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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

O-specific polysaccharide has been isolated on autohydrolysis of lipopolysaccharide from Yersinia intermedia O: 4.33 (strain 1476) and shown to consist of the yersiniose B (3.6-dideoxy-4-C-(1-hydroxyethyl)-xylo-hexose) and 2-acetamido-2-deoxy-D-galactose residues in a molar ratio of 1 : 2. Acid hydrolysis, methylation. solvolysis with anhydrous hydrogen fluoride. and 13C-NMR studies indicate the polysaccharide to be composed of trisaccharide repeating units of the following structure: (Formula: see text).
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PMID:[Structure of the O-specific polysaccharide chain of the lipopolysaccharide from Yersinia intermedia serotype O:4.33]. 245 23

O-Specific polysaccharide has been isolated on mild acid hydrolysis of the lipopolysaccharide from Yersinia enterocolitica O: 4.32 (strain 96) and shown to consist of yersiniose B (3,6-dideoxy-4-C-(1-hydroxyethyl)-D-xylo-hexose, YerB) acetylated at C1' and 2-acetamido-2-deoxy-D-galactose residues in a molar ratio 1:2. Acid hydrolysis, methylation and 13C NMR studies indicated the polysaccharide to be composed of trisaccharide repeating units of the following structure: (sequence; see text) The data obtained revealed structural and serological interrelation between O-antigens of Y. enterocolitica O:4.32 and Y. intermedia O:4.33.
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PMID:[Structure of the O-specific polysaccharide of the Yersinia enterocolitica serovar O:4.32 lipopolysaccharide. Serologic relations of lipopolysaccharides of Y. enterocolitica O:4.32 and Y. intermedia O:4.33]. 247 96

A branched chain octose, 3,6-dideoxy-4-C-(L-glycero-1'-hydroxyethyl)-D-xylo- hexose, was isolated from the lipopolysaccharide of Yersinia frederiksenii, serovar O: 16.29 and identified as yersiniose A from Y. pseudotuberculosis, serovar VI. Mild hydrolysis of the lipopolysaccharide with acetic acid afforded a rhamnan. Structural features of the trisaccharide repeating unit were elucidated on the basic of 13C NMR spectral data, methylation studies and periodate oxidation. Using these data as well as data on sugar composition and methylation studies of the lipopolysaccharide, the following structural pattern of the repeating unit of O-specific polysaccharide was proposed: (formula; see text)
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PMID:[The structure of O-specific polysaccharide of Yersinia frederiksenii serotype O:16,29 lipopolysaccharide]. 248 41

Activation of Leishmania enriettii-infected mouse macrophages in vitro by treatment with macrophage activating factor (MAF)-rich media supplemented with lipopolysaccharide (LPS) leads to rapid killing of the microorganism. When exposed to MAF + LPS in the presence of 30-100 microM lead acetate, however, macrophages failed to destroy the parasites. This effect was not due to lead toxicity for macrophages. Decreased microbicidal activity correlated with depressed respiratory burst as determined by measurements of glucose oxidation through the hexose monophosphate shunt (HMPS). Lead had little effect on intracellular parasite killing induced by exposure of macrophages to the electron carrier methylene blue; HMPS in such cells was similarly little affected, indicating that chemical triggering of this pathway bypassed the lead-imposed blockade. Lead also abolished macrophage activation measured by the lysis of tumor target cells in vitro. The metal failed, however, to interfere with target-cell lysis by macrophages activated in lead-free medium, suggesting that lead inhibited the acquisition of the activated state rather than the functional expression of such state. Lead did not prevent the binding of radiolabelled interferon-gamma to macrophages; it did, however, slow down receptor turnover and degradation of bound interferon. Lead also inhibited the LPS-triggered cytotoxicity in macrophages previously exposed to interferon-gamma in lead-free medium, suggesting that depressed intracellular killing might result from an effect on both the priming (interferon or MAF-dependent) and the triggering (LPS-dependent) steps of activation.
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PMID:Lead inhibits intracellular killing of Leishmania parasites and extracellular cytolysis of target cells by macrophages exposed to macrophage activating factor. 249 92

