NeMeSys: a biological resource for narrowing the gap between sequence and function in the human pathogen Neisseria meningitidis

Rusniok, Christophe; Vallenet, David; Floquet, Stéphanie; Ewles, Helen A.; Mouzé-Soulama, Coralie; Brown, D.; Lajus, Aurélie; Buchrieser, Carmen; Médigue, Claudine; Glaser, Philippe; Pelicic, Vladimir

doi:10.1186/gb-2009-10-10-r110

Cited by 86 publications

(141 citation statements)

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“…Using this method, a total of 375 distinct proteins were quantified from both the 32°C and 37°C conditions (see Table S1 in the supplemental material). All quantified proteins were classified according to their known or predicted subcellular localization using the NeMeSys database, the UniProt database, and/or the PSORTb algorithm (30)(31)(32). Among the 375 identified proteins, 49 were predicted to be localized in the outer membrane (OM), 21 (predominantly lipoproteins) in either the inner or outer membrane (I/OM), 35 in the periplasm (P), 56 in the inner membrane (IM), and 208 in the cytosol (C), whereas the location of 6 proteins could not be inferred (no) by either database annotation or computational prediction (Fig.…”

Section: Resultsmentioning

confidence: 99%

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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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Section: Resultsmentioning

confidence: 99%

“…Subcellular localization of proteins was allocated according to the annotation in the NeMeSys database (30) and/or UniProt (31). For all proteins without database annotation of subcellular localization, the PSORTb algorithm was used for prediction (32).…”

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confidence: 99%

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

et al. 2016

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“…meningitidis strains used in this study are derivatives of the sequenced and systematically mutagenized serogroup C clinical isolate 8013 (35,36). The comP mutants have been previously described (21 Variants in which charged residues in the identified electropositive stripe were changed to Ala (ComP R78A , ComP K94A , and ComP K108A ) were constructed by site-directed mutagenesis, and the resulting proteins were purified.…”

Section: Methodsmentioning

confidence: 99%

Specific DNA recognition mediated by a type IV pilin

Cehovin

Simpson

McDowell

et al. 2013

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

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Natural transformation is a dominant force in bacterial evolution by promoting horizontal gene transfer. This process may have devastating consequences, such as the spread of antibiotic resistance or the emergence of highly virulent clones. However, uptake and recombination of foreign DNA are most often deleterious to competent species. Therefore, model naturally transformable Gramnegative bacteria, including the human pathogen Neisseria meningitidis, have evolved means to preferentially take up homotypic DNA containing short and genus-specific sequence motifs. Despite decades of intense investigations, the DNA uptake sequence receptor in Neisseria species has remained elusive. We show here, using a multidisciplinary approach combining biochemistry, molecular genetics, and structural biology, that meningococcal type IV pili bind DNA through the minor pilin ComP via an electropositive stripe that is predicted to be exposed on the filaments surface and that ComP displays an exquisite binding preference for DNA uptake sequence. Our findings illuminate the earliest step in natural transformation, reveal an unconventional mechanism for DNA binding, and suggest that selective DNA uptake is more widespread than previously thought.DNA receptor | genetic competence

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“…Cysteine, which is a major source of sulfur and hence essential for growth of N. meningitides, was fed about a concentration of 0.04%. Cysteine is converted to glutathione (GSH), then to glutathione sulfide by oxidation, hence controls the cellular H 2 O 2 level [35,36]. Transcriptome analysis suggested that cysteine depletion impairs sulfur supply for Fe-S protein assembly and cause oxidative stress [37].…”

Section: +mentioning

confidence: 99%

Optimization of Media and Feeding Strategy for Improved Capsular Polysaccharide Yield for Neisseria meningitidis W-135

Kambrath¹,

Reddy²

2017

THE IJES

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has turned out to be the reason for recent outbreak of meningitis in the sub-Saharan regions of Africa including Cameroon, Chad, Gambia, Burkina Faso, and other countries. The capsular polysaccharide (PS) of Neisseria meningitidis serogroups A, C, X, Y, and W-135 are excellent vaccine targets against meningitis caused by this bacterium. This study promotes a novel feed solution including amino acids, vitamins, and glucose along with an optimal fermentation medium; and feeding strategy to cultivate high yield polysaccharide at harvest level. The study is based on the hypothesis that glucose is one of the major growth determining factors with the combinations of nitrogen sources. In this study, fed-batch cultivation was performed in a 2L fermenter, maintaining the following conditions: (i) Temperature = 37ºC (ii) pH = 7.0 (iii) Agitation frequency in the range 150 rotations per minute (rpm) to 500 rpm, and (iv) Dissolved oxygen (DO) 20%-25%. The bacterial growth and polysaccharide production were found to be enhanced when the feed flow was increased periodically from late lag phase to early decline phase. The polysaccharide production was found to be maximum in the early decline phase of the bacterial growth. The said method produced polysaccharide of about 1000mg/L, which is twice the reported method. There is limited research information available on fed-batch cultivation and feeding strategy for growing Neisseria meningitidis W-135. The major findings of this study can provide significant contribution in the field of capsular polysaccharide production from which MenW polysaccharide vaccines are manufactured.

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NeMeSys: a biological resource for narrowing the gap between sequence and function in the human pathogen Neisseria meningitidis

Abstract: The genome of a clinical isolate of Neisseria meningitidis is described. This and other reannotated Neisseria genomes are compiled in a database.

Cited by 86 publications

References 56 publications

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

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

Specific DNA recognition mediated by a type IV pilin

Optimization of Media and Feeding Strategy for Improved Capsular Polysaccharide Yield for Neisseria meningitidis W-135

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