scholarly journals Interspecies Outer Membrane Vesicles (OMVs) Modulate the Sensitivity of Pathogenic Bacteria and Pathogenic Yeasts to Cationic Peptides and Serum Complement

2019 ◽  
Vol 20 (22) ◽  
pp. 5577 ◽  
Author(s):  
Justyna Roszkowiak ◽  
Paweł Jajor ◽  
Grzegorz Guła ◽  
Jerzy Gubernator ◽  
Andrzej Żak ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Pathogenic Bacteria ◽  
Membrane Vesicles ◽  
Polymyxin B ◽  
Outer Membrane Vesicles ◽  
Antifungal Drugs ◽  
Cationic Peptides ◽  
Serum Complement ◽  
Fungicidal Action ◽  
Potential Measurement

The virulence of bacterial outer membrane vesicles (OMVs) contributes to innate microbial defense. Limited data report their role in interspecies reactions. There are no data about the relevance of OMVs in bacterial-yeast communication. We hypothesized that model Moraxella catarrhalis OMVs may orchestrate the susceptibility of pathogenic bacteria and yeasts to cationic peptides (polymyxin B) and serum complement. Using growth kinetic curve and time-kill assay we found that OMVs protect Candida albicans against polymyxin B-dependent fungicidal action in combination with fluconazole. We showed that OMVs preserve the virulent filamentous phenotype of yeasts in the presence of both antifungal drugs. We demonstrated that bacteria including Haemophilus influenza, Acinetobacter baumannii, and Pseudomonas aeruginosa coincubated with OMVs are protected against membrane targeting agents. The high susceptibility of OMV-associated bacteria to polymyxin B excluded the direct way of protection, suggesting rather the fusion mechanisms. High-performance liquid chromatography-ultraviolet spectroscopy (HPLC-UV) and zeta-potential measurement revealed a high sequestration capacity (up to 95%) of OMVs against model cationic peptide accompanied by an increase in surface electrical charge. We presented the first experimental evidence that bacterial OMVs by sequestering of cationic peptides may protect pathogenic yeast against combined action of antifungal drugs. Our findings identify OMVs as important inter-kingdom players.

scholarly journals Antibiotic-Mediated Modulations of Outer Membrane Vesicles in Enterohemorrhagic Escherichia coli O104:H4 and O157:H7

2017 ◽  
Vol 61 (9) ◽  
Author(s):  
Andreas Bauwens ◽  
Lisa Kunsmann ◽  
Helge Karch ◽  
Alexander Mellmann ◽  
Martina Bielaszewska
Keyword(s):  
Escherichia Coli ◽  
Outer Membrane ◽  
Shiga Toxin ◽  
Membrane Vesicles ◽  
Polymyxin B ◽  
Outer Membrane Vesicles ◽  
Enterohemorrhagic Escherichia Coli ◽  
Content Type ◽  
E Coli ◽  
Major Virulence Factor

ABSTRACT Ciprofloxacin, meropenem, fosfomycin, and polymyxin B strongly increase production of outer membrane vesicles (OMVs) in Escherichia coli O104:H4 and O157:H7. Ciprofloxacin also upregulates OMV-associated Shiga toxin 2a, the major virulence factor of these pathogens, whereas the other antibiotics increase OMV production without the toxin. These two effects might worsen the clinical outcome of infections caused by Shiga toxin-producing E. coli. Our data support the existing recommendations to avoid antibiotics for treatment of these infections.

scholarly journals Lipidomic Analysis of the Outer Membrane Vesicles from Paired Polymyxin-Susceptible and -Resistant Klebsiella pneumoniae Clinical Isolates

2018 ◽  
Vol 19 (8) ◽  
pp. 2356 ◽  
Author(s):  
Raad Jasim ◽  
Mei-Ling Han ◽  
Yan Zhu ◽  
Xiaohan Hu ◽  
Maytham Hussein ◽  
...  
Keyword(s):  
Klebsiella Pneumoniae ◽  
Outer Membrane ◽  
Membrane Vesicles ◽  
Average Diameter ◽  
Polymyxin B ◽  
Outer Membrane Vesicles ◽  
Resistant Isolate ◽  
Average Particle ◽  
Lipid Species ◽  
The Impact

