Biological Functions and Biogenesis of Secreted Bacterial Outer Membrane Vesicles

Kulp, Adam; Kuehn, Meta J.

doi:10.1146/annurev.micro.091208.073413

Cited by 1,169 publications

(1,290 citation statements)

References 86 publications

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“…2a, b). When cultures were starved of nutrients for 16 h, a subpopulation of imaged cells (around 1 %) provided evidence of a novel mechanism of mxOMV production, more complex than merely budding from the outer membrane, as generally proposed for Gram-negative bacteria (Kulp & Kuehn, 2010). Circular structures (protovesicles) with a diameter of 100-200 nm were observed at the surface of several cells (Fig.…”

Section: Microscopy Of Mxomv Productionmentioning

confidence: 58%

“…However, a subset of cells appeared to produce mxOMVs by an alternative mechanism, at specialized cellular structures ('pinches'). Potentially the two processes might result in distinct subpopulations of mxOMVs, as suggested for OMVs of other species (Kulp & Kuehn, 2010). In the majority of cases the peptidoglycan layer appeared perturbed at pinches, and it may be that pinch-mediated mxOMV production occurs at areas of peptidoglycan weakness, a feature of OMV production suggested by other studies (reviewed by Kulp & Kuehn, 2010).…”

Section: A G L Evans and Othersmentioning

confidence: 73%

“…OMVs are roughly spherical membrane-bounded structures, which are selectively laden with hydrolases and metabolites (Kulp & Kuehn, 2010;Whitworth, 2011). For instance, phosphatases (hydrolases that liberate inorganic phosphate from organophosphate molecules) are frequently found in OMVs (e.g.…”

Section: Introductionmentioning

confidence: 99%

“…OMVs can lyse next to Gram-positive cells, releasing their contents next to a target cell. However, they can also fuse directly with the outer membrane of Gram-negative prokaryotes and eukaryotes (Kulp & Kuehn, 2010). The OMVs of Gram-negative bacteria are typically capable of killing other bacteria, leading to their initial description as 'predatory MVs' by Li et al (1998).…”

Section: Introductionmentioning

confidence: 99%

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Predatory activity of Myxococcus xanthus outer-membrane vesicles and properties of their hydrolase cargo

et al. 2012

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The deltaproteobacterium Myxococcus xanthus predates upon members of the soil microbial community by secreting digestive factors and lysing prey cells. Like other Gram-negative bacteria, M. xanthus produces outer membrane vesicles (OMVs), and we show here that M. xanthus OMVs are able to kill Escherichia coli cells. The OMVs of M. xanthus were found to contain active proteases, phosphatases, other hydrolases and secondary metabolites. Alkaline phosphatase activity was found to be almost exclusively associated with OMVs, implying that there is active targeting of phosphatases into OMVs, while other OMV components appear to be packaged passively. The kinetic properties of OMV alkaline phosphatase suggest that there may have been evolutionary adaptation of OMV enzymes to a relatively indiscriminate mode of action, consistent with a role in predation. In addition, the observed regulation of production, and fragility of OMV activity, may protect OMV-producing cells from exploitation by M. xanthus cheating genotypes and/or other competitors. Killing of E. coli by M. xanthus OMVs was enhanced by the addition of a fusogenic enzyme (glyceraldehyde-3-phosphate dehydrogenase; GAPDH), which triggers fusion of vesicles with target membranes within eukaryotic cells. This suggests that the mechanism of prey killing involves OMV fusion with the E. coli outer membrane. M. xanthus secretes GAPDH, which could potentially modulate the fusion of co-secreted OMVs with prey organisms in nature, enhancing their predatory activity.

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Section: Microscopy Of Mxomv Productionmentioning

confidence: 58%

Section: A G L Evans and Othersmentioning

confidence: 73%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Predatory activity of Myxococcus xanthus outer-membrane vesicles and properties of their hydrolase cargo

et al. 2012

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“…OMVs are spherical lipid bilayer blebs with an average diameter of 50-250 nm that are naturally secreted by Gram-negative bacteria [23].…”

Section: Introductionmentioning

confidence: 99%

Towards a non-living vaccine against Shigella flexneri: From the inactivation procedure to protection studies

Camacho

Souza-Rebouças

Irache

et al. 2013

Methods

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Shigellosis is one of the leading causes of diarrhea worldwide with more than 165 million cases annually. Hence, a vaccine against this disease is a priority, but no licensed vaccine is still available. Considering target population as well as intrinsic risks of live attenuated vaccines, non-living strategies appear as the most promising candidates. Remarkably, the preservation of antigenic properties is a major concern since inactivation methods of bacteria affect these qualities. We previously reported the use of a subcellular antigen complex for vaccination against Shigellosis, based on outer membrane vesicles (OMVs) released from Shigella flexneri. Now, we describe in more detail the employment of binary ethylenimine (BEI) for inactivation of Shigella and its subsequent effect on the antigenic conservation of the vaccinal product. Results demonstrate the effectiveness of BEI treatment to completely inactivate Shigella cells without disturbing the antigenicity and immunogenicity of the OMVs. Thus, OMVs harvested after BEI inactivation were able to protect mice against an experimental infection with S. flexneri.

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Structural identification of the lipopolysaccharide‐binding capability of a cupin‐family protein from Helicobacter pylori

Sim

Kim

et al. 2016

FEBS Letters

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We solved the crystal structure of a functionally uncharacterized protein, HP0902, from Helicobacter pylori. Its structure demonstrated an all-β cupin fold that cannot bind metal ions due to the absence of a metal-binding histidine that is conserved in many metallo-cupins. In contrast, isothermal titration calorimetry and NMR titration demonstrated that HP0902 is able to bind bacterial endotoxin lipopolysaccharides (LPS) through its surface-exposed loops, where metal-binding sites are usually found in other metallo-cupins. This report constitutes the first identification of an LPS-interacting protein, both in the cupin family and in H. pylori. Furthermore, identification of the ability of HP0902 to bind LPS uncovers a putative role for this protein in H. pylori pathogenicity.

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Biological Functions and Biogenesis of Secreted Bacterial Outer Membrane Vesicles

Cited by 1,169 publications

References 86 publications

Predatory activity of Myxococcus xanthus outer-membrane vesicles and properties of their hydrolase cargo

Predatory activity of Myxococcus xanthus outer-membrane vesicles and properties of their hydrolase cargo

Towards a non-living vaccine against Shigella flexneri: From the inactivation procedure to protection studies

Structural identification of the lipopolysaccharide‐binding capability of a cupin‐family protein from Helicobacter pylori

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