scholarly journals Global proteomic profiling of native outer membrane vesicles derived fromEscherichia coli

PROTEOMICS ◽  
2007 ◽  
Vol 7 (20) ◽  
pp. 3821-3821
Author(s):  
Eun-Young Lee ◽  
Joo Young Bang ◽  
Gun Wook Park ◽  
Dong-Sic Choi ◽  
Ji Seoun Kang ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Proteomic Profiling ◽  
Fromescherichia Coli

Global proteomic profiling of native outer membrane vesicles derived from Escherichia coli

PROTEOMICS ◽  
2007 ◽  
Vol 7 (17) ◽  
pp. 3143-3153 ◽  
Author(s):  
Eun-Young Lee ◽  
Joo Young Bang ◽  
Gun Wook Park ◽  
Dong-Sic Choi ◽  
Ji Seoun Kang ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Proteomic Profiling

scholarly journals Comprehensive proteomic profiling of outer membrane vesicles from Campylobacter jejuni

2014 ◽  
Vol 98 ◽  
pp. 90-98 ◽  
Author(s):  
Kyoung-Soon Jang ◽  
Michael J. Sweredoski ◽  
Robert L.J. Graham ◽  
Sonja Hess ◽  
William M. Clemons
Keyword(s):  
Outer Membrane ◽  
Campylobacter Jejuni ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Proteomic Profiling

scholarly journals Influence of Environmental and Genetic Factors on Proteomic Profiling of Outer Membrane Vesicles from Campylobacter jejuni

2019 ◽  
Vol 68 (2) ◽  
pp. 255-261 ◽  
Author(s):  
RENATA GODLEWSKA ◽  
JOANNA KLIM ◽  
JANUSZ DĘBSKI ◽  
AGNIESZKA WYSZYŃSKA ◽  
ANNA ŁASICA
Keyword(s):  
Outer Membrane ◽  
Flagellar Apparatus ◽  
Membrane Vesicles ◽  
Fold Increase ◽  
Polymyxin B ◽  
Outer Membrane Vesicles ◽  
Proteomic Profiling ◽  
Cell Compartments ◽  
Common Group ◽  
Quantitative Changes

The proteomes of outer membrane vesicles (OMVs) secreted by C. jejuni 81–176 strain, which was exposed to oxygen or antibiotic stress (polymyxin B), were characterized. We also assessed the OMVs production and their content in two mutated strains – ∆dsbI and ∆htrA. OMVs production was significantly increased under the polymyxin B stress and remained unaltered in all other variants. Interestingly, the qualitative load of OMVs was constant regardless of the stress conditions or genetic background. However, certain proteins exhibited notable quantitative changes, ranging from 4-fold decrease to 10-fold increase. Up- or downregulated proteins (e.g. major outer membrane protein porA, iron ABC transporter, serine protease- htrA, 60 kDa chaperonin-groL, enolase) represented various cell compartments (cytoplasm, periplasm, and membrane) and exhibited various functions; nevertheless, one common group was noted that consisted of components of flagellar apparatus, i.e., FlaA/B, FlgC/E, which were mostly upregulated. Some of these proteins are the putative substrates of DsbI protein. Further investigation of the regulation of C. jejuni OMVs composition and their role in virulence will allow a better understanding of the infectious process of C. jejuni.

Electrophysiological Characterization of Transport Across Outer Membrane Channels from Gram-Negative Bacteria in Their Native Environment

2019 ◽  
Author(s):  
Jiajun Wang ◽  
Rémi Terrasse ◽  
Jayesh Arun Bafna ◽  
Lorraine Benier ◽  
Mathias Winterhalter
Keyword(s):  
Outer Membrane ◽  
Lipid Membrane ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Multi Drug Resistance ◽  
Gram Negative Bacteria ◽  
Membrane Channels ◽  
Gram Negative ◽  
Electrophysiological Characterization

Multi-drug resistance in Gram-negative bacteria is often associated with low permeability of the outer membrane. To investigate the role of membrane channels in the uptake of antibiotics, we extract, purify and reconstitute them into artificial planar membranes. To avoid this time-consuming procedure, here we show a robust approach using fusion of native outer membrane vesicles (OMV) into planar lipid bilayer which moreover allows also to some extend the characterization of membrane protein channels in their native environment. Two major membrane channels from <i>Escherichia coli</i>, OmpF and OmpC, were overexpressed from the host and the corresponding OMVs were collected. Each OMV fusion revealed surprisingly single or only few channel activities. The asymmetry of the OMV´s translates after fusion into the lipid membrane with the LPS dominantly present at the side of OMV addition. Compared to conventional reconstitution methods, the channels fused from OMVs containing LPS have similar conductance but a much broader distribution. The addition of Enrofloxacin on the LPS side yields somewhat higher association (<i>k<sub>on</sub></i>) and lower dissociation (<i>k<sub>off</sub></i>) rates compared to LPS-free reconstitution. We conclude that using outer membrane vesicles is a fast and easy approach for functional and structural studies of membrane channels in the native membrane.

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