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

The structure of the 4-amino-L-arabinose-lacking lipopolysaccharide of the Proteus mirabilis Rc-type mutant R4, derived from wild-type O28, was elucidated. The lipopolysaccharide core structure has previously been partially characterized. The linkage between heptose and deoxyoctulosonic acid(dOclA) is now reported, as well as the structure of the lipid A moiety of this mutant strain. Besides the tentative identification of an alpha-linked glucosamine disaccharide in the lipid A backbone accompanying the usual beta 1----6-linked glucosamine-disaccharide, the only significant structural variation to previous studies was the lack of substitution of the C-4' phosphate by 4-amino-L-arabinose. In addition, the substitution at C-8 of one dOclA unit by 4-amino-L-arabinose, previously reported for the R45 mutant of P. mirabilis 1959, is lacking in this R mutant. Also in addition to previous findings, the terminal unit of heptose was found to be substituted at C-7 with phosphorylethanolamine (PEtN) and not only with phosphate, although this substitution is not complete as demonstrated by the relevant signals in 31P-NMR. Additional studies with the wild-type strain P. mirabilis O28 revealed the presence of 4-amino-L-arabinose in both the core and the lipid A regions suggesting that the R4 mutant is defective in the biosynthesis of this amino sugar rather than in its transfer. Otherwise the lipid A regions of the mutant and the wild-type strain show no structural differences. The following formula is proposed for the lipopolysaccharide of 4-amino-L-arabinose-lacking mutant R4/O28 P. mirabilis: (Formula; see text)
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PMID:Structural studies on the core and lipid A region of a 4-amino-L-arabinose-lacking Rc-type mutant of Proteus mirabilis. 328 Mar 11

Pure lipopolysaccharide extracted from Selenomonas spp. isolated from human periodontal pockets was composed of 23.7% carbohydrate, 16.5% hexosamine, 1.2% 2-keto-3-deoxyoctonate, 0.7% heptose, 26.0% lipid, 1.8% protein, and 1.3% phosphorus. It was shown to be quite lethal, to have very active pyrogenicity, to give a typical biphasic-fever response, and to produce a positive local Shwartzman reaction.
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PMID:Biological and chemical characterization of lipopolysaccharide from Selenomonas spp. in human periodontal pockets. 351 46

A highly purified bacterial lipopolysaccharide (LPS) preparation was exposed in water to megadoses of ionizing radiation from a 60Co source. As evidenced by electrophoresis, the radiation treatment progressively degraded the lipopolysaccharide molecules by removing first the O-side chain units and then components of the R-core. Chemical analysis of the irradiated (LPS) preparations showed that, in accord with the structural changes, the most profound effects of ionizing radiation occurred in the hydrophilic oligo/polysaccharide moieties (R-core and O-side chain). Progressively higher doses of radiation degraded the simple sugars in decreasing order of galactose, galactosamine, glucosamine, glucose, and heptose. The R-core component 2-keto-3-deoxyoctonate was the most "resistant" sugar derivative to ionizing radiation. Due to its central position in the LPS aggregates in water, even at comparatively high doses of radiation the hydrophobic lipid A moiety of endotoxin was less affected than the sugar components. Of the fatty acids of lipid A, however, either partial conversion of beta-hydroxymyristic acid into myristic acid or selective loss of the former occurred. The observed structural and chemical changes of LPS are consistent with the effect of active oxygen radicals of radiolysis. In addition, the extensive physicochemical changes explain the altered biological reactivity of radiation-treated endotoxins.
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PMID:Modification of the chemical composition and structure of the U.S. Reference Standard Endotoxin (RSE) by 60Co radiation. 351 96

The chemical constitutional analysis of the lipopolysaccharide (LPS) isolated from Providencia rettgeri was carried out. Polyacrylamide gel electrophoresis using sodium dodecylsulfate or sodium deoxycholate showed that the lipopolysaccharide mostly consisted of short sugar chains. The lipid A was precipitated out after mild acid hydrolysis of LPS. From the supernatant degraded polysaccharide and unsubstituted core fractions were isolated. Compositional analysis of the core material revealed the presence of galacturonic acid, galactose, glucose, glucosamine, L-glycero-D-manno-heptose, 3-deoxy-D-manno-octulosonic acid, alanine and phosphorus. Methylation analysis of the core material indicated the presence of terminal units of glucose, galacturonic acid and glucosamine. The chemical structure of the lipid A was elucidated. It constitutes a beta-1,6-glucosamine disaccharide substituted on either side by ester and glycosidically-bond phosphate residues. The ester-bound phosphate was found to be substituted by a 4-amino-4-deoxy-L-arabinosyl residue. The amino groups of the backbone disaccharide are N-acylated by 3-O-(14:0)14:0 and 3-O-14:0. Two hydroxyl groups of the disaccharide are esterified by 3-O-(14:0)14:0 and 3-O-14:0. The taxonomical importance of these structural details will be discussed.
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PMID:Lipopolysaccharide of Providencia rettgeri. Chemical studies and taxonomical implications. 352 98

