Haemagglutination and glycolipid‐binding activities of
            <i>Lactobacillus reuteri</i>

Mukai, T.; Kaneko, Shigeo; Ohori, Hitoshi

doi:10.1046/j.1472-765x.1998.00418.x

Cited by 28 publications

(19 citation statements)

References 12 publications

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“…Galactosylated glycoconjugates mediate attachment of pathogens, such as Listeria monocytogenes (Mouricout, 1997), and indigenous flora to epithelial surfaces and provide a source of nutrients for members of the microflora, such as Escherichia coli (Mouricout, 1997), and Lactobacillus reuteri (Mukai et al, 1998). The ability of B. thetaiotaomicron SCS to increase the galactose-specific lectin-binding residues in the intestinal cells may affect the ability of other components of the normal flora to establish a stable niche or could affect the vulnerability of the intestine to colonization by pathogens.…”

Section: Discussionmentioning

confidence: 99%

A heat labile soluble factor from Bacteroides thetaiotaomicron VPI-5482 specifically increases the galactosylation pattern of HT29-MTX cells

et al. 2001

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The aim of this work was to set up and validate an in vitro model to study a molecular response of an intestinal host cell line (HT29-MTX), to a non-pathogen microflora component. We found that Bacteroides thetaiotaomicron strain VPI-5482 had the capacity to change a specific glycosylation process in HT29-MTX cells via a mechanism that involved a soluble factor. Differentiated HT29-MTX cells were grown in the presence of 20% of spent culture supernatant from the B. thetaiotaomicron during 10 days. Glycosylation processes were followed using a large panel of lectins and analysed using confocal microscopy, western blotting and flow cytometry techniques. Our results show that a B. thetaiotaomicron soluble factor modified specifically the galactosylation pattern of HT29-MTX cells, whereas other glycosylation steps remained mainly unaffected. Further characterization of this soluble factor indicates that it is a heat labile, low molecular weight compound. Reverse transcript-PCR (RT-PCR) analysis was unable to show any significant change in mRNA expression level of the main galactosyltransferases expressed in HT29-MTX cells. By contrast, galactosyltransferase activities dramatically increased in HT29-MTX cells treated by the soluble extract of B. thetaiotaomicron, suggesting a post-translational regulation of these activities. Our in vitro model allowed us to study the cross-talk between a single bacteria and intestinal cells. The galactosylation process appears to be a target of this communication, thus uncovering a new window to study the functional consequences of co-operative symbiotic bacterial-host interactions.

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Section: Discussionmentioning

confidence: 99%

A heat labile soluble factor from Bacteroides thetaiotaomicron VPI-5482 specifically increases the galactosylation pattern of HT29-MTX cells

et al. 2001

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“…This epithelial coat consists largely of several glycoproteins, glycolipids, and mucins which contain different sugar residues: N-acetylglucosamine (GlcNAc), galactose (Gal), N-acetylgalactosamine (GalNac), fucose (Fuc), N-acetylneuraminic acid (NeuNAc) or sialic acid, mannose, glucose, and xylose. Susceptibility and resistance to intestinal infections is often associated with the presence or absence of receptors appropriately glycosylated (Karlsson 1998;Dai et al 2000;Mouricout 1997;Mukai et al 1998;Walker 2000). The glycan structure of glycoconjugates is determined genetically and specifically for a particular individual, and is a product of genes coding for specific enzymes involved in the glycosylation process (e.g., glycosyltransferases, glycosidases; Falk et al 1998).…”

Section: Introductionmentioning

confidence: 99%

Indigenous microbes and their soluble factors differentially modulate intestinal glycosylation steps in vivo

Freitas

Axelsson

Cayuela

et al. 2005

Histochem Cell Biol

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It has been shown that Bacteroides thetaiotaomicron, a representative member of the gut microflora, signals intestinal epithelial cells both in vivo and in vitro and modulate specific glycosylation processes that may mediate intestinal functions. However it is not known whether these modulations depend on the presence of live bacteria or may be elicited by soluble factors produced in vitro by this bacterium. We used lectins and an histochemical approach to survey tissue sections prepared from various cellular compartments of the small and large intestine of NRMI/KI mice grown under gnotobiotic conditions. We compared the results obtained with bacterial culture supernatant and live B. thetaiotaomicron to those obtained from germ-free mice or mice having a conventional microflora. This approach allowed us to conclude that (1) a small but specific number of glycan patterns were restored after treatment with bacterial culture supernatant and (2) the B. thetaiotaomicron associated mice restored a larger number of patterns, however, the complete conventional mice pattern must be a function of the whole microflora in the gut. The possibility to modulate this complex glycosylation pattern by introducing exogenous bacteria and bacterial products should be considered as a promising approach towards understanding the molecular basis of microbial-host interactions.