Peritoneal and bone marrow-derived macrophages of the C57BL/6 and DBA/2 mouse strains were exposed in vitro to increasing concentrations of the bacterial lysate Broncho-Vaxom (BV), in the presence or absence of macrophage-activating factor (MAF)-rich media. Two metabolic pathways and two functional activities of the macrophages were studied. First, oxidative metabolism was found to increase sharply in macrophages incubated with BV, as measured by the catabolism of glucose via the hexose monophosphate shunt pathway, and by the production of the superoxide anion (O2-). Both effects were further increased by co-stimulation of macrophages with MAF. Second, exposure to BV together with MAF (or with recombinant murine interferon-gamma) led to acquisition by macrophages of the capacity to destroy the intracellular parasite Leishmania enriettii; such activated macrophages were also lytic towards P815 mastocytoma indicator target cells. These cytotoxic properties failed to develop in the absence of MAF. The BV-dependent increase in metabolic and functional activities was of the same magnitude as that induced by incubation of macrophages with 10 ng/ml of bacterial lipopolysaccharide (LPS). Residual contamination of BV by endotoxin was however much lower. In addition, polymyxin B, a LPS inhibitor, blocked the effect of LPS without significantly affecting macrophage stimulation by BV. These experiments indicate that BV can markedly stimulate macrophage metabolic and functional parameters that are important for host defense against pathogens and tumors.
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PMID:Stimulation by a bacterial extract (Broncho-Vaxom) of the metabolic and functional activities of murine macrophages. 255 25

The reversible binding of phage G13, a phi X174-like single-strand DNA phage, to a 3H-labelled nonasaccharide from the lipopolysaccharide of its natural host Escherichia coli C was studied with equilibrium dialysis. The binding constant (Ka) was determined to 1.3 x 10(7) M-1 in Scatchard and Lineweaver-Burk plots. Approximately one saccharide bound per G13 phage particle which suggests that only one of the 12 spikes in each G13 virion was engaged in the phage/receptor saccharide interaction. Equilibrium dialysis inhibition experiments with saccharides from lipopolysaccharides of an isogenic series of Salmonella typhimurium mutants showed that hepta- and pentasaccharides from two G13-sensitive bacteria, i.e., with efficiencies of plating of 0.1-1.0 compared to E. coli C, were efficient inhibitors with Ka-values greater than or equal to 1.2 x 10(7) M-1. The octa- and hexasaccharides from two G13 resistant strains, with efficiency of plating less than or equal to x 10(-4), were either greater than 1000-fold or greater than 15-fold less efficient as inhibitors with Ka-values less than or equal to 8.8 x 10(5) M-1. The results show that phage G13 binds in a specific and reversible way to penta-, hepta-, and nonasaccharides from G13 sensitive bacteria with the specificity residing in the hexose and heptose region of the core lipopolysaccharide.
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PMID:Interaction between phage G13 and its oligosaccharide receptor studied by equilibrium dialysis. 270 69

Twenty-nine murine monoclonal antibodies (MAbs) were prepared against antigenic determinants in the core and lipid A regions of Escherichia coli and Salmonella minnesota lipopolysaccharide (LPS). At least eight distinct MAb specificities were identified. Epitopes recognized by MAbs bearing these specificities were localized in the hexose, heptose, and 2-keto-3-deoxy-D-manno-octulosonic acid regions of the core oligosaccharide and on lipid A. Two groups of MAbs exhibited multispecificity for similar but distinct core- and lipid A-related epitopes. Some core-reactive MAbs cross-reacted with corresponding E. coli and Salmonella rough mutant chemotypes; others were specific for E. coli J5 LPS. Lipid A-specific MAbs reacted with free lipid A from diverse sources. Few MAbs reacted with smooth LPS. Antibody cross-reactivity was restricted by inter- and intraspecies differences in covalent core structure and by epitope concealment by overlying O-side chain and core sugars. The putative cross-reactive and antiendotoxic properties of MAbs specific for the core-lipid A complex may be limited by the inability of such MAbs to recognize determinants on "native" LPS.
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PMID:Specificity and cross-reactivity of monoclonal antibodies reactive with the core and lipid A regions of bacterial lipopolysaccharide. 291 51

