Proteomic Characterization of the Outer Membrane Vesicle of Pseudomonas putida KT2440

Outer membrane vesicles (OMVs) are produced by various pathogenic Gram-negative bacteria such as Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii. In this study, we isolated OMVs from a representative soil bacterium, Pseudomonas putida KT2440, which has a biodegradative activity...

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Bibliographic Details
Published in:Journal of proteome research 2014-10, Vol.13 (10), p.4298-4309
Main Authors: Choi, Chi-Won, Park, Edmond Changkyun, Yun, Sung Ho, Lee, Sang-Yeop, Lee, Yeol Gyun, Hong, Yeonhee, Park, Kyeong Ryang, Kim, Sang-Hyun, Kim, Gun-Hwa, Kim, Seung Il
Format: Article
Language:English
Subjects:
Apoptosis
Bacterial Outer Membrane Proteins - metabolism
Cell Line
Chromatography, Liquid
Humans
Microscopy, Electron, Transmission
Proteomics
Pseudomonas putida - metabolism
Subcellular Fractions - metabolism
Tandem Mass Spectrometry
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Summary:Outer membrane vesicles (OMVs) are produced by various pathogenic Gram-negative bacteria such as Escherichia coli, Pseudomonas aeruginosa, and Acinetobacter baumannii. In this study, we isolated OMVs from a representative soil bacterium, Pseudomonas putida KT2440, which has a biodegradative activity toward various aromatic compounds. Proteomic analysis identified the outer membrane proteins (OMPs) OprC, OprD, OprE, OprF, OprH, OprG, and OprW as major components of the OMV of P. putida KT2440. The production of OMVs was dependent on the nutrient availability in the culture media, and the up- or down-regulation of specific OMPs was observed according to the culture conditions. In particular, porins (e.g., benzoate-specific porin, BenF-like porin) and enzymes (e.g., catechol 1,2-dioxygenase, benzoate dioxygenase) for benzoate degradation were uniquely found in OMVs prepared from P. putida KT2440 that were cultured in media containing benzoate as the energy source. OMVs of P. putida KT2440 showed low pathological activity toward cultured cells that originated from human lung cells, which suggests their potential as adjuvants or OMV vaccine carriers. Our results suggest that the protein composition of the OMVs of P. putida KT2440 reflects the characteristics of the total proteome of P. putida KT2440.
ISSN:1535-3893
1535-3907
DOI:10.1021/pr500411d