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

Mergenhagen, Stephan E. (National Institutes of Health, Bethesda, Md.). Polysaccharide-lipid complexes from Veillonella parvula. J. Bacteriol. 90:1730-1734. 1965.-A strain of Veillonella parvula (V2) elaborates an extracellular slime when grown in a nutrient medium containing only dialyzable components. Deproteinization with chloroform-butanol of ethyl alcohol-precipitated material from the supernatant culture fluid leads to the isolation of a water-soluble lipopolysaccharide (LPS1). Another component (LPS2), showing similarity in biological and immunological properties to the endotoxic antigen (LPC) isolated from whole cells, was extracted with phenol from the insoluble emulsion remaining after chloroform-butanol extraction of slime. Analysis of polysaccharides by thin-layer chromatography demonstrated the presence of glucose and galactose in LPS1 and glucose, glucosamine, galactosamine, and a methyl pentose in LPC. LPS1 failed to give a positive epinephrine skin test after intravenous injection in rabbits and failed to kill pertussis-sensitized mice, whereas LPS2 and LPC were active in both of these bioassays. Both lipopolysaccharides (LPS1 and LPC) exhibited type-specific haptenic activity in hemagglutination tests with numerous anti-Veillonella rabbit sera. LPS1 was found in these tests to be unrelated to a heterologous strain of Veillonella possessing a related somatic antigen. These experiments reveal the presence of two chemically and immunologically distinguishable polysaccharide-lipid complexes in this strain of V. parvula.
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PMID:Polysaccharide-lipid complexes from Veillonella parvula. 585 93

Previously we found that Klebsiella O3 lipopolysaccharide (KO3 LPS) isolated from culture supernatant of strain Kasuya (O3: K1) or its decapsulated mutant strain LEN-1 (O3: K1-) exhibited very strong adjuvant activity in augmenting antibody response and delayed-type hypersensitivity to protein antigens in mice. The preparation of KO3 LPS after deproteinization by four cycles of treatment with chloroform-butanol (5: 1) usually contained a small percentage of proteins and a definite amount of another antigen which was destroyed by heating at 100 C for 1 hr. This antigen proved to be derived from type 1 fimbriae which are responsible for mannose-sensitive hemagglutination of guinea pig erythrocytes. The preparation of KO3 LPS isolated from culture supernatant of the strains which did not produce type 1 fimbriae exhibited strong adjuvant activity similar to that of the preparation from those which produced them. The preparation of KO3 LPS treated with hot phenol water which is known to remove lipid A-associated proteins exhibited a similar strong adjuvant activity. The preparation of KO3 LPS after extensive deproteinizing, two cycles of pronase treatment followed by ten cycles of treatment with chloroform-butanol, no longer contained detectable amounts of proteins and the fimbrial antigen, but this preparation also exhibited similar strong adjuvant activity. Moreover, there was no difference in strength of the adjuvant activity between the preparation of KO3 LPS isolated from culture supernatant and that isolated by the phenol method from bacterial cells. The present study demonstrates that the strong adjuvant activity of the preparation of KO3 LPS does not depend in any way on proteins contaminating the preparation.
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PMID:Adjuvant activity of Klebsiella O3 lipopolysaccharide: no contribution of proteins to the expression of adjuvant activity. 614 85

Fermentor growth of Bacteroides fragilis under controlled conditions in a complex medium containing 1% glucose and 10% fetal calf serum resulted in high yields of bacteria. After hot phenol-water extraction of the organisms, capsular polysaccharide was isolated from the aqueous phase and purified by Sephacryl S-300 chromatography in a buffer with 3% sodium deoxycholate. Lipopolysaccharide was isolated by phenol-chloroform-light petroleum ether extraction. The capsular polysaccharide from B. fragilis strain NCTC 9343 contained six sugars: L-fucose, D-galactose, D- and L-quinovosamine, D-glucosamine, and galacturonic acid. The capsule of strain ATCC 23745 also contained D-glucose, L-fucosamine, L-rhamnosamine, and a 3-amino-3,6-dideoxyhexose but lacked D-quinovosamine. The latter capsule also contained alanine (4%). The capsular polysaccharides were different immunochemically by ELISA inhibition. The lipopolysaccharide of both strains contained the same sugars (L-rhamnose, D-glucose, D-galactose, and D-glucosamine) and fatty acids (13-methyl-tetradecanoic and 3-hydroxy-hexadecanoic and 3-hydroxy-15 methyl-hexadecanoic as major constituents) and were identical by ELISA inhibition.
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PMID:Capsular polysaccharides and lipopolysaccharides from two Bacteroides fragilis reference strains: chemical and immunochemical characterization. 618 69

Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) of purified lipopolysaccharide (LPS) from Neisseria gonorrhoeae resulted in the formation of multiple bands. Many of the bands consisted of LPS aggregates, which could be dissociated by treatment with 0.1 M NaOH or by addition of 4 M urea to the separating gel. The unaggregated LPS was usually found in one to three bands toward the bottom of the gels, a result suggesting that a long repeating O antigen is not present on gonococcal LPS. SDS-PAGE of LPS from different LPS serotypes of N gonorrhoeae indicated that structural heterogeneity exists. Antigenic analysis by enzyme-linked immunosorbent assay inhibition of gonococcal LPS extracted with phenol-chloroform-petroleum ether (PCP) and phenol-water revealed that PCP-extracted LPS contained substantially less serotype-specific antigen than did phenol-water-extracted LPS. These results suggest that the PCP and phenol-water methods extract different molecular species of LPS from N gonorrhoeae.
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PMID:Electrophoretic and serological characterization of the lipopolysaccharide produced by Neisseria gonorrhoeae. 620 6

Endotoxic lipopolysaccharide and glycolipids ( RGl ) extracted from Salmonella minnesota wild type and R mutant cells ( chemotypes Ra, Rb, Rc, Rd1, and Rd2 ), respectively, with hot phenol-water (PW) and phenol-chloroform-petroleum ether (PCP) were analyzed chemically and electron microscopically. All RGl extracted with PW ( RGl -PW) contained excess amounts of phosphate, O-ester linked fatty acids and neutral sugars, while all RGl extracted with PCP ( RGl -PCP) contained excess amounts of free amino groups and fatty acids, in addition to the RGl constituents. Polyamine (cadaverine), phosphoethanolamine, and an unidentified amino compound were contained in RGl -PCP as free amino groups. When stained with uranyl formate, the ultrastructure of RGl -PW showed a spherical form (onion-like form), whereas the micrographs of RGl -PCP showed a filamentous structure, regardless of strain differences. On the other hand, the micrographs of RGl -PW represented spherical and doughnut-shaped forms, and the micrographs of RGl -PCP showed filamentous or stick forms, when stained with uranyl acetate. Thus, it is suggested that the ultrastructures of RGl were dominated by the solvent systems used for extraction, and not by the strains used here.
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PMID:Chemical and ultrastructural comparison of endotoxins extracted from Salmonella minnesota wild type and R mutants. 620 17

Rough lipopolysaccharide, extracted by a mixture of phenol, chloroform, and petroleum ether from freeze-dried Brucella ovis cells with a yield of 0.71%, contained relatively small amounts of protein and nucleic acid contaminants as compared with lipopolysaccharides from other Brucellae. The crude lipopolysaccharide was suitable as a diagnostic antigen in an enzyme-linked immunosorbent assay for the sensitive and specific detection of ram epididymitis caused by B. ovis infection. In comparative serological tests, the enzyme-linked immunosorbent assay with B. ovis lipopolysaccharide gave better identification of infections and fewer false-negative results than the enzyme-linked immunosorbent assay with sonicated antigen or the complement fixation test.
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PMID:Characterization of Brucella ovis lipopolysaccharide and its use for diagnosis of ram epididymitis by enzyme-linked immunosorbent assay. 639 18

