoregulation possess links within pathogenic Vibrio species [32].…”

A Comprehensive Proteomics and Transcriptomics Analysis ofBacillus subtilisSalt Stress Adaptation

“…However, no study has yet addressed the changes in the membrane proteome of salt-stressed B. subtilis cells in a quantitative manner. Furthermore, quantitative studies investigating salt-induced changes in a prokaryotic membrane proteome are generally rare (6,22,31,67,68). For these reasons, we designed an experimental strategy that combined quantitative shotgun proteomics for the analysis of both the cytosolic and the cytoplasmic membrane proteome with wholegenome microarray data to profile in a time-dependent fashion the physiological adaptation of B. subtilis to a sudden and strong osmotic upshift.…”

Role of the Carboxy Terminus of SecA in Iron Acquisition, Protein Translocation, and Virulence of the Bacterial Pathogen Acinetobacter baumannii

“…All these are bona fide outer membrane proteins, a cellular location that requires the activity of the Sec protein secretion system. The reduction in the production of OmpW, which might act like OmpF in osmotic stress responses as seen in Vibrio alginolyticus growing at different NaCl concentrations (56), could contribute to the significantly reduced growth of the 2010 mutant compared with the ATCC 19606 T parental strain after incubation in LB broth containing 500 mM NaCl for 4 h (P Յ 0.05) or 750 mM NaCl for 3 h (P Յ 0.01) (Fig. 7).…”