Gram-negative bacteria produce outer membrane vesicles (OMVs) as delivery vehicles for nefarious bacterial cargo such as virulence factors, which are antibiotic resistance determinants. This study aimed to investigate the impact of polymyxin B treatment on the OMV lipidome from paired polymyxin-susceptible and -resistant Klebsiella pneumoniae isolates. K. pneumoniae ATCC 700721 was employed as a reference strain in addition to two clinical strains, K. pneumoniae FADDI-KP069 and K. pneumoniae BM3. Polymyxin B treatment of the polymyxin-susceptible strains resulted in a marked reduction in the glycerophospholipid, fatty acid, lysoglycerophosphate and sphingolipid content of their OMVs. Conversely, the polymyxin-resistant strains expressed OMVs richer in all of these lipid species, both intrinsically and increasingly under polymyxin treatment. The average diameter of the OMVs derived from the K. pneumoniae ATCC 700721 polymyxin-susceptible isolate, measured by dynamic light scattering measurements, was ~90.6 nm, whereas the average diameter of the OMVs isolated from the paired polymyxin-resistant isolate was ~141 nm. Polymyxin B treatment (2 mg/L) of the K. pneumoniae ATCC 700721 cells resulted in the production of OMVs with a larger average particle size in both the susceptible (average diameter ~124 nm) and resistant (average diameter ~154 nm) strains. In light of the above, we hypothesize that outer membrane remodelling associated with polymyxin resistance in K. pneumoniae may involve fortifying the membrane structure with increased glycerophospholipids, fatty acids, lysoglycerophosphates and sphingolipids. Putatively, these changes serve to make the outer membrane and OMVs more impervious to polymyxin attack.

Outer membrane vesicles from pathogenic bacteria initiate an inflammatory response in human endothelial cells

2013 ◽  
Vol 184 (1) ◽  
pp. 458-466 ◽  
Author(s):  
Michael C. Soult ◽  
Natalie E. Lonergan ◽  
Bhairav Shah ◽  
Woong-Ki Kim ◽  
L.D. Britt ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Inflammatory Response ◽  
Outer Membrane ◽  
Pathogenic Bacteria ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Human Endothelial Cells

scholarly journals The Role of Porphyromonas gingivalis Outer Membrane Vesicles in Periodontal Disease and Related Systemic Diseases

2021 ◽  
Vol 10 ◽  
Author(s):  
Zhiying Zhang ◽  
Dongjuan Liu ◽  
Sai Liu ◽  
Shuwei Zhang ◽  
Yaping Pan
Keyword(s):  
Periodontal Disease ◽  
Outer Membrane ◽  
Porphyromonas Gingivalis ◽  
Pathogenic Bacteria ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Systemic Diseases ◽  
Alcoholic Fatty Liver ◽  
New Ideas

Periodontal disease is a chronic infectious disease associated with a variety of bacteria, which can cause damage to the periodontal support structure and affect a variety of systemic system diseases such as cancer, cardiovascular disease, diabetes, rheumatoid arthritis, non-alcoholic fatty liver, and Alzheimer’s disease. Porphyromonas gingivalis (P. gingivalis) is the most important pathogenic bacteria for periodontal disease. It can produce outer membrane vesicles (OMVs) and release them into the environment, playing an important role in its pathogenesis. This article focuses on P. gingivalis OMVs, reviews its production and regulation, virulence components, mode of action and related diseases, with a view to providing new ideas for the prevention and treatment of diseases related to P. gingivalis infections.

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 Rotation of Vibrio fischeri Flagella Produces Outer Membrane Vesicles That Induce Host Development

2016 ◽  
Vol 198 (16) ◽  
pp. 2156-2165 ◽  
Author(s):  
Marie-Stephanie Aschtgen ◽  
Jonathan B. Lynch ◽  
Eric Koch ◽  
Julia Schwartzman ◽  
Margaret McFall-Ngai ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Pathogenic Bacteria ◽  
Vibrio Fischeri ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Surface Epithelium ◽  
Light Organ ◽  
Present Evidence ◽  
Content Type ◽  
Host Development

