Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P43026 (lipopolysaccharide)
 62,215 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Murine peritoneal macrophages elicited by dimethyldioctadecylammonium bromide (DDA), which is a potent immunologic adjuvant, were examined for cytotoxic and growth inhibiting activity for malignant cells. DDA macrophages had no cytolytic activity for murine B16BL-6 melanoma or human SMS-SB pre-B leukemia cells even in the presence of up to 1 microgram bacterial endotoxin (lipopolysaccharide, LPS)/ml. However, they exhibited a variable inhibitory effect on the growth of several lines of leukemia cells. The number of SMS-SB and human NALL cells remained essentially static in the presence of DDA macrophages while they increased significantly when cultured with resident macrophages. In contrast, L1210 cells increased 5-8-fold in the presence of macrophages elicited either by DDA or the inflammatory agent proteose peptone (PP). Although DDA macrophages retarded L1210 growth relative to PP macrophages, both populations responded to LPS in a comparable dose dependent manner to become essentially cytostatic at 1 microgram LPS/ml.
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PMID:Effect of dimethyldioctadecylammonium bromide induced macrophages on malignant cell proliferation. 400 32

Previous studies have shown that the outer membrane of Escherichia coli O111 gives a single, major, 42,000-dalton protein peak when analyzed by sodium dodecyl sulfate (SDS)-polyacrylamide gel electrophoresis at neutral pH. Further studies have shown that this peak consists of more than a single polypeptide species, and on alkaline SDS-gel electrophoresis this single peak is resolved into three subcomponents designated as proteins 1, 2, and 3. By chromatography of solubilized, outer membrane protein on diethylaminoethyl-cellulose followed by chromatography on Sephadex G-200 in the presence of SDS, it was possible to separate the 42,000-dalton major protein into four distinct protein fractions. Comparison of cyanogen bromide peptides derived from these fractions indicated that they represented at least four distinct polypeptide species. Two of these proteins migrated as proteins 1 and 2 on alkaline gels. The other two proteins migrated as protein 3 on alkaline gels and cannot be separated by SDS-polyacrylamide gel electrophoresis. In purified form, these major proteins do not contain bound lipopolysaccharide, phospholipid, or phosphate. These proteins may contain a small amount of carbohydrate, as evidenced by the labeling of these proteins by glucosamine, and to a lesser extent by glucose, under conditions where the metabolism of these sugars to amino acids and lipids is blocked. All of the proteins were labeled to the same extent by these sugars. Thus, it was concluded that there are at least four distinct polypeptide species with apparent molecular masses of about 42,000 daltons in the outer membrane of E. coli O111.
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PMID:Outer membrane proteins of Escherichia coli. 3. Evidence that the major protein of Escherichia coli O111 outer membrane consists of four distinct polypeptide species. 420 34

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

Ribosomal ribonucleic acid (RNA) and lipopolysaccharide (LPS) from P. aeruginosa were compared with respect to their protective activities in mice against an infection with P. aeruginosa. This study is concentrated on the protective activity of RNA. RNA isolated from purified ribosomes did not contain LPS as determined with the Limulus test. Injection of RNA with the adjuvant dimethyldioctadecylammonium bromide (DDA) protected mice against P. aeruginosa without inducing LPS-specific antibodies. C3H/HeJ mice which are relatively insensitive to the protective activity of LPS could be protected with RNA. The protective activities of RNA and LPS from a mutant strain of P. aeruginosa, PAC 605, containing defective lipopolysaccharide, were compared with the protective activities of RNA and LPS from the parent strain, PAC IR. The protective activity of LPS from PAC 605 was 1000 fold lower than the protective activity of LPS from PAC IR. RNA preparations of both strains induced similar percentages of survival. The protective activity of ribosomal RNA from P. aeruginosa was nonspecific since mice were also protected against a heterologous serotype of P. aeruginosa and against Escherichia coli. RNA from ribosomes of P. aeruginosa, E. coli and the non-lipopolysaccharide containing Saccharomyces cerevisiae had similar protective activities. No protection was obtained with the ribonucleic acid from the E. coli phage MS2. It is concluded that ribosomal RNA has protective activities distinct from those of LPS.
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PMID:Protective activities of ribosomal ribonucleic acid and lipopolysaccharide of Pseudomonas aeruginosa: a comparative study. 619 55

