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

On mild acid degradation of the Pseudomonas cepacia serotype 6 lipopolysaccharide, the O-specific polysaccharide was obtained, which contains D-mannose and D-galactose residues in the ratio approximately 1:1, as well as O-acetyl groups. On the basis of 1H and 13C NMR analysis, calculation of specific optical rotation, and methylation, it was concluded that the polysaccharide possesses the following structure: (formula; see text) Regularities in glycosidation effects in 13C NMR spectra of 1,3-linked disaccharides containing furanoside residues are discussed.
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PMID:[Antigenic polysaccharides of bacteria. 33. The structure of O-specific polysaccharide chain of lipopolysaccharide from Pseudomonas cepacia serotype 6]. 246 65

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

The lipopolysaccharide produced by Salmonella livingstone (O:6,7) was composed of an antigenic O-polysaccharide which was shown by composition, methylation analysis, and high resolution nuclear magnetic resonance studies to be a high molecular weight polymer containing D-glucose, 2-acetamido-2-deoxy-D-glucose, and D-mannose residues (1:1:4) composed in a repeating hexasaccharide unit having the structure: (formula; see text)
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PMID:Structure of the lipopolysaccharide antigenic O-chain produced by Salmonella livingstone (O:6,7). 247 61

Chemical and serological characterization of the Pseudomonas fluorescens IMV 2763 (biovar G) lipopolysaccharide was carried out. The O-specific polysaccharide chain of the lipopolysaccharide is composed of D-mannose, 6-deoxy-L-talose, N-acetyl-D-galactosamine and O-acetyl groups in the ratio of approximately 2:1:1:1. The polysaccharide is branched and a half of residues of 6-deoxytalose and monosubstituted mannose carry O-acetyl groups. On the basis of methylation, partial acid hydrolysis and 13C NMR analysis it was concluded that the repeating unit of the polysaccharide has the following structure: (formula; see text)
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PMID:[Antigenic bacterial polysaccharides. 36. A study of the structure of the O-specific polysaccharide chain of the lipopolysaccharide of Pseudomonas fluorescens IMV 2763 (biostrain G)]. 248 48

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

A new lectin has been isolated from the coral Gerardia savaglia by affinity chromatography, using locust gum as an absorbent, and D-mannose as eluant. Final purification was achieved by Bio-Gel P300 gel filtration. The agglutinin is a protein composed of two polypeptide chains with a Mr of 14800; the two subunits are not linked by disulfide bond(s). The isoelectric point is 4.8, the amino acid composition is rich in the acidic amino acids aspartic acid and glutamic acid. The absorption maximum for the protein was at 276 nm; with a molar absorption coefficient of 1.27 X 10(5) M-1 cm-1. The lectin precipitated erythrocytes from humans (A, B and O), sheep, rabbit and carp with a titer between 2(5) and 10(10); the affinity constant for lectin binding to sheep red blood cells was 2.8 X 10(8) M-1 and the number of binding sites, 3.2 X 10(5)/cell. Ca2+ ions are required for full activity; the pH optimum lies in the range between 6 and 11. Inhibition experiments revealed that the lectin is specific for D-mannose. The lectin is mitogenic only for those spleen lymphocytes from mice which had been activated by lipopolysaccharide. An interesting feature of this lectin is its ability to bind to glycoproteins present in nuclei from CV-1 monkey kidney cells. The fluorescein-isothiocyanate-labelled lectin reacted with six polypeptides in the nuclear envelope from rat liver (Mr 190,000, 115,000, 80,000, 62,000, 56,000 and 42,000) and with two polypeptides in the nuclear matrix or pore complex lamina fraction (Mr 190,000 and 62,000). The lectin inhibited the nuclear envelope mRNA translocation system in vitro. It is suggested that this effect is due to an interaction of the lectin with the nuclear glycoproteins gp190 and/or gp62.
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PMID:A D-mannose-specific lectin from Gerardia savaglia that inhibits nucleocytoplasmic transport of mRNA. 289 May 21

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


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