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

Klebsiella pneumoniae serotype 1 and serotype 2 and their capsular variants were examined for production of cell-associated capsular polysaccharides and extracellular capsular polysaccharides. The virulence of these organisms in experimental animals was examined via intraperitoneal injection in mice and transtracheal inoculation into the lungs of rats. It was found that the production of either polysaccharide component correlated with the observed virulence. The extracellular polysaccharides were purified by ethanol precipitation, electrodialysis, extraction with quaternary ammonium salts, and gel filtration. These purification steps allowed for the separation and purification of both the extracellular lipopolysaccharide and the extracellular capsular polysaccharide. Purified extracellular capsular polysaccharide and extracellular lipopolysaccharide were co-injected with K. pneumoniae intraperitoneally into mice to determine if either of these substances would produce an effect on the natural course of infection in these animals. These studies showed that only purified extracellular lipopolysaccharide enhanced the virulence of K. pneumoniae when co-injected into mice, and this virulence enhancement correlated with the content of extracellular lipopolysaccharide, but not extracellular capsular polysaccharide in mixtures of these polysaccharides. Saponification of K. pneumoniae serotype 1 extracellular polysaccharides significantly decreased their virulence-enhancing capabilities in mice, further suggesting that extracellular lipopolysaccharide may play a role in these infections.
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PMID:Extracellular polysaccharide production by Klebsiella pneumoniae and its relationship to virulence. 389 Oct 56

Partially purified water extract was obtained from the initial water extract by ultracentrifugation. Nine protein fractions differing in molecular weight, homogeneity and the content of lipopolysaccharide (LPS) were obtained by stepwise precipitation with ammonium sulfate and subsequent fractionation in columns packed with Sephadex G-100 and DEAE cellulose. Two protein fractions with a molecular weight of 30000 and 40000 daltons were practically free of LPS. These fractions were homogeneous as shown by analytical centrifugation and formed a single precipitation line with P. aeruginosa antiserum; both fractions were found to be antigenically identical. In the enzyme immunoassay these two fractions proved to be least active in comparison with the other protein fractions, but when used for the immunization of rabbits, they induced the formation of specific protective (for mice) antibodies. Both antisera were equally active in the experiments of the passive protection of mice. The isolated LPS-free proteins are supposed to be the proteins of the outer membrane of P. aeruginosa cell wall and have the properties of protective antigens.
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PMID:[Protective protein antigens of Pseudomonas aeruginosa]. 393 89

Various uniform salt forms of an R-form lipopolysaccharide (LPS) extracted from Klebsiella strain LEN-111 (O3-:K1-) were prepared and their ultrastructure was examined. The LPS, which was extracted by the phenol-water method, freed from contamination with RNA by treatment with RNase, and precipitated by addition of two volumes of 10 mM MgCl2-ethanol, was used as the original preparation for uniform salt forms. The original LPS preparation formed a hexagonal lattice structure with a lattice constant of 14.9 +/- 0.2 nm. The LPS after electrodialysis retained the ability to form a hexagonal lattice structure, although its lattice constant was large (18.7 +/- 0.5 nm) and the lattice structure of the electrodialyzed LPS was labile at pH 8.0 in contrast to that of the original LPS preparation. The magnesium salt form of the LPS formed essentially the same ordered hexagonal lattice structure (lattice constant of 15.0 +/- 0.2 nm) as that of the original LPS preparation. The calcium and ammonium salt forms formed a hexagonal lattice structure, but the lattice constants of the calcium and ammonium salt forms were larger (18.6 +/- 0.6 nm and 19.3 +/- 0.4 nm, respectively) than that of the magnesium salt form. The sodium and potassium salt forms consisted of freely branching ribbon-like structures with an average width of 13 nm and an average thickness of 9 nm. The triethylamine salt form consisted principally of short rods (10 nm X 9-13 nm).
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PMID:Formation of a hexagonal lattice structure by an R-form lipopolysaccharide of Klebsiella: relationship between lattice formation and uniform salt forms. 409 71