The electron spin resonance probes 5-doxylstearate and 4-(dodecyldimethylammonio)-1-oxy-2,2,6,6-tetramethylpiperidine bromide were used to characterize the fluidity of the acyl chain and head-group regions, respectively, of defined salts of lipopolysaccharide (LPS) from Escherichia coli K12. The removal of the weakly bound divalent cations from native LPS by electrodialysis and their replacement by sodium had little effect on the midpoint of the lipid-phase transition or on head-group mobility. In contrast, lipopolysaccharide acyl chain mobility increased following electrodialysis. The replacement of most of the remaining cations with sodium resulted in a further dramatic increase in mobility in both the polar and nonpolar regions of lipopolysaccharide. Head-group mobility of the sodium salt of LPS was shown to be reduced with the addition of divalent cations. Furthermore, evidence is presented which suggests that low magnesium concentrations may induce phase separations in the sodium salt. The magnesium salt of lipopolysaccharide closely resembled the native form in both head-group and acyl chain mobility although the cation charge to phosphorus ratio in the magnesium salt was greater than that detected in the native isolate. Analyses of other lipopolysaccharide salts support our hypothesis that many of the observed differences in the physical and pathological properties of lipopolysaccharide salts may simply be explained by the degree of charge neutralization.
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PMID:Physical properties of defined lipopolysaccharide salts. 630

The synthesis of the trisaccharide O-beta-L-rhamnopyranosyl-(1 leads to 4)-O-beta-L-rhamnopyranosyl-(1 leads to 2)-L-rhamnopyranose (14) and the tetrasaccharide O-2-acetamido-2-deoxy-beta-D-galactopyranosyl)-(1 leads to 2)-O-[beta-L-rhamnopyranosyl-(1 leads to 4)]-O-beta-L-rhamnopyranosyl-(1 leads to 2)-L-rhamnopyranose (21) is described. The latter structure has been proposed as the repeating unit of the O-specific side-chain of the lipopolysaccharide obtained from Shigella flexneri Serotype 6. The key-intermediate was 4-O-acetyl-2-O-allyl-3-O-benzyl-alpha-D-rhamnopyranosyl bromide, which was first linked to benzyl 3,4-di-O-benzyl-alpha-L-rhamnopyranoside, to give a blocked beta-linked disaccharide. This was O-deacetylated and coupled with 2,3,4-tri-O-benzyl-alpha-L-rhamnopyranosyl bromide at O-4' to afford benzyl O-(2,3,4-tri-O-benzyl-beta-L-rhamnopyranosyl)-(1 leads to 4)-O-(2-O-allyl-3-O-benzyl-beta-L-rhamnopyranosyl)-(1 leads to 2)-3,4-di-O-benzyl-alpha-L-rhamnopyranoside (11), which was deprotected to give 14. Deallylation of 11 and coupling with 6-O-acetyl-2-azido-3,4-di-O-benzyl-2-deoxy-alpha-D-galactopyranosyl bromide led to a protected tetrasaccharide from which 21 was obtained. The method of catalysis by silver silicate was employed to obtain the beta-glycosidic linkage of all monosaccharide units.
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PMID:[Synthesis of beta-L-rhamnoside linked oligosaccharides of lipopolysaccharides from Shigella flexneri serotype 6]. 635 43

Alkali-treated lipopolysaccharide from Brucella abortus S1119.3 coupled to agarose beads by cyanogen bromide activation resulted in an immunoadsorbent with which a large amount of B. abortus-specific antibodies could be purified. The method described gave alkali-treated lipopolysaccharide binding efficiencies of up to 98%. There was little loss of alkali-treated lipopolysaccharide from the column after several pH shifts, allowing the immunoadsorbent to be regenerated and used repeatedly.
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PMID:Affinity purification of bovine antibodies to Brucella abortus Lipopolysaccharide. 640 76

