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

Killed Coxiella burnetii (C.b.) cells in phase II but not in phase I had a mild stimulatory effect on hexose monophosphate shunt (HMPS) and superoxide anion production by human polymorphonuclear (PMN) leukocytes. Preincubation of C.b. cells of either phase with serum of a leukocyte donor lacking detectable antibodies to C.b. did not affect the studied activities of PMN leukocytes. In contrast, both HMPS stimulation and superoxide production were enhanced by specific opsonization of C.b. cells with rabbit immune sera containing corresponding phase I and/or phase II antibodies. Stimulatory effect was observed also with lipopolysaccharide-protein-phospholipid (LPS-Pr-Pl) complex but not with lipopolysaccharide-protein (LPS-Pr) complex and with purified lipopolysaccharide (LPS) isolated from phase I C.b. cells. Possible consequences of these findings for explanation of C.b. resistance to intracellular killing by professional phagocytes are discussed.
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PMID:Effect of Coxiella burnetii on the stimulation of hexose monophosphate shunt and on superoxide anion production in human polymorphonuclear leukocytes. 614 2

Several saccharides representative of the O-antigenic polysaccharide chain of Salmonella typhimurium (O antigens 4 and 12) were used as haptenic groups covalently linked to bovine serum albumin. The disaccharide abequose 1 --> 3 D-mannose was synthesized, and the [Formula: see text] tetra-, octa- and dodecasaccharides were isolated after cleavage of isolated S. typhimurium O-polysaccharide chains by using bacteriophage endo-glycosidases. Rabbits immunized with the saccharide-protein conjugates suspended in Freund complete adjuvant readily responded with O4 antibody titers as high, or almost as high, as those elicited by heat-killed bacteria. The octa- and dodecasaccharide conjugates also gave rise to O12 antibody titers. The antibody response in mice differed in two ways from that seen in rabbits: mice did not respond with measurable antibody production against the disaccharide haptens, and the highest S. typhimurium lipopolysaccharide antibody response elicited by the saccharide haptens was still approximately 50-fold lower than that elicited by heat-killed bacteria. The latter difference may be a consequence of the fact that the mouse preferentially produces antibodies against the galactose residue which is terminal in the hapten but not in the native O-antigenic polysaccharide chain. Antibodies elicited in rabbits against all saccharide-protein conjugates protected passively transferred mice against intraperitoneal challenge with 100 times the 50% lethal dose of S. typhimurium SH 2201 (O4, 12) but not against challenge with S. enteritidis SH 2204 (O9, 12). The antibodies elicited by the saccharide-protein conjugates protected as well as antibodies elicited by heat-killed bacteria.
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PMID:Artificial Salmonella vaccines: Salmonella typhimurium O-antigen-specific oligosaccharide-protein conjugates elicit protective antibodies in rabbits and mice. 616 55

Pseudomonas aeruginosa lectins interact with Escherichia coli strains O86B7 and O128B12, which possess B and H (O) blood group determinants, respectively. The interaction could be demonstrated by specific agglutination of the bacteria, by haemagglutination inhibition tests and by lectin-mediated peroxidase binding to the bacteria. The agglutination of E. coli O86B7 by the Pseudomonas galactose-binding lectin was inhibited by D-galactose and by the lipopolysaccharide extracted from E. coli O86B7. Similarly, the specific agglutination of E. coli O128B12 by the Pseudomonas mannose-binding lectin (which also binds L-fucose, L-galactose and D-fructose) was inhibited by D-mannose, L-fucose, L-galactose and D-fructose, as well as by athe lipopolysaccharide extracted from E. coli O128B12. The interaction between E. coli O128B12 and the Pseudomonas mannose-binding lectin was also demonstrated by lectin-mediated peroxidase binding to the bacterial surface. Peroxidase binding was also inhibited by the above-mentioned sugars and E. coli O128B12 lipopolysaccharide. Treatment of cells of the two E. coli strains with protein-denaturing agents did not reduce their agglutination by the Pseudomonas lectins. On the other hand, oxidation of the cell surface sugars by sodium metaperiodate or boiling the cells in the presence of 1% acetic acid for 1 h abolished their agglutination by the two lectins. It is, therefore, suggested that the Pseudomonas lectins interact with the B and H (O) blood group determinant sugars (D-galactose in E. coli O86B7 and L-fucose in E. coli O128B12) residing in the lipopolysaccharides of these E. coli strains.
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PMID:Interactions of Pseudomonas aeruginosa lectins with Escherichia coli strains bearing blood group determinants. 617 47