Short tail fibres of T-even like phages are involved in host recognition. To determine the specificity of the fibres, the region containing gene 12 of phages T2, K3, and K3hx was cloned. The genes 11, 12, wac, and 13, coding for the baseplate outer wedge, short tail fibres, collar wishes, and a head completion component, respectively, were localized on the cloned fragments. Plasmid-encoded gene 12 could be expressed without helper phage. Efficient expression of gene 12 from T2 and K3hx made an extraction of protein 12 possible. Hybrid phages obtained by in vitro complementation, recombination analysis and protein 12 binding to host range mutant bacteria excluded a role of the short tail fibres from T2, K3 or K3hx in the recognition of outer membrane proteins. Binding patterns of protein 12 to different Escherichia coli lipopolysaccharide mutants and inhibition of binding of protein 12 by a monoclonal antibody against the core region of E. coli K12 lipopolysaccharide suggested that heptose residues are necessary for efficient binding. The binding site of the same monoclonal antibody is different from the short tail fibre binding site in an E. coli B strain suggesting different binding specificities of protein 12. Thus, the ability of different bacterial strains to inactivate phage could be related to differences in the binding specificity of the short tail fibres for the lipopolysaccharides of these bacteria.
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PMID:Receptor specificity of the short tail fibres (gp12) of T-even type Escherichia coli phages. 355 59

Endotoxin (lipopolysaccharide, LPS) from an oral strain of Bacteroides intermedius was isolated by phenol extraction and purified by ultracentrifugation and gel filtration. The preparation was essentially free from contaminating nucleic acid and protein. The LPS contained rhamnose, fucose, mannose, glucose, galactose, glucosamine, and an unidentified sugar (approximate molar ratios 9:1:6:3:1:7:2). Neither heptose nor 2-keto-3-deoxyoctonate was detected. The major fatty acids were 3-hydroxy-15-methylhexadecanoic acid and 3-hydroxyhexadecanoic acid. The LPS was homogeneous with regard to molecular size, and its polysaccharide chain appeared short compared to the E. coli 055 LPS which was used as reference. A molecular weight of approximately 7,800 was estimated from gas chromatography data and by gel filtration in the presence of sodium deoxycholate. The B. intermedius LPS demonstrated low potency in the Limulus amoebocyte lysate assay, and in the chick embryo and mouse lethality tests and gave negative response in the local Shwartzman reaction.
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PMID:Chemical composition and biological properties of a lipopolysaccharide from Bacteroides intermedius. 375 80

The mechanism through which human blood platelets interact with gram-negative bacteria with well-defined structural variations in endotoxic lipopolysaccharide was studied. Secretion of 14C-serotonin and aggregation of platelets separated from plasma proteins were observed on challenge with rough mutant Re595 of Salmonella minnesota possessing a glycolipid outer layer composed of Lipid A and 2-keto-3-deoxyoctonate (KDO) but lacking heptose phosphate in the core and O-polysaccharide in its outer portion. Both 14C-serotonin secretion and platelet aggregation were concentration-dependent, with a half-maximum response at the ratio of one bacterial colony-forming unit (CFU) to two platelets. The aggregation of human platelets induced by mutant Re595 was divalent cation-dependent and required secretion of ADP and fibrinogen from platelet storage granules because it was inhibited by chelators, by the ADP-splitting enzyme apyrase, and by monospecific antifibrinogen Fab fragments. The synthetic peptide analog of the platelet receptor recognition site on the gamma chain of fibrinogen, gamma 400-411, inhibited platelet aggregation induced by mutant Re595 (IC50 160 mumol/L), whereas serotonin secretion was unaffected. Tetrapeptide, RGDS, analogous to human fibrinogen alpha chain (alpha 572-575) and to the cell adhesion site of fibronectin, also inhibited aggregation induced by mutant Re595 (IC50 60 mumol/L). Secretion of 14C-serotonin was preceded by a very rapid phosphorylation of a platelet protein of mol wt 47,000, which is associated with protein kinase C activation. Myosin light chain (mol wt 20,000) was also phosphorylated. Both phosphoproteins were dephosphorylated while secretion was reaching maximum. Furthermore, release of 3H-arachidonic acid from platelet phospholipids and generation of thromboxane B2 via the cyclooxygenase pathway were observed. Inhibition of this pathway with acetylsalicylic acid (10(-4) mol/L) or indomethacin (5 X 10(-4) mol/L) reduced 14C-serotonin secretion and platelet aggregation. The role of Lipid A in the interaction of mutant Re595 with human platelets was deduced from the inhibitory effect of the Lipid A-binding protein present in Limulus amebocyte lysate. Likewise, polymyxin B, known to complex with Lipid A, was inhibitory. The reactivity of mutant Re595 toward platelets was attenuated by mild acid hydrolysis, during which KDO was dissociated from the glycolipid, and by alkaline hydrolysis, which breaks ester-linked fatty acids in Lipid A. In contrast to mutant Re595, strain S218 of S minnesota bearing "complete" endotoxic lipopolysaccharide did not induce secretion and aggregation of human platelets.(ABSTRACT TRUNCATED AT 400 WORDS)
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PMID:Mechanism of human platelet activation by endotoxic glycolipid-bearing mutant Re595 of Salmonella minnesota. 376 28

