Comparative Proteome Analysis of Spontaneous Outer Membrane Vesicles and Purified Outer Membranes of Neisseria meningitidis

Lappann, Martin; Otto, Andreas; Becher, Dörte; Vogel, Ulrich

doi:10.1128/jb.00625-13

Cited by 102 publications

(100 citation statements)

References 62 publications

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“…For instance, deletion of DegP, a periplasmic protease/chaperone that controls envelope stress caused by the presence of misfolded proteins, results in a hypervesiculation phenotype (31,54). Moreover, disruption of connections between the outer and inner membranes and the peptidoglycan increases OMV production (33,41,50,55,56). Although X. fastidiosa harbors a degP ortholog (PD0231/XF0285) that is up-regulated upon heat shock (57), its expression does not appear to be RpfF-dependent (14).…”

Section: Discussionmentioning

confidence: 99%

Xylella fastidiosa outer membrane vesicles modulate plant colonization by blocking attachment to surfaces

Ionescu

Zaini

Baccari

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

138

140

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Significance Release of outer membrane vesicles (OMVs) is a general feature of Gram-negative bacteria. Most studies have addressed the mechanisms of their formation or the cargo they can carry, but other roles remain to be explored further. Here we provide evidence for a novel role for OMVs in Xylella fastidiosa , a bacterial pathogen that colonizes the xylem of important crop plants. OMVs, whose production is suppressed by a quorum-sensing system, serve as an autoinhibitor of cell adhesion to surfaces, thereby blocking attachment-driven biofilm formation that would restrict movement within the xylem and thus colonization of plants. The ubiquity of OMV formation in the bacterial world suggests that these extracellular products may have alternative roles that might modulate movement and biofilm formation.

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Section: Discussionmentioning

confidence: 99%

Xylella fastidiosa outer membrane vesicles modulate plant colonization by blocking attachment to surfaces

Ionescu

Zaini

Baccari

et al. 2014

Proc. Natl. Acad. Sci. U.S.A.

138

140

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“…In addition, our experiments suggested that a virulence factor, which specifically cleaves human IgA1, extracellular metalloprotease IgA1 (89), was uniformly present in MVs isolated from GC strains (Table III). Although protease IgA1 was the first autotransporter described in Neisseriaceae (89), its presence in MVs has also been observed in N. meningitidis (86,90,91), which further suggests that IgA1 might be associated with the MVs.…”

Section: Strategy For Rigorous Proteomic Profiling Of the Gc Cell Envmentioning

confidence: 99%

“…Sorting of these proteins into MVs was established in N. meningitidis and N. lactamica (75,76,78,79,86). One of the more fascinating features of a major GC porin, PorB (65) is its translocation from bacterial outer membrane and insertion into the membranes of eukaryotic cell organelles (87).…”

Section: Strategy For Rigorous Proteomic Profiling Of the Gc Cell Envmentioning

confidence: 99%

Quantitative Proteomics of the Neisseria Gonorrhoeae Cell Envelope and Membrane Vesicles for the Discovery of Potential Therapeutic Targets

Zielke

Wierzbicki

Weber

et al. 2014

Molecular & Cellular Proteomics

163

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Neisseria gonorrhoeae (GC) is a human-specific pathogen, and the agent of a sexually transmitted disease, gonorrhea. There is a critical need for new approaches to study and treat GC infections because of the growing threat of multidrug-resistant isolates and the lack of a vaccine. Despite the implied role of the GC cell envelope and membrane vesicles in colonization and infection of human tissues and cell lines, comprehensive studies have not been undertaken to elucidate their constituents. Accordingly, in pursuit of novel molecular therapeutic targets, we have applied isobaric tagging for absolute quantification coupled with liquid chromatography and mass spectrometry for proteome quantitative analyses. Mining the proteome of cell envelopes and native membrane vesicles revealed 533 and 168 common proteins, respectively, in analyzed GC strains FA1090, F62, MS11, and 1291. A total of 22 differentially abundant proteins were discovered including previously unknown proteins. Among those proteins that displayed similar abundance in four GC strains, 34 were found in both cell envelopes and membrane vesicles fractions. Focusing on one of them, a homolog of an outer membrane protein LptD, we demonstrated that its depletion caused loss of GC viability. In addition, we selected for initial characterization six predicted outer membrane proteins with unknown function, which were identified as ubiquitous in the cell envelopes derived from examined GC isolates. These studies entitled a construction of deletion mutants and analyses of their resistance to different chemical probes. Loss of NGO1985, in particular, resulted in dramatically decreased GC viability upon treatment with detergents, polymyxin B, and chloramphenicol, suggesting that this protein functions in the maintenance of the cell envelope permeability barrier. Together, these findings underscore the concept that the cell envelope and membrane vesicles contain crucial, yet under-explored determinants of GC physiology, which may represent promising targets for designing new therapeutic interventions. Molecular &