A simple polysaccharide, the neutral mannan from Saccharomyces cerevisiae wild type strain (WNM) was found to kill ddY strain mice by intravenous administration, showing a LD50 value of 12.2 mg/kg. On the other hand, the acidic mannan fraction from the same yeast containing phosphate (WAM025), and chemically phosphorylated WNM (WNM-P) were practically non-toxic. Concerning the relationship between chemical structure and lethal effect of these mannans, it was demonstrated that a mannan possessing a highly branched structure exhibited stronger lethality than those with less branched structures. Against C3H/HeJ strain mice with no responsiveness to lipopolysaccharide, the LD50 value of WNM was as high as 75 mg/kg. Pretreatment with 500 mg/kg of D-mannose, N-acetyl-D-glucosamine, D-galactose, and L-fucose prevented mice from the lethal effects of WNM. However, WNM (LD100) did not show any lethal effect in mice for 2 to 12 hr after treatment with dexamethasone, an anti-inflammatory steroid.
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PMID:Lethal effect of neutral mannan fraction of bakers' yeast in mice. 639 33

Pseudomonas aeruginosa PAO grown in glucose mineral salts medium released lipopolysaccharide which was chemically and immunologically similar to the cellular lipopolysaccharide. In addition, it possessed identical phage E79-inactivating properties. Through neutralization of phage activity and hemolysis inhibition assays, the organism was found to liberate lipopolysaccharide at a constant rate during log-phase growth equivalent to 1.3 to 2.2 ng/10(8) cells over a growth temperature range of 25 to 42 degrees C. At 19 degrees C, a lipopolysaccharide was released which was deficient in phage-inactivating activity but retained its immunological properties. Chemical analysis of lipopolysaccharide extracted from cells grown at 19 degrees C showed a deficiency in the O-side-chain component fucosamine. Gel exclusion chromatography of the polysaccharide fraction derived from lipopolysaccharide isolated from cells grown at 19 degrees C exhibited a decreased content of side-chain polysaccharide as well as a difference in the hexosamine:hexose ratio. The results of sodium dodecyl sulfate-polyacrylamide gel electrophoretic analysis confirmed these results as well as establishing that an essentially normal distribution of side-chain repeating unit lengths were to be found in the 19 degrees C preparation. These results suggest a decrease in the frequency of capping R-form lipopolysaccharide at 19 degrees C.
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PMID:Spontaneous release of lipopolysaccharide by Pseudomonas aeruginosa. 640 83

Receptor for phage PIK specific for Pseudomonas aeruginosa strain PAO1 was studied. Phage PIK was strongly inactivated by lipopolysaccharide (LPS) in vitro, exhibiting a PhI50 of 4.8 micrograms/ml. Further it was noted that this inactivation by LPS was reduced to 50% by several mono- and disaccharides when tested in vitro. D-glucosamine, D-mannose and L-rhamnose were found to be most effective at the concentration of 0.045 M, 0.25 M and 0.35 M respectively. This suggests the possibility that phage PIK receptor in LPS contains D-mannose, L-rhamnose and D-glucosamine. Either one of the former two could be located at a terminal position alpha-linked to the adjacent residue or located internally in the polysaccharide chain linked through its C-4 position. A theoretical approach to the interpretation of phage cell interaction was also investigated.
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PMID:Studies on the Pseudomonas aeruginosa PAO1 bacteriophage receptors. 641 17