Colicin D-CA23, obtained by sonic treatment of mitomycin C-induced cells of Escherichia coli K-12 W1485 (colD), was purified by ammonium sulfate precipitation, gel filtration on Sephadex G200, ion-exchange chromatography on diethylaminoethyl cellulose, and isoelectrofocusing. Polyacrylamide-gel electrophoresis, sedimentation velocity analysis, and antigenic analysis indicated that the preparation was homogeneous. Colicin D is composed entirely of amino acids and hence is a simple protein uncomplexed with lipid or lipopolysaccharide. It contains six residues of cysteine per molecule. The molecular weight of colicin D is approximately 92,000, as determined by sodium dodecyl sulfate-polyacrylamide-gel electrophoresis and gel filtration on Sephadex G200. Its sedimentation coefficient is 4.41S. The behavior of colicin D in solutions of sodium dodecyl sulfate and 2-mercaptoethanol indicates that it does not consist of subunits and exists as a single polypeptide chain. Its high molecular weight and presence of six cysteine residues per molecule distinguish colicin D from all colicins previously described. Although colicins D and E3 have similar modes of action, their gross molecular properties are entirely different.
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PMID:Purification and characterization of colicin D. 462 24

Electron microscopy has confirmed previous studies and has provided much new information on the mechanism of endotoxin-platelet interaction. The Boivin lipopolysaccharide preparation is particulate, and on electron microscope examination appears as a three-layered structure, morphologically similar to bacterial cell wall. In vitro and in vivo experiments have demonstrated that these endotoxin particles adhere to platelets. In some species, particularly the rabbit, this is associated with loss of platelet contents, due to lysosomal and cell membrane lysis, resulting in platelet sphering and apparent cell death. Serial observation of degranulating platelets and metabolic studies indicate that although some platelet engulfment of endotoxin occurs, degranulation is not dependent upon phagocytosis. Several observations suggest that these endotoxin effects are mediated through immune mechanisms: (1) Inactivation of complement in the suspending plasma by heating to 56 degrees C, anticoagulation with EDTA, a reaction temperature of 5 degrees C, ammonium hydroxide incubation, and adsorption with either zymosan or washed antigen-antibody complexes, inhibits both endotoxin adherence and platelet degranulation. (2) The reaction requires a plasma cofactor, possibly antibody, which can be adsorbed out by endotoxin. (3) Endotoxin adheres selectively to nonprimate platelets and primate red cells, a pattern conforming to immune adherence, a phenomenon requiring antigen, antibody, and complement. It is suggested that endotoxin-induced platelet damage is dependent upon the intimate contact provided by immune adherence. We have not established whether degranulation is an endotoxin or complement effect. The species variation in susceptibility to endotoxin also merits further investigation.
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PMID:An ultrastructural study of the mechanisms of platelet-endotoxin interaction. 496 86

A new technique for purification of bacterial pili was developed and applied to Escherichia coli strains isolated from the urine of patients with symptomatic urinary tract infections. After mechanical detachment from the bacterial cells, the pili were concentrated by precipitation with ammonium sulfate, dialyzed, and solubilized in buffer containing deoxycholate. The fraction containing the pili was purufied further by ultracentrifugation in a sucrose gradient and by elution through a Sepharose 4B column in 6 M urea buffer. The pilus filaments were not dissociated by concentrated urea and were eluted in the void volume of the column. The purified pili had a molecular weight of 17,000. The isoelectric point of the pili from one of the strains was 4.9, and about 43% of the amino acids were hydrophobic. Hyperimmunesera raised in rabbits against the purified pili did not contain detectable antibodies to the lipopolysaccharide O antigen or to the capsular polysaccharide K antigen of the homologous strain. The pili obtained by this purification procedure are free from other detectable bacterial surface antigens, and the purified pilus filaments are of relatively homogeneous size. This procedure enables purification of the pili also from flagellated strains.
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PMID:New Method for isolation of immunologically pure pili from Escherichia coli. 610 71