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“…The cultures were then immediately chilled on ice, and cells were harvested by centrifugation. In order to obtain an internal 15 N standard (23), equal portions of reaction mixtures corresponding to each set of conditions were mixed with equal amounts of 15 N-labeled MC58 cells grown on minimal medium for meningococci (MMM) with 15 NH 4 Cl as the sole source of nitrogen (22). Subsequently, outer membrane (OM) preparations were prepared using the "shakeand-bake" method (24) without further purification.…”

mentioning

confidence: 99%

“…Sample preparation for proteome analysis was conducted using a method similar to that described recently (22). Strain MC58 was grown in 1 liter of liquid culture at either 32°C or 37°C for 6 h in MDM.…”

mentioning

confidence: 99%

Impact of Moderate Temperature Changes on Neisseria meningitidis Adhesion Phenotypes and Proteome

et al. 2016

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bNeisseria meningitidis, the meningococcus, bears the potential to cause life-threatening invasive diseases, but it usually colonizes the nasopharynx without causing any symptoms. Within the nasopharynx, Neisseria meningitidis must face temperature changes depending on the ambient air temperature. Indeed, the nasopharyngeal temperature can be substantially lower than 37°C, the temperature commonly used in experimental settings. Here, we compared the levels of meningococcal biofilm formation, autoaggregation, and cellular adherence at 32°C and 37°C and found a clear increase in all these phenotypes at 32°C suggestive of a stronger in vivo colonization capability at this temperature. A comparative proteome analysis approach revealed differential protein expression levels between 32°C and 37°C, predominantly affecting the bacterial envelope. A total of 375 proteins were detected. Use of database annotation or the PSORTb algorithm predicted 49 of those proteins to be localized in the outer membrane, 21 in either the inner or outer membrane, 35 in the periplasm, 56 in the inner membrane, and 208 in the cytosol; for 6 proteins, no annotation or prediction was available. Temperature-dependent regulation of protein expression was seen particularly in the periplasm as well as in the outer and inner membranes. Neisserial heparin binding antigen (NHBA), NMB1030, and adhesin complex protein (ACP) showed the strongest upregulation at 32°C and were partially responsible for the observed temperature-dependent phenotypes. Screening of different global regulators of Neisseria meningitidis suggested that the extracytoplasmic sigma factor E might be involved in temperature-dependent biofilm formation. In conclusion, subtle temperature changes trigger adaptation events promoting mucosal colonization by meningococci. Microorganisms constantly adapt to changing environmental conditions. These changes include oxygen and nutrient availability, osmotic conditions, and temperature. The physiology of bacterial adaptation, including the underlying regulatory mechanisms that operate in response to radical temperature changes such as classical heat shock or cold shock, has been studied intensely (1-3). The heat shock response occurs during a transient upshift of growth temperature from 37°C to approximately 50°C (4). The heat shock response is controlled by the alternative sigma factor 32 , which regulates the expression of heat shock proteins mainly involved in protein folding or processing (4). In Escherichia coli, the cold shock response is triggered by a transient downshift from 37°C to 10°C that leads to generally slower transcriptional and translational responses except for about 26 upregulated proteins (5). The functions of these so-called cold shock proteins are less well understood than those of heat shock proteins, but they are likely involved in securing proper transcription, translation, and protein folding (5). Surprisingly little is known about the influence on bacterial physiology of slight temperature differences within mamma...

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Comparative Proteome Analysis of Spontaneous Outer Membrane Vesicles and Purified Outer Membranes of Neisseria meningitidis

Cited by 102 publications

References 62 publications

Xylella fastidiosa outer membrane vesicles modulate plant colonization by blocking attachment to surfaces

Xylella fastidiosa outer membrane vesicles modulate plant colonization by blocking attachment to surfaces

Quantitative Proteomics of the Neisseria Gonorrhoeae Cell Envelope and Membrane Vesicles for the Discovery of Potential Therapeutic Targets

Impact of Moderate Temperature Changes on Neisseria meningitidis Adhesion Phenotypes and Proteome

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