Lipopolysaccharide was isolated from a phage-selected mutant of a wild strain of Aeromonas salmonicida by the aqueous phenol method. The lipopolysaccharide consisted of the R form, containing per mole, three moles of L-glycero-D-manno-heptopyranose, one mole of 3-deoxy-D-manno-2-octulosonic acid (dOclA) and lipid A. The dOclA was not fully assayable by the thiobarbituric acid methods usually used, but its degradation product was detected, after Smith degradation of the lipopolysaccharide, either as free 3-deoxy-2-heptulosonic acid (after hydrolysis) or substituted by a mannopyranosyl residue derived from heptose. Mass spectrometry indicated that the dOclA existed in the furanose form and was substituted by the heptose trisaccharide through position six. Methylation analysis, chemical degradation, chromium trioxide oxidation and nuclear magnetic resonance spectroscopy were used to identify the structure of the core oligosaccharide as: L alpha DHepp(1----2)L alpha DHepp(1----3)L alpha DHepp(1----6)dOclAf(2----.
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PMID:The structure of the heptose-3-deoxy-D-mannooctulosonic-acid region in a mutant form of Aeromonas salmonicida lipopolysaccharide. 378 Jul 44

Capsular structure and biochemical composition varied between two isolates (virulent and avirulent) of Haemophilus pleuropneumoniae serotype 5. The presence of capsule was determined by transmission electron microscopy with glutaraldehyde-osmium, ruthenium red, alcian blue, and phosphotungstic acid staining procedures. The virulent isolate of H. pleuropneumoniae had a distinct, adherent capsule. The avirulent isolate had a fragile, easily removed capsule. Capsular material (CM) and a lipopolysaccharide (LPS) were isolated from each bacterial isolate and were compared biochemically and biologically. CM from both isolates contained carbohydrates, no detectable protein, and no detectable to trace amounts of lipid A. Each LPS contained heptose, hexose, galactose, glucosamine, 2-keto-3-deoxyoctonate, and lipid A. Biological responses to CM and LPS from both isolates were demonstrated in the proclotting enzyme of Limulus polyphemus amebocyte lysate activation and in serological cross-reactions by immunofluorescence and immunodiffusion precipitation. The virulent isolate contained approximately 10 mg of LPS per g more on an original dry weight basis than the avirulent isolate. LPS from the virulent isolate contained approximately 13 times more galactose than LPS from the avirulent isolate. The differences of capsular structure and biochemical composition may contribute to the role of CM in porcine H. pleuropneumoniae infections.
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PMID:Morphological and biochemical comparison of virulent and avirulent isolates of Haemophilus pleuropneumoniae serotype 5. 394 95

Lipopolysaccharide components 3-deoxy-D-manno-2-octulosonic acid and L-glycero-D-manno-heptose were detected in hydrolysates from whole cells of Neisseria elongata by gas-liquid chromatography. Cells from a single plate were hydrolyzed, and carbohydrate components were converted to aldononitrile and O-methyloxime acetate derivatives for subsequent analyses by gas-liquid chromatography. 3-Deoxy-D-manno-2-octulosonic acid was well separated from other cell components as the O-methyloxime acetate derivative. With both derivatives, L-glycero-D-manno-heptose was readily identified by their different retention times. The procedure requires only a relatively small number of cells, and detection is accomplished without prior isolation of the lipopolysaccharide.
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PMID:Detection by gas chromatography of 3-deoxy-D-manno-2-octulosonic acid and L-glycero-D-manno-heptose in whole cells of Neisseria elongata. 395 40


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