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“…Lactobacillus, one of the common indigenous organisms of the gastrointestinal tracts of mammals (46,48,49) and a potential probiotic microbe that contributes to the health of the host (11,16), has the capacity to adhere to epithelial cells (5,6,9,10,16,21,23,24,33,34,44,49) and mucus gel (25,32,35,38,41,51,52) from the intestinal tracts of different species. Lactobacillus surface proteins have been proposed to be involved in colonization of gastrointestinal epithelial cells and mucosa of mammals (9,12,21,41,44,53).…”

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confidence: 99%

Purification and Characterization of a Surface Protein from Lactobacillus fermentum 104R That Binds to Porcine Small Intestinal Mucus and Gastric Mucin

Rojas-Contreras

Ascencio²,

Conway

2002

Appl Environ Microbiol

161

124

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An adhesion-promoting protein involved in the binding of Lactobacillus fermentum strain 104R to small intestinal mucus from piglets and to partially purified gastric mucin was isolated and characterized. Spent culture supernatant fluid and bacterial cell wall extracts were fractionated by ammonium sulfate precipitation and gel filtration. The active fraction was purified by affinity chromatography. The adhesion-promoting protein was detected in the fractions by adhesion inhibition and dot blot assays and visualized by polyacrylamide gel electrophoresis (PAGE), sodium dodecyl sulfate-PAGE, and Western blotting with horseradish peroxidaselabeled mucus and mucin. The active fraction was characterized by estimating the relative molecular weight and by assessing the presence of carbohydrates in, and heat sensitivity of, the active region of the adhesionpromoting protein. The purified protein was digested with porcine trypsin, and the peptides were purified in a SMART system. The peptides were tested for adhesion to horseradish peroxidase-labeled mucin by using the dot blot adhesion assay. Peptides which bound mucin were sequenced. It was shown that the purified adhesionpromoting protein on the cell surface of L. fermentum 104R is extractable with 1 M LiCl and low concentrations of lysozyme but not with 0.2 M glycine. The protein could be released to the culture supernatant fluid after 24 h of growth and had affinity for both small intestinal mucus and gastric mucin. In the native state this protein was variable in size, and it had a molecular mass of 29 kDa when denatured. The denatured protein did not contain carbohydrate moieties and was not heat sensitive. Alignment of amino acids of the adhering peptides with sequences deposited in the EMBL data library showed poor homology with previously published sequences. The protein represents an important molecule for development of probiotics.Proteinaceous surface appendages or coverings, e.g., fimbriae, flagella, or surface (S)-layers with affinity for mammalian extracellular matrix (55) or mucosa (17, 28), have been extensively characterized for many pathogenic bacteria. It is thought that adhesion to mammalian extracellular matrix components is a prerequisite for bacterial colonization and invasion to subepithelial tissues (55) Cell surface-adhesive proteins from nonpathogenic bacteria and their role in colonization has not been as thoroughly characterized.Lactobacillus, one of the common indigenous organisms of the gastrointestinal tracts of mammals (46,48,49) and a potential probiotic microbe that contributes to the health of the host (11,16), has the capacity to adhere to epithelial cells (5,6,9,10,16,21,23,24,33,34,44,49) and mucus gel (25,32,35,38,41,51,52) from the intestinal tracts of different species. Lactobacillus surface proteins have been proposed to be involved in colonization of gastrointestinal epithelial cells and mucosa of mammals (9,12,21,41,44,53). Collagen binding by lactobacilli (1, 47) is known, and purification of collagen binding proteins from L...

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Haemagglutination and glycolipid‐binding activities of Lactobacillus reuteri

Cited by 28 publications

References 12 publications

A heat labile soluble factor from Bacteroides thetaiotaomicron VPI-5482 specifically increases the galactosylation pattern of HT29-MTX cells

A heat labile soluble factor from Bacteroides thetaiotaomicron VPI-5482 specifically increases the galactosylation pattern of HT29-MTX cells

Indigenous microbes and their soluble factors differentially modulate intestinal glycosylation steps in vivo

Purification and Characterization of a Surface Protein from Lactobacillus fermentum 104R That Binds to Porcine Small Intestinal Mucus and Gastric Mucin

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