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 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 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.

scholarly journals Campylobacter jejuni Outer Membrane Vesicles Play an Important Role in Bacterial Interactions with Human Intestinal Epithelial Cells

2012 ◽  
Vol 80 (12) ◽  
pp. 4089-4098 ◽  
Author(s):  
Abdi Elmi ◽  
Eleanor Watson ◽  
Pamela Sandu ◽  
Ozan Gundogdu ◽  
Dominic C. Mills ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Campylobacter Jejuni ◽  
Virulence Factors ◽  
Intestinal Epithelial Cells ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Host Cells ◽  
Intestinal Epithelial ◽  
Secretion Systems ◽  
Content Type

ABSTRACTCampylobacter jejuniis the most prevalent cause of food-borne gastroenteritis in the developed world; however, the molecular basis of pathogenesis is unclear. Secretion of virulence factors is a key mechanism by which enteric bacterial pathogens interact with host cells to enhance survival and/or damage the host. However,C. jejunilacks the virulence-associated secretion systems possessed by other enteric pathogens. Many bacterial pathogens utilize outer membrane vesicles (OMVs) for delivery of virulence factors into host cells. In the absence of prototypical virulence-associated secretion systems, OMVs could be an important alternative for the coordinated delivery ofC. jejuniproteins into host cells. Proteomic analysis ofC. jejuni11168H OMVs identified 151 proteins, including periplasmic and outer membrane-associated proteins, but also many determinants known to be important in survival and pathogenesis, including the cytolethal distending toxin (CDT).C. jejuniOMVs contained 16N-linked glycoproteins, indicating a delivery mechanism by which these periplasm-located yet immunogenic glycoproteins can interact with host cells.C. jejuniOMVs possess cytotoxic activity and induce a host immune response from T84 intestinal epithelial cells (IECs), which was not reduced by OMV pretreatment with proteinase K or polymyxin B prior to coincubation with IECs. Pretreatment of IECs with methyl-beta-cyclodextrin partially blocks OMV-induced host immune responses, indicating a role for lipid rafts in host cell plasma membranes during interactions withC. jejuniOMVs. OMVs isolated from aC. jejuni11168HcdtAmutant induced interleukin-8 (IL-8) to the same extent as did wild-type OMVs, suggesting OMV induction of IL-8 is independent of CDT.

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