ABSTRACTUsing the squid-vibrio association, we aimed to characterize the mechanism through whichVibrio fischericells signal morphogenesis of the symbiotic light-emitting organ. The symbiont releases two cell envelope molecules, peptidoglycan (PG) and lipopolysaccharide (LPS) that, within 12 h of light organ colonization, act in synergy to trigger normal tissue development. Recent work has shown that outer membrane vesicles (OMVs) produced byV. fischeriare sufficient to induce PG-dependent morphogenesis; however, the mechanism(s) of OMV release by these bacteria has not been described. Like several genera of both beneficial and pathogenic bacteria,V. fischericells elaborate polar flagella that are enclosed by an extension of the outer membrane, whose function remains unclear. Here, we present evidence that along with the well-recognized phenomenon of blebbing from the cell's surface, rotation of this sheathed flagellum also results in the release of OMVs. In addition, we demonstrate that most of the development-inducing LPS is associated with these OMVs and that the presence of the outer membrane protein OmpU but not the LPS O antigen on these OMVs is important in triggering normal host development. These results also present insights into a possible new mechanism of LPS release by pathogens with sheathed flagella.IMPORTANCEDetermining the function(s) of sheathed flagella in bacteria has been challenging, because no known mutation results only in the loss of this outer membrane-derived casing. Nevertheless, the presence of a sheathed flagellum in such host-associated genera asVibrio,Helicobacter, andBrucellahas led to several proposed functions, including physical protection of the flagella and masking of their immunogenic flagellins. Using the squid-vibrio light organ symbiosis, we demonstrate another role, that ofV. fischericells require rotating flagella to induce apoptotic cell death within surface epithelium, which is a normal step in the organ's development. Further, we present evidence that this rotation releases apoptosis-triggering lipopolysaccharide in the form of outer membrane vesicles. Such release may also occur by pathogens but with different outcomes for the host.

scholarly journals Outer membrane vesicles displaying engineered glycotopes elicit protective antibodies

2016 ◽  
Vol 113 (26) ◽  
pp. E3609-E3618 ◽  
Author(s):  
Linxiao Chen ◽  
Jenny L. Valentine ◽  
Chung-Jr Huang ◽  
Christine E. Endicott ◽  
Tyler D. Moeller ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Pathogenic Bacteria ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Protective Antibodies ◽  
Vaccine Potential ◽  
Glycoconjugate Vaccines ◽  
Alternative Methodology ◽  
Protection Against Infection ◽  
Schu S4

The O-antigen polysaccharide (O-PS) component of lipopolysaccharides on the surface of gram-negative bacteria is both a virulence factor and a B-cell antigen. Antibodies elicited by O-PS often confer protection against infection; therefore, O-PS glycoconjugate vaccines have proven useful against a number of different pathogenic bacteria. However, conventional methods for natural extraction or chemical synthesis of O-PS are technically demanding, inefficient, and expensive. Here, we describe an alternative methodology for producing glycoconjugate vaccines whereby recombinant O-PS biosynthesis is coordinated with vesiculation in laboratory strains ofEscherichia colito yield glycosylated outer membrane vesicles (glycOMVs) decorated with pathogen-mimetic glycotopes. Using this approach, glycOMVs corresponding to eight different pathogenic bacteria were generated. For example, expression of a 17-kb O-PS gene cluster from the highly virulentFrancisella tularensissubsp.tularensis(type A) strain Schu S4 in hypervesiculatingE. colicells yielded glycOMVs that displayedF. tularensisO-PS. Immunization of BALB/c mice with glycOMVs elicited significant titers of O-PS–specific serum IgG antibodies as well as vaginal and bronchoalveolar IgA antibodies. Importantly, glycOMVs significantly prolonged survival upon subsequent challenge withF. tularensisSchu S4 and provided complete protection against challenge with two differentF. tularensissubsp.holarctica(type B) live vaccine strains, thereby demonstrating the vaccine potential of glycOMVs. Given the ease with which recombinant glycotopes can be expressed on OMVs, the strategy described here could be readily adapted for developing vaccines against many other bacterial pathogens.

scholarly journals A novel decoy strategy for polymyxin resistance in Acinetobacter baumannii

eLife ◽  
2021 ◽  
Vol 10 ◽  
Author(s):  
Jaeeun Park ◽  
Misung Kim ◽  
Bora Shin ◽  
Mingyeong Kang ◽  
Jihye Yang ◽  
...  
Keyword(s):  
Acinetobacter Baumannii ◽  
Outer Membrane ◽  
Galleria Mellonella ◽  
Membrane Vesicles ◽  
Polymyxin B ◽  
Outer Membrane Vesicles ◽  
Clinical Isolates ◽  
Infection Model ◽  
Taxonomic Profiling