A new procedure was developed for the purification of pili from Escherichia coli and Salmonella typhimurium. The pili were removed from the bacterial cells by mechanical agitation and then concentrated by precipitation with ammonium sulfate. After dialysis, the pili were solubilized in a buffer containing deoxycholate. This treatment did not solubilize the outer membrane proteins. The pili were then separated by ultracentrifugation in a sucrose gradient and finally passed through a Sepharose 4B column in a 6 M urea buffer. The pili were not dissociated by concentrated urea and they eluted in the void volume of the Sepharose 4B column. Because the enterobacterial flagella dissociate in concentrated urea, this procedure enables the purification of the pili from the flagellated strains also. The purified pilus proteins were free from lipopolysaccharide and outer membrane proteins. The molecular characteristics and the binding properties of these pilus proteins are briefly described.
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PMID:Purification of pili from Escherichia coli and Salmonella typhimurium. A preliminary report. 611 Nov 21

The local immune response to pili of Escherichia coli O6:K13:H1 was determined in experimental hematogenous pyelonephritis in rabbits. Pili purified from sheared cells by ammonium sulfate precipitation were found to be pure by electron microscopy and negative for lipopolysaccharide by limulus lysate assay. Antipilus antibody was detected in serum and newly synthesized protein from infected animals with enzyme-linked immunosorbent assay. Serum and local (intrarenal) antibodies were of the immunoglobulin G class, were detectable by day 20 of infection, and persisted though 250 days of infection. These data suggest that pili are present on the organism at the site of infection, since they induce the local synthesis of antipilus antibody in experimental pyelonephritis.
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PMID:Local immune response to Escherichia coli pili in experimental pyelonephritis. 611 36

In mice, active protection against Pseudomonas aeruginosa could be induced with two fractions derived from a crude preparation of ribosomes from P. aeruginosa. The two fractions were obtained by gel filtration chromatography of the crude ribosomal preparation on Sepharose CL-2B. In fraction I, less than 1% of the ribonucleic acid (RNA) applied to the column was recovered. Fraction II contained RNA and protein in a ratio of 1.94. The presence of ribosomes in this fraction was confirmed by analysis on a sucrose density gradient. The protection by fraction I was not affected by treatment with ribonuclease; in contrast, incubation of fraction II with ribonuclease completely abolished active protection. Fraction I contained lipopolysaccharide (LPS) as was indicated by the presence of 2-keto-3-deoxyoctonic acid. No LPS was found in fraction II. The adjuvant dimethyl dioctadecyl ammonium bromide enhanced the protection by fraction II; however, immunity by a low dose of fraction I was abolished by dimethyl dioctadecyl ammonium bromide. Protection by fractions I and II appeared to be restricted to the homologous serotype of P. aeruginosa. These results indicate that RNA is required for protection by fraction II. Active protection by fraction I is likely due to LPS.
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PMID:Ribonuclease-sensitive ribosomal vaccine of Pseudomonas aeruginosa. 615 37

Klebsiella O3 lipopolysaccharide (KO3 LPS) isolated from the culture supernatant, which was found to exhibit a very strong adjuvant activity in augmenting antibody response and delayed-type hypersensitivity to protein antigens in mice, was examined by electron microscopy. When negatively stained with uranyl acetate or ammonium molybdate, the KO3 LPS was found to consist principally of flat ribbon-like structures branching freely (average width 16 nm and average thickness 7 nm) and to contain a small proportion of spheres (diameter 20-50 nm), both structures covered with fine hairy structures (average length approximately 10 nm). When the polysaccharide of KO3 LPS was stained by the periodic acid-thiosemicarbazide-silver proteinate procedure, silver granules were deposited on the ribbon-like structures and around the spheres, suggesting that the polysaccharide moiety is located on their surface and that the fine hairy structures consist of the polysaccharide moiety. Comparison by means of preparations stained with uranyl acetate or ammonium molybdate showed that KO3 LPS isolated from the culture supernatant has structural features in common with KO3 LPS isolated from bacterial cells, Escherichia coli O9 LPS isolated from the culture supernatant, and E. coli O127 LPS isolated from bacterial cells. On the basis of the present results, schematic representations of the common physical structure of LPS were drawn; the fine hairy structures attach to the wide surface of the flat ribbon-like structures along their lateral margin.
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PMID:Ultrastructure of Klebsiella O3 lipopolysaccharide isolated from culture supernatant: comparison with other lipopolysaccharides. 620 77


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