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

Fu, Ling-Lin ; Wang, Rui ; Wang, Yanbo ; Lin, Junda

Journal of the science of food and agriculture, 2014-10, Vol.94 (13), p.2630-2638 [Periódico revisado por pares]

Chichester, UK: John Wiley & Sons, Ltd

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Título:
Proteomic identification of responsive proteins of Vibrio parahaemolyticus under high hydrostatic pressure
Autor: Fu, Ling-Lin ; Wang, Rui ; Wang, Yanbo ; Lin, Junda
Assuntos: Activation ; Bacterial Proteins - analysis ; Bacterial Proteins - genetics ; Bacterial Proteins - metabolism ; Blotting, Western ; Cell Membrane - metabolism ; Cell Membrane - ultrastructure ; Cellular ; Databases, Protein ; Electrophoresis ; Food contamination & poisoning ; Food Preservation - methods ; Food processing industry ; Foods ; Gene Expression Regulation, Bacterial ; Gram-negative bacteria ; high hydrostatic pressure (HHP) ; Hydrostatic Pressure ; Microbial Viability ; Microscopy, Electron, Transmission ; Pathogens ; Protein expression ; Proteins ; Proteome - analysis ; Proteome - metabolism ; Proteomics ; Real-Time Polymerase Chain Reaction ; responsive protein ; Reverse Transcriptase Polymerase Chain Reaction ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Stress, Physiological ; Symbols ; Tandem Mass Spectrometry ; Two-Dimensional Difference Gel Electrophoresis ; Vibrio ; Vibrio parahaemolyticus ; Vibrio parahaemolyticus - growth & development ; Vibrio parahaemolyticus - metabolism ; Vibrio parahaemolyticus - ultrastructure
É parte de: Journal of the science of food and agriculture, 2014-10, Vol.94 (13), p.2630-2638
Notas: MS spectra of the 18 identified protein spots
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Descrição: BACKGROUND 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. RESULTS 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. CONCLUSIONS 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. © 2014 Society of Chemical Industry
Editor: Chichester, UK: John Wiley & Sons, Ltd
Idioma: Inglês

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

Fu, Ling-Lin ; Wang, Rui ; Wang, Yanbo ; Lin, Junda

Chichester, UK: John Wiley & Sons, Ltd

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