Modification of the outer membrane charge by a polymyxin B (PMB)-induced PmrAB two-component system appears to be a dominant phenomenon in PMB-resistant Acinetobacter baumannii. PMB-resistant variants and many clinical isolates also appeared to produce outer membrane vesicles (OMVs). Genomic, transcriptomic, and proteomic analyses revealed that upregulation of the pmr operon and decreased membrane-linkage proteins (OmpA, OmpW and BamE) are linked to overproduction of OMVs, which also promoted enhanced biofilm formation. The addition of OMVs from PMB-resistant variants into the cultures of PMB-susceptible A. baumannii and the clinical isolates protected these susceptible bacteria from PMB. Taxonomic profiling of in vitro human gut microbiomes under anaerobic conditions demonstrated that OMVs completely protected the microbial community against PMB treatment. A Galleria mellonella-infection model with PMB treatment showed that OMVs increased the mortality rate of larvae by protecting A. baumannii from PMB. Taken together, OMVs released from A. baumannii functioned as decoys against PMB.

scholarly journals Xanthomonas campestris pv. vesicatoria Secretes Proteases and Xylanases via the Xps Type II Secretion System and Outer Membrane Vesicles

2015 ◽  
Vol 197 (17) ◽  
pp. 2879-2893 ◽  
Author(s):  
Magali Solé ◽  
Felix Scheibner ◽  
Anne-Katrin Hoffmeister ◽  
Nadine Hartmann ◽  
Gerd Hause ◽  
...  
Keyword(s):  
Outer Membrane ◽  
Xanthomonas Campestris ◽  
Pathogenic Bacteria ◽  
Membrane Vesicles ◽  
Outer Membrane Vesicles ◽  
Type Ii Secretion ◽  
Type Ii ◽  
Content Type ◽  
Plant Pathogenic Bacteria ◽  
Extracellular Milieu

ABSTRACTMany plant-pathogenic bacteria utilize type II secretion (T2S) systems to secrete degradative enzymes into the extracellular milieu. T2S substrates presumably mediate the degradation of plant cell wall components during the host-pathogen interaction and thus promote bacterial virulence. Previously, the Xps-T2S system fromXanthomonas campestrispv. vesicatoria was shown to contribute to extracellular protease activity and the secretion of a virulence-associated xylanase. The identities and functions of additional T2S substrates fromX. campestrispv. vesicatoria, however, are still unknown. In the present study, the analysis of 25 candidate proteins fromX. campestrispv. vesicatoria led to the identification of two type II secreted predicted xylanases, a putative protease and a lipase which was previously identified as a virulence factor ofX. campestrispv. vesicatoria. Studies with mutant strains revealed that the identified xylanases and the protease contribute to virulence andin plantagrowth ofX. campestrispv. vesicatoria. When analyzed in the related pathogenX. campestrispv. campestris, several T2S substrates fromX. campestrispv. vesicatoria were secreted independently of the T2S systems, presumably because of differences in the T2S substrate specificities of the two pathogens. Furthermore, inX. campestrispv. vesicatoria T2S mutants, secretion of T2S substrates was not completely absent, suggesting the contribution of additional transport systems to protein secretion. In line with this hypothesis, T2S substrates were detected in outer membrane vesicles, which were frequently observed forX. campestrispv. vesicatoria. We, therefore, propose that extracellular virulence-associated enzymes fromX. campestrispv. vesicatoria are targeted to the Xps-T2S system and to outer membrane vesicles.IMPORTANCEThe virulence of plant-pathogenic bacteria often depends on TS2 systems, which secrete degradative enzymes into the extracellular milieu. T2S substrates are being studied in several plant-pathogenic bacteria, includingXanthomonas campestrispv. vesicatoria, which causes bacterial spot disease in tomato and pepper. Here, we show that the T2S system fromX. campestrispv. vesicatoria secretes virulence-associated xylanases, a predicted protease, and a lipase. Secretion assays with the related pathogenX. campestrispv. campestris revealed important differences in the T2S substrate specificities of the two pathogens. Furthermore, electron microscopy showed that T2S substrates fromX. campestrispv. vesicatoria are targeted to outer membrane vesicles (OMVs). Our results, therefore, suggest that OMVs provide an alternative transport route for type II secreted extracellular enzymes.

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