The chemical composition and classical biologic activities of lipopolysaccharide (LPS; phenol-water) and endotoxin (butanol-water) preparations from virulent Treponema hyodysenteriae and avirulent Treponema innocens were examined. The LPS and endotoxin preparations from T. hyodysenteriae B204 contained approximately 80.9 and 35.2% hexose, 0.12 and 0.45% thiobarbituric acid-reactive compound, and less than 1 and 11.3% protein, respectively. The LPS and endotoxin preparations of T. innocens B1555a contained approximately 56.3 and 37.8% hexose, 0.45 and 0.4% thiobarbituric acid-reactive compound, and less than 1 and 26% protein, respectively. A silver-stained 7.5 to 15% sodium dodecyl sulfate-polyacrylamide gel showed four bands for the T. hyodysenteriae preparations, while the T. innocens preparations failed to resolve into discrete bands on electrophoresis. We determined by the Limulus amebocyte lysate assay that the treponemal preparations had comparable amounts of endotoxin activity when Escherichia coli LPS was used as a standard. The 50% lethal doses of LPS and endotoxin from T. hyodysenteriae for BALB/cByJ mice were 380 and 80 micrograms, respectively. The treponemal preparations were poor adjuvants, failed to induce a dermal Shwartzman reaction, and were not pyrogenic. The treponemal LPS preparations, unlike the endotoxin preparations, were not mitogenic for murine spleen cells. Differences in virulence between the two treponemal species could not be associated with the biologic activities of the respective LPS or endotoxin moieties, but the endotoxin preparations were consistently more active than the purified LPS preparations.
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PMID:Comparison of the biological responses induced by lipopolysaccharide and endotoxin of Treponema hyodysenteriae and Treponema innocens. 291 84

The influence of tumour promoters and growth factors on glycolysis and on fructose-2,6-bisphosphate concentration was studied in isolated mouse spleen lymphocytes and in purified B-cells. The intracellular concentration of fructose 2,6-bisphosphate and the rate of lactate release were increased 2-3-fold in spleen lymphocytes exposed to active phorbol esters, mitogenic lectins, interleukin 4 or lipopolysaccharide. The maximal effect was observed after 1 h of exposure. In these cells hexose 6-phosphates increased 2-fold and 6-phosphofructo-2-kinase activity remained unchanged after treatment with phorbol 12,13-dibutyrate or with lectins. Exposure of B-cells to phorbol 12,13-dibutyrate, interleukin 4 or lipopolysaccharide increased the glycolytic flux and the concentration of fructose 2,6-bisphosphate without relation to their mitogenic activity. Lymphocytes and rat liver 6-phosphofructo-2-kinase were partially purified using the same procedure. The lymphocyte enzyme was not inhibited by sn-glycerol 3-phosphate in contrast to the potent inhibition observed in liver. Treatment of both enzymes with the catalytic subunit of the cyclic-AMP-dependent protein kinase failed to inactivate 6-phosphofructo-2-kinase from lymphocytes. These differences suggest that lymphocytes and liver contain different forms of this enzyme.
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PMID:Phorbol 12,13-dibutyrate and mitogens increase fructose 2,6-bisphosphate in lymphocytes. Comparison of lymphocyte and rat-liver 6-phosphofructo-2-kinase. 296 4

Structural studies on the O-specific polysaccharide of Citrobacter PCM 1487 lipopolysaccharide, using methylation analysis, Smith degradation and 1H-NMR spectroscopy, indicate that it consists of the trisaccharide repeating units (formula, see text) In this structure, 4-deoxy-D-araHex stands for 4-deoxy-D-arabino-hexose.
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PMID:Citrobacter lipopolysaccharides: structure elucidation of the O-specific polysaccharide from strain PCM 1487 by mass spectrometry, one-dimensional and two-dimensional 1H-NMR spectroscopy and methylation analysis. 298 2


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