A purified fraction of the extracellular slime of Pseudomonas aeruginosa, characterized chemically as a glycolipoprotein (GLP), has been identified as responsible for a number of biologic properties of the viable cell. Mice immunized actively or passively against GLP are protected against an otherwise lethal challenge with viable bacteria. GLP is chemically, physically, and antigenically distinct from the lipopolysaccharide of the same strain. An in vivo association of GLP with blood leukocytes has been demonstrated, and the leukopenia in mice following challenge with P. aeruginosa may be accounted for by the subsequent sequestration of a neutrophil-GLP complex in the liver. Anti-GLP serum in the absence of complement mediates the phagocytosis and eventual killing of viable P. aeruginosa by mouse polymorphonuclear leukocytes and unstimulated peritoneal macrophages. A polysaccharide fraction isolated from the GLP is responsible for its protective immunogenicity. Although the lipid moiety governs the leukopenic and lethal capacities, the carbohydrate, specifically the mannose of this moiety, is required for full expression of GLP lethality. Mannose is also an immunodominant sugar.
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PMID:Determinants of the biologic activity of surface slime in experimental Pseudomonas aeruginosa infections. 641 19

Lectin-like molecules on the surface of murine peritoneal exudate macrophages induced by thioglycolate or an anti-tumor streptococcal preparation, OK-432, were investigated and isolated. Furthermore, their sugar-binding specificities and their role in macrophage-mediated tumor cytotoxicity were examined. A neoglycoprotein, D-galactose (Gal)-bovine serum albumin, bound to these murine peritoneal macrophages. This binding of Gal-bovine serum albumin was inhibited by D-galactose, and by complex-type oligosaccharides (unit B) and high mannose-type oligosaccharides (unit A) prepared from porcine thyroglobulin. When thioglycolate-elicited macrophages were activated by lipopolysaccharide and/or the culture supernatant of concanavalin A-activated mouse spleen cells, they became tumoricidal and the number of the lectin-like molecules on the macrophage surface was found to increase. Since the binding and cytotoxic activities of these tumoricidal macrophages toward tumor cells were partially inhibited by D-galactose, the D-galactose-binding lectin-like molecules on the surface of tumoricidal macrophages might play an important role in macrophage-mediated cytotoxicity. These lectin-like molecules were then isolated from solubilized murine peritoneal exudate cells labeled with pyridoxal 5'-phosphate and sodium [3H]borohydride by affinity chromatography on columns of asialo unit B oligosaccharide-Sepharose 4B and/or beta-D-galactose-Bio-Gel P-100. The proteins bound to the asialo unit B oligosaccharide-Sepharose 4B column and eluted specifically were found to have approximate molecular weights of 79 000 and 18 000, and the protein bound to and eluted from the beta-D-galactose-Bio-Gel P-100 column had an approximate molecular weight of 77 000. These isolated proteins bound to the surface of glutaraldehyde-fixed tumor cells, and their binding was inhibited by D-galactose and also by D-mannose. Since most of the 77 kDa protein bound to the asialo unit B oligosaccharide-Sepharose 4B, this protein was assumed to be identical with the 79 kDa protein. These results suggest that the lectin-like molecules on murine macrophages have wide specificity and that one lectin-like molecule can bind both D-galactose and D-mannose.
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PMID:Lectin-like molecules on the murine macrophage cell surface. 648 61

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

Peritoneal macrophages from young (3-8 mo) and aging (12-29 mo) mice of the C58, BALB/c, C3H/He, C57BI/6J, and B6D2F1 stains were compared for their capacity to become activated by various adjuvants in four assays. In chemiluminescence, activation by phorbol myristic acetate or zymosan of macrophages from aging mice of the C58, BALB/c, and C3H/He strains was increased approximately twofold greater than that of cells from young mice. A reversal of this was seen in the same three strains when measuring activation of phagocytosis by lipopolysaccharide, polyadenylate:polyuridylate (polyA:poly U), or muramyl dipeptide in that increased activity was induced readily in macrophages from young but not aging mice. Similarly, tumoricidal activity of macrophages from young but not aging mice was stimulated 6.0- and 4.4-fold by lipopolysaccharide and poly A:poly U, respectively, in the C58 strain (the only strain studied). Activation by lipopolysaccharide and poly A:poly U of the hexose monophosphate shunt in macrophages from the C58 and C3H/He strains also was significant in young but not aging mice, whereas it occurred in both age groups of the BALB/c and C57B1/6J mice. A reversal of response patterns was observed between aging female virgin and breeder C58 mice in the chemiluminescence and hexose monophosphate shunt assays in that the breeding mice mimicked the young virgin mice.
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PMID:Macrophage activation by adjuvants in aging mice. 658 21


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