Hydrolysis of the chromogenic beta-lactam nitrocefin by periplasmic beta-lactamase in intact Pseudomonas aeruginosa cells was used to assess the influence of various compounds on the permeability of the P. aeruginosa outer membrane. In addition to the five previously described outer membrane-active compounds EDTA, polymyxin B, gentamicin, poly-L-lysine, and Tris, seven other compounds were shown to increase outer membrane permeability to nitrocefin by 14- to 63-fold. These other compounds included poly-L-ornithine, neomycin, cetyltrimethylammonium bromide, nitrilotriacetate, L-ascorbate, and acetylsalicylate. In each case, Mg2+ ions antagonized, to different extents, the enhancement of outer membrane permeability. The same compounds increased the permeability of the outer membrane to the protein lysozyme and to the hydrophobic fluorescent probe 1-N-phenylnaphthylamine, although L-ascorbate and acetylsalicylate showed only very weak enhancement of uptake in these assays. In this report, we discuss the possibility that these compounds act at a common outer membrane site at which divalent cations noncovalently cross-bridge adjacent lipopolysaccharide molecules.
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PMID:Compounds which increase the permeability of the Pseudomonas aeruginosa outer membrane. 643 88

Mycobacterial polymethyl polysaccharides, which bind long-chain fatty acids tightly [Ballou, C.E. (1981) Pure Appl. Chem. 53, 107-112], have been purified on a preparative scale by use of an affinity column packing consisting of (palmitoylamino)alkylsilyl silicate. The relatively large amount of material obtained in this way has allowed a study of the polysaccharide-lipid interactions at millimolar concentrations. The anomeric protons for all of the alpha 1----4-linked hexose units in the mycobacterial methylglucose polysaccharide occur in an envelope centered at delta 5.40, and, on titration with hexadecyltrimethylammonium bromide, the majority of these resonances move upfield to about delta 5.15. This shift is consistent with a change in the polysaccharide from a less ordered chain to one that has a significant proportion of helical conformation, and it is probable that the alkyl chain is included in the coiled portion of the polysaccharide in a manner analogous to the interaction of methylmannose polysaccharide with palmitic acid [Yabusaki, K. K., Cohen, R. E., & Ballou, C. E. (1979) J. Biol. Chem. 254, 7282-7286]. The native methylglucose lipopolysaccharide, which contains several short-chain acyl groups as well as an esterified octanoyl group, has an anomeric proton nuclear magnetic resonance spectrum similar to that of the methylglucose polysaccharide-hexadecyltrimethylammonium bromide complex. This suggests that the acylation stabilizes the polysaccharide chain in the same conformation it assumes when complexed to a long-chain lipid. Thus, acylation of the methylglucose polysaccharide could have an important role in regulating its shape and lipid-binding properties.
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PMID:Affinity purification of mycobacterial polymethyl polysaccharides and a study of polysaccharide-lipid interactions by 1H NMR. 670 84

Potent, mono-specific anti-Pseudomonas immunoglobulins were isolated from serum and lung lavage fluid from patients with cystic fibrosis using immunotype specific Pseudomonas aeruginosa lipopolysaccharide (LPS) substituted immunoadsorbent gel. Iodinated monovalent Pseudomonas LPS somatic antigens, Fisher immunotypes, were used as ligands for two different insoluble gel matrices. LPS iodination, using the water insoluble chloroglycoluril reagent, permitted quantitation of the percent LPS bound as a ligand. The coupling efficiencies of epoxy-activated and cyanogen bromide-activated Sepharose matrices for various Pseudomonas immunotype specific LPS preparations were compared. Although each of the 7 LPS somatic antigens produced an equivalent amount of coupling, higher percentages of coupling were found using the cyanogen bromide-activated gel when compared to the epoxy-activated gel. IgG fractions prepared from cystic fibrosis sera and lung lavage fluid were passed through the LPS affinity gels, and Pseudomonas LPS immunotype specific antibodies were eluted. The presence of specific antibody activity against individual Pseudomonas immunotypes was determined with a passive micro-hemagglutination assay. Bronchial lavage fluid seemed to be as effective as serum as a source of Pseudomonas specific antibody. Use of such a LPS substituted gel permits direct recovery of Pseudomonas monospecific antibodies suitable for physical-chemical analyses and for biologic functional assays.
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PMID:Use of Pseudomonas aeruginosa lipopolysaccharide immunoadsorbents to prepare high potency, mono-specific antibodies. 677 26


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