Human lymphocyte proliferation is inhibited in vitro in the presence of killed Pseudomonas aeruginosa or cell-free P. aeruginosa culture supernatants. A comparison of culture supernatants obtained under similar conditions from Staphylococcus aureus, Escherichia coli, P. aeruginosa, and Pseudomonas cepacia strains demonstrated that all P. aeruginosa supernatants were strongly inhibitory, whereas supernatants from other bacteria were mildly inhibitory or not inhibitory at all. These P. aeruginosa inhibitors prevent proliferative responses of resting cells upon mitogen activation and decrease [3H]thymidine uptake when added to human lymphocytes undergoing active proliferation in culture. The inhibitory effect is reversible and not due to cytotoxicity. Most of the inhibitory activity present in crude supernatants was detected in ultrafiltrates of molecular weights below 2,000. Purified P. aeruginosa pyocyanine, a low-molecular-weight phenazine pigment present in culture supernatant, was strongly inhibitory for lymphocyte proliferation. Extraction of pyocyanine and phenazine pigments from inhibitory P. aeruginosa supernatants eliminated their inhibitory activity. Inhibitors were recovered from reverse-phase chromatographic cartridges by both chloroform and methanol elution, indicating that pyocyanine and other phenazine pigments present in P. aeruginosa supernatants are responsible for the inhibition of lymphocyte proliferation. In addition to the identification of phenazine pigments as lymphocyte proliferation inhibitors, several criteria ruled out major contributions of P. aeruginosa polysaccharide, exotoxin A, and proteases to this phenomenon. P. aeruginosa strains selected for very low protease production or for very low exotoxin A production produced supernatants as inhibitory for lymphocyte proliferation as supernatants obtained from clinical P. aeruginosa isolates. Purified P. aeruginosa lipopolysaccharide and protease preparations failed to induce reversible lymphocyte proliferation inhibition. Finally, heat inactivation of P. aeruginosa supernatants at 100 degrees C for 60 min inactivates exotoxin A and proteases but produced only a moderate decrease of the inhibitory activity for lymphocyte proliferation.
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PMID:In vitro inhibition of lymphocyte proliferation by Pseudomonas aeruginosa phenazine pigments. 640 2

The lambda receptor protein (LamB) was assembled into an ordered hexagonal lattice structure with a lattice constant of about 7.8 nm in the presence of lipopolysaccharide. Both the heptose-containing polysaccharide region and the fatty acid region are suggested to be involved in the interaction with LamB. The lattice structure was preferably formed on the peptidoglycan layer when the lipoprotein was covalently bound to this layer. In the presence of chloroform, the ordered hexagonal lattice structure was active in the receptor function for lambda, resulting in phage adsorption and DNA ejection.
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PMID:Arrangement of bacteriophage lambda receptor protein (LamB) in the Escherichia coli cell surface. 646 86

The antigenic material removed form Campylobacter jejuni by the boiling of whole cells in saline was examined biochemically. Analyses showed that the extracted material contained 3 micrograms of protein per ml per mg of wet cells and ca. 2.6 micrograms of carbohydrate per ml per mg of wet cells. Further extraction of the material with chloroform-methanol produced about 0.5 microgram of water-insoluble residue per ml per mg of wet cells, suggesting the presence of lipid as well. Additional analyses revealed the presence of hexose, pentose, heptose, hexosamine, and 2-keto-3-deoxyoctonic acid, and the extract was also positive by the Limulus amoebocyte lysate assay for lipopolysaccharide. An examination by sodium dodecyl sulfate-polyacrylamide gel electrophoresis showed that at least 10 different protein bands could be detected. One of the major bands corresponded to the major outer membrane protein, as determined by comparison with an outer membrane protein preparation by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Another major protein in the heated extract corresponded to a band previously shown to be flagellin. An analysis of the time course of the release of material showed that a significant amount was removed after 3 to 10 min at 100 degrees C, but the release of material seemed to be delayed at lower temperatures. These results show that the treatment of C. jejuni with heat produces a complex mixture of components, including cell wall lipopolysaccharide, the major outer membrane protein, and flagellin. It is likely that some cytoplasmic components are present as well. Blebs of outer membrane have been observed with this organism by electron microscopy. Our results confirm this and suggest that the heating of cells accelerates this blebbing process.
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PMID:Composition of the antigenic material removed from Campylobacter jejuni by heat. 652 Feb 19

Chemical analysis of the lipopolysaccharide from Rhodopseudomonas sphaeroides ATCC 17023, isolated by the phenol-chloroform-petroleum ether method, revealed the presence of glucuronic acid, 2-keto-3-deoxyoctonate, threonine, and phosphorus in the polysaccharide moiety. The lipid A component contained glucosamine, glucosamine phosphate, amide-bound 3-oxotetradecanoic acid and 3-hydroxytetradecanoic acid, and ester-bound 3-hydroxydecanoic acid and 7-tetradecenoic acid. Structural similarity of the lipid A from R. sphaeroides ATCC 17023 to enterobacterial lipid A is indicated by the existence of a serological cross-reaction occurring between the lipid A from R. sphaeroides ATCC 17023 and that from Salmonella minnesota R595. The lipopolysaccharide and lipid A of R. sphaeroides, however, were found to be neither toxic in mice nor pyrogenic in rabbits.
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PMID:Nontoxic lipopolysaccharide from Rhodopseudomonas sphaeroides ATCC 17023. 660 1


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