Bacterial Capsular Polysaccharide and Sugar Transferases

Miyake, Katsuhide; Iijima, Shinji

doi:10.1007/b94193

Cited by 7 publications

(5 citation statements)

References 38 publications

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“…The GBS enzyme (gbs0738) shares high identity with an E. coli enzyme within this family of glycosyltransferases that is involved in synthesis of the outer core region of lipo-oligosaccharide, catalyzing the ␣-1,2 linkage of donor sugar to their acceptors (26). In Streptococcus spp., glycosyltransferases participate in the biosynthesis of capsular polysaccharides, cell wall peptidoglycan, and anchoring of lipotechoic acid within the cell wall (27,28). In GBS, glycosyltransferase-encoding cpsE is important for the synthesis of the surface polysaccharide capsules (29), and iagA is a glycosyltransferase that aids in the anchoring of lipotechoic acid (21), but neither are essential for GBS growth (21,29).…”

Section: Discussionmentioning

confidence: 99%

Human milk oligosaccharides inhibit growth of group B Streptococcus

Lin¹,

Autran

Szyszka

et al. 2017

Journal of Biological Chemistry

139

113

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(group B , GBS) is a leading cause of invasive bacterial infections in newborns, typically acquired vertically during childbirth secondary to maternal vaginal colonization. Human milk oligosaccharides (HMOs) have important nutritional and biological activities that guide the development of the immune system of the infant and shape the composition of normal gut microbiota. In this manner, HMOs help protect against pathogen colonization and reduce the risk of infection. In the course of our studies of HMO-microbial interactions, we unexpectedly uncovered a novel HMO property to directly inhibit the growth of GBS independent of host immunity. By separating different HMO fractions through multidimensional chromatography, we found the bacteriostatic activity to be confined to specific non-sialylated HMOs and synergistic with a number of conventional antibiotic agents. Phenotypic screening of a GBS transposon insertion library identified a mutation within a GBS-specific gene encoding a putative glycosyltransferase that confers resistance to HMOs, suggesting that HMOs may function as an alternative substrate to modify a GBS component in a manner that impairs growth kinetics. Our study uncovers a unique antibacterial role for HMOs against a leading neonatal pathogen and expands the potential therapeutic utility of these versatile molecules.

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Section: Discussionmentioning

confidence: 99%

Human milk oligosaccharides inhibit growth of group B Streptococcus

Lin¹,

Autran

Szyszka

et al. 2017

Journal of Biological Chemistry

139

113

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“…Most clinical isolates of GBS are capsulated, and so far, 10 different serotypes (Ia, Ib, II-IX) have been described [33,34]. This bacterium was chosen for the experiments, as glycan assays have shown M-ficolin to be the lectin pathway PRM with the highest propensity for binding to sialic acid residues [29], and the capsular polysaccharides of GBS contain sialic acid as terminal side-chain residues [30,31]. In agreement with this, all serotypes of GBS were able to deplete serum of M-ficolin in a dose-dependent manner, whereas we saw no depletion of MBL or H-or L-ficolin (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…M-ficolin binds to a variety of different acetylated ligands [7,8,12], and strong binding to polysaccharides containing sialic acids is reported [29]. We therefore decided to examine if M-ficolin binds to GBS, which presents sialic acid as the terminal side-chain residues of the capsular polysaccharides of different chemical structures [30,31]. When incubating a number of capsulated GBS with 10% NHS, we observed dose-dependent binding of M-ficolin, with some variation between the different serotypes (Fig.…”

Section: M-ficolin Binding To Bacteriamentioning

confidence: 99%

Investigations on the pattern recognition molecule M-ficolin: quantitative aspects of bacterial binding and leukocyte association

