Journal Highlight: Proteomic identification of responsive proteins of Vibrio parahaemolyticus under high hydrostatic pressure

Skip to Navigation

Ezine

  • Published: Oct 27, 2014
  • Author: spectroscopyNOW
  • Channels: Proteomics
thumbnail image: Journal Highlight: Proteomic identification of responsive proteins of <em>Vibrio parahaemolyticus</em> under high hydrostatic pressure
Proteome profiles were performed to determine the effects of high hydrostatic pressure on the food pathogen Vibrio parahaemolyticus ATCC 17802 in order to understand how it responds to mechanical stress injury.



Proteomic identification of responsive proteins of Vibrio parahaemolyticus under high hydrostatic pressure

Journal of the Science of Food and Agriculture, 2014, 94, 2630-2638
Ling-Lin Fu, Rui Wang, Yanbo Wang and Junda Lin

Abstract: High hydrostatic pressure (HHP) processing is currently being used as a treatment for certain foods to inhibit spoilage organisms and control the presence of foodborne pathogens. In this study proteome profiles were performed by two-dimensional gel electrophoresis (2-DE) coupled with MALDI-TOF/TOF identification to determine the effects of HHP (50, 100, 150 and 200 MPa, each for 10 min) on Vibrio parahaemolyticus ATCC 17802 (∼8 log CFU mL−1) in order to understand how it responds to mechanical stress injury. Multiple comparisons of 2-DE revealed that the majority of changes in protein abundance occurred in a pressure-dependent fashion. A total of 18 differentially expressed protein spots were successfully identified by MALDI-TOF/TOF analysis. Moreover, quantitative RT-PCR and immunoblotting also substantiated the changes of transcriptional and translational levels of representative proteins. Our results suggested that V. parahaemolyticus may respond to HHP treatment through suppression of membrane stability and functionality (PfaC, Alr2, MltA, PLA2 and PatH), depression of biosynthesis and cellular processes (NadB, PyrB and ArgB), decreased levels of transcription (RpoD) and translation (RpsA, RplJ and PheS), and effective activation of protein folding and stress-related elements (GroES, DnaK and GroEL). This study may provide insight into the nature of the cellular targets of high pressure and in high-pressure resistance mechanisms in V. parahaemolyticus.

  • This paper is free to view for all users registered on spectroscopyNOW.com until the end of November 2014.
    After this time, you can purchase it using Pay-Per-View on Wiley Online Library.

Social Links

Share This Links

Bookmark and Share

Microsites

Suppliers Selection
Societies Selection

Banner Ad

Click here to see
all job opportunities

Copyright Information

Interested in separation science? Visit our sister site separationsNOW.com

Copyright © 2017 John Wiley & Sons, Inc. All Rights Reserved