Characterization of an iron-regulated alpha-enolase of Bacteroides fragilis

Sijbrandi, Robert; Blaauwen, Tanneke den; Tame, J.R.H.; Oudega, Bauke; Luirink, Joen; Otto, Ben R.

doi:10.1016/j.micinf.2004.09.013

Cited by 26 publications

(26 citation statements)

References 38 publications

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“…However, B. fragilis utilizes outer membrane proteins for the acquisition of iron from heme-compounds present in normal serum, indicating that iron chelators are rarely used in B. fragilis. [50][51][52] Therefore, the apical secretion of Lcn-2 by BFT may play a role in the growth inhibition of other bacterial groups except B. fragilis.…”

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confidence: 99%

Bacteroides fragilis enterotoxin upregulates lipocalin-2 expression in intestinal epithelial cells

Yoo

Jung

et al. 2013

Laboratory Investigation

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Enterotoxigenic Bacteroides fragilis (ETBF) produces an B20 kDa B. fragilis enterotoxin (BFT), which plays an essential role in mucosal inflammation. Lipocalin (Lcn)-2, a siderophore-binding antimicrobial protein, is critical for control of bacterial infection; however, expression of Lcn-2 in BFT-exposed intestinal epithelial cells has not been elucidated. In the present study, stimulation of human intestinal epithelial cells with BFT resulted in the upregulation of Lcn-2 expression that was a relatively late response of intestinal epithelial cells compared with human b-defensin (hBD)-2 expression. The upregulation of Lcn-2 was dependent on AP-1 but not on NF-kB signaling. Lcn-2 induction via AP-1 was regulated by mitogenactivated protein kinases (MAPKs) including ERK and p38. Lcn-2 was secreted from the apical and basolateral surfaces in BFT-treated cells. These results suggest that a signaling pathway involving MAPKs and AP-1 is required for Lcn-2 induction in intestinal epithelial cells exposed to BFT, after which the secreted Lcn-2 may facilitate antimicrobial activity within ETBF-infected mucosa.

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confidence: 99%

Bacteroides fragilis enterotoxin upregulates lipocalin-2 expression in intestinal epithelial cells

Yoo

Jung

et al. 2013

Laboratory Investigation

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“…In particular, in the human gastrointestinal niche, enteropathogens such as Salmonella enterica, Listeria monocytogenes, Helicobacter pylori, and Escherichia coli, as well as Bacteroides fragilis, an opportunistic pathogen and common member of the normal human gut flora, have been shown to capture human Plg on the cell surface (16,27,33,38,40). Plg is a single-chain glycoprotein with a molecular mass of 92 kDa and represents the monomeric proenzyme of the serine protease plasmin.…”

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confidence: 99%

“…Because of these characteristics and the broad proteolytic activity of plasmin, the mammalian Plg system offers a high-potential proteolytic system to bacteria for colonization of the human host. In fact, with the recruitment of human Plg on the bacterial cell surface and its subsequent conversion to plasmin, microorganisms acquire a surfaceassociated proteolytic activity useful for facilitating the migration across physical and molecular barriers and for re-sponding to the nutritional demands during the colonization process (4,8,16,17,25,27,33,38,39).…”

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confidence: 99%

Binding of Human Plasminogen toBifidobacterium

Candela

Bergmann

Vici³

et al. 2007

J Bacteriol

109

103

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Bifidobacteria constitute up to 3% of the total microbiota and represent one of the most important healthpromoting bacterial groups of the human intestinal microflora. The presence of Bifidobacterium in the human gastrointestinal tract has been directly related to several health-promoting activities; however, to date, no information about the specific mechanisms of interaction with the host is available. In order to provide some insight into the molecular mechanisms involved in the interaction with the host, we investigated whether Bifidobacterium was able to capture human plasminogen on the cell surface. By using flow cytometry, we demonstrated a dose-dependent human plasminogen-binding activity for four strains belonging to three bifidobacterial species: Bifidobacterium lactis, B. bifidum, and B. longum. The binding of human plasminogen to Bifidobacterium was dependent on lysine residues of surface protein receptors. By using a proteomic approach, we identified five putative plasminogen-binding proteins in the cell wall fraction of the model strain B. lactis BI07. The data suggest that plasminogen binding to B. lactis is due to the concerted action of a number of proteins located on the bacterial cell surface, some of which are highly conserved cytoplasmic proteins which have other essential cellular functions. Our findings represent a step forward in understanding the mechanisms involved in the Bifidobacterium-host interaction.

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“…This modality of interaction with the components of the host Plg system resembles the one characteristic of several enteropathogens, such as Salmonella enterica, Listeria monocytogenes, and Escherichia coli (16,25,29,30,32,36). Different from the case for Bifidobacterium, the role of Plg in bacterial pathogens has been determined, and the bacterial capacity to intervene with the host Plg system has been traditionally considered a paradigm of pathogenicity (5,16,25,29,30,32,35). Facilitating the bacterial transmigration through epithelial monolayers, for pathogens, the acquisition of a Plg-dependent surface-associated plasmin activity is necessary for dissemination in the host tissues.…”

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confidence: 85%

Tumor Necrosis Factor Alpha Modulates the Dynamics of the Plasminogen-Mediated Early Interaction between Bifidobacterium animalis subsp. lactis and Human Enterocytes

Centanni

Bergmann

Turroni

et al. 2012

Appl Environ Microbiol

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The capacity to intervene with the host plasminogen system has recently been considered an important component in the interaction process between Bifidobacterium animalis subsp. lactis and the human host. However, its significance in the bifidobacterial microecology within the human gastrointestinal tract is still an open question. Here we demonstrate that human plasminogen favors the B. animalis subsp. lactis BI07 adhesion to HT29 cells. Prompting the HT29 cell capacity to activate plasminogen, tumor necrosis factor alpha (TNF-␣) modulated the plasminogen-mediated bacterium-enterocyte interaction, reducing the bacterial adhesion to the enterocytes and enhancing migration to the luminal compartment.

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Characterization of an iron-regulated alpha-enolase of Bacteroides fragilis

Cited by 26 publications

References 38 publications

Bacteroides fragilis enterotoxin upregulates lipocalin-2 expression in intestinal epithelial cells

Bacteroides fragilis enterotoxin upregulates lipocalin-2 expression in intestinal epithelial cells

Binding of Human Plasminogen toBifidobacterium

Tumor Necrosis Factor Alpha Modulates the Dynamics of the Plasminogen-Mediated Early Interaction between Bifidobacterium animalis subsp. lactis and Human Enterocytes

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