Kjær

Hansen

Sørensen

et al. 2011

Journal of Leukocyte Biology

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M-ficolin is a PRM of the innate immune system, found in serum and associated with leukocytes. We used the soluble form to study specificity toward Gram-positive bacteria and characterized and quantified cell-associated M-ficolin. The binding of M-ficolin to capsulated and noncapsulated strains of Streptococcus agalactiae (GBS) and Staphylococcus aureus was investigated. We did not observe binding of M-ficolin to any of 13 serotypes of S. aureus. Dose-dependent binding of M-ficolin was demonstrated for all of the capsulated GBS strains. The binding was abolished by prior treatment of the bacteria with sialidase, indicating that sialic acid is the ligand for M-ficolin on these bacteria. GlcNAc could inhibit the binding, suggesting that M-ficolin binds via its FBG. M-ficolin was found associated with the complement-activating enzyme in serum, and M-ficolin bound to GBS mediated activation of the complement system. M-ficolin expression on leukocytes was evaluated by flow cytometry with anti-M-ficolin mAb. Total M-ficolin of different leukocytes was quantified in detergent extracts. Monocytes and granulocytes showed similar M-ficolin surface expression, 1.1 × 10(5) and 0.7 × 10(5) M-ficolin molecules/cell, respectively. The total M-ficolin content of the cells was 1.5 × 10(6) molecules/monocyte and approximately one-third of this for granulocytes. Lymphocytes contained <1.5% of the amount estimated for monocytes, and none was revealed on the surface of lymphocytes by flow cytometry. Immunohistochemical analysis of the distribution of M-ficolin in 25 tissues revealed staining of only granulocytes and monocytes. Reported M-ficolin expression by type II pneumocytes could not be verified. We demonstrate the specific binding of M-ficolin to sialic acids in the capsule of GBS and give quantitative aspects of the cell-associated M-ficolin.

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“…While there are a number of known substrates for GNAT superfamily members, including antibiotics such as aminoglycosides, homoserine lactones and glucosamine‐1‐phosphate (GlcN‐1‐PO 4 ), only a few GNATs have been functionally characterized. In several bacterial species, atf is located within a capsular polysaccharide biosynthesis locus (Annunziato et al ., 1995; van Selm et al ., 2002; Miyake and Iijima, 2004). Thus, atf is likely to play a role in exopolysaccharide biosynthesis.…”

Section: Discussionmentioning

confidence: 99%

Streptococcus gordonii utilizes several distinct gene functions to recruit Porphyromonas gingivalis into a mixed community

Kuboniwa

Tribble

James

et al. 2006

Molecular Microbiology

127

122

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SummaryDental plaque biofilm formation proceeds through a developmental pathway initiated by the attachment of pioneer organisms, such as Streptococcus gordonii, to tooth surfaces. Through a variety of synergistic interactions, pioneer organisms facilitate the colonization of later arrivals including Porphyromonas gingivalis , a potential periodontal pathogen. We have investigated genes of S. gordonii required to support a heterotypic biofilm community with P. gingivalis . By screening a plasmid integration library of S. gordonii, genes were identified that are crucial for the accumulation of planktonic P. gingivalis cells into a multispecies biofilm. These genes were further investigated by specific mutation and complementation analyses. The biofilm-associated genes can be grouped into broad categories based on putative function as follows: (i) intercellular or intracellular signalling ( cbe and spxB ), (ii) cell wall integrity and maintenance of adhesive proteins ( murE, msrA and atf ), (iii) extracellular capsule biosynthesis ( pgsA and atf ), and (iv) physiology ( gdhA, ccmA and ntpB ). In addition, a gene for a hypothetical protein was identified. Biofilm visualization and quantification by confocal microscopy confirmed the role of these genes in the maturation of the multispecies community, including biofilm architectural development. The results suggest that S. gordonii governs the development of heterotypic oral biofilms through multiple genetic pathways.

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Bacterial Capsular Polysaccharide and Sugar Transferases

Cited by 7 publications

References 38 publications

Human milk oligosaccharides inhibit growth of group B Streptococcus

Human milk oligosaccharides inhibit growth of group B Streptococcus

Investigations on the pattern recognition molecule M-ficolin: quantitative aspects of bacterial binding and leukocyte association

Streptococcus gordonii utilizes several distinct gene functions to recruit Porphyromonas gingivalis into a mixed community

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