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

Polyacrylamide gel electrophoresis of unfractionated lysates of radioactively labeled cells resolves not only proteins and polynucleotides into discrete bands but also cellular lipopolysaccharides and phospholipids. This allows a determination of the intracellular amounts of all of these macromolecules. In addition, this technique is sensitive enough to detect mutational alterations in lipopolysaccharide structure. Polyacrylamide gel electrophoresis is herein shown to be a useful tool for investigations into the structure of lipopolysaccharides and the synthesis of lipopolysaccharides and phospholipids.
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PMID:Identification of lipopolysaccharides and phospholipids of Escherichia coli in polyacrylamide gels. 32 66

Inhibition of Proteus mirabilis growth by cerulenin, a specific inhibitor of fatty acid biosynthesis, was reversed by exogenously supplied fatty acid mixtures containing oleic acid and palmitic or pentadecanoic acids. The growth rate of the cells treated with cerulenin in the presence of the fatty acid mixtures was slower, however, than that of untreated cells, and their lipopolysaccharide content was decreased by 30-50%, resulting in an increased sensitivity of the organisms to rifamycin and vancomycin. Polyacrylamide gel electrophoresis of the lipopolysaccharide fraction from cerulenin-treated cells revealed that of the two P. mirabilis lipopolysaccharide types, the relative amount of the higher molecular weight lipopolysaccharide was reduced from 50% to 30% of the total lipopolysaccharide. Fatty acid analysis of the phospholipid and lipopolysaccharide fractions from cells grown with cerulenin, pentadecanoate, and oleate revealed that over 60% of the native even-numbered fatty acids of the phospholipid fraction was substituted by the odd-numbered fatty acid, while no incorporation of either the pentadecanoate or oleate could be demonstrated in the lipid A moiety of the lipopolysaccharide. The only change in the lipid A observed was an increase in the content of 3-hydroxymyristic acid accompanied by a decrease in the nonhydroxylated fatty acids, supporting the highly conserved nature of this molecule.
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PMID:Cerulenin-induced changes in the lipopolysaccharide content and phospholipid composition of Proteus mirabilis. 34 72

From Escherichia coli 0124 two lipopolysaccharide preparations were obtained with phenol/water extraction and cetavlon precipitation. Polyacrylamide gel electrophoresis in the presence of sodium dodecylsulfate and chemical analysis showed that the two preparations from E. coli 0124 and the corresponding preparations from Shigella dysenteriae type 3 reacted alike. The O-specific polysaccharide moiety was characterized with proton magnetic resonance spectroscopy, optical rotation and paper electrophoresis. The constituents were determined by gas chromatography and ion-exchange chromatography. The polysaccharide contained glucose (Glc), galactose (Gal), galactosamine (GalN) and 4-O-(1'-carboxyethyl)-D-glucopyranose (glucolactilic acid, GlcLA) in the molar ratios of 1:2:1:1. Glucolactilic acid, which has a structure similar to muramic acid, was first found in Sh. dysenteriae. The polysaccharide from E. coli 0124 and oligosaccharides obtained from it by partial acid hydrolysis were subjected to methylation analysis using the method of combined gas chromatography--mass spectrometry. The results indicated that the pentasaccharide repeating unit of the polysaccharide is (see article). In the polysaccharide the repeating units are joined through galactofuranosidic linkages. This structure is identical with that of the somatic polysaccharide of Sh. dysenterae type 3.
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PMID:Cell-wall lipopolysaccharide of the 'Shigella-like' Escherichia coli 0124. Structure of the polysaccharide chain. 81 66

We have found whole human platelets, granulocytes, and mononuclear leukocytes to possess high affinity for the toxic lipopolysaccharide from all gram-negative bacteria tested. We have extracted these cells and platelets with n-butanol-water; all endotoxin-binding activity resided in the organic phase. These endotoxin-binding extracts did not block serologically active groupings on endotoxins or receptors on the erythrocytes. The specificity of these still crude materials was less that that of the highly purified erythrocyte lipopolysaccharide receptor previously described by us, since they bound some bacterial antigens not related to endotoxins. Depending on source, the n-butanol extracts contained 40 to 52% glycerophosphatides (most active), 15 to 22% sphingomyelin, 17% cholesterol, less than 2 to 5% triglycerides, and 7 to 13% inactive peptide. The most active substances in the n-butanol extract were soluble in petroleum ether, whereas the peptide and sphingomyelin were not. Thus, no constituent protein, carbohydrate, or nucleic acid was present in the most highly active material. Polyacrylamide gel electrophoresis of the petroleum ether-soluble material showed for each extract one lipid band only, which was well defined and migrated similarly to phosphatidyllipids. Because of the lipidic nature of the inhibitory substances from leukocytes and platelets we also tested the lipid A component of bacterial endotoxins and some of its derivatives. Lipid A inhibited endotoxin coating of erythrocytes. De-O-acylation of lipid A left amide-linked 3-D-hydroxymyristic acid intact and increased the inhibitory activity of lipid A 20-fold. Complete de-O- and de-N-acylation destroyed its inhibitory effect.
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PMID:Endotoxin-binding substances from human leukocytes and platelets. 119 35

Keratinocytes produce multiple cytokines in response to a variety of stimuli. The release of interleukin 1 (IL-1) from keratinocytes may be significant in initiation of cutaneous inflammation, and the presence of granulocyte/macrophage colony-stimulating factor (GM-CSF) is thought to be important in the regulation of antigen-presenting function by epidermal Langerhans cells. Because cyclosporin inhibits interleukin 2 release from T cells, it has been suggested that cyclosporin may function as an anti-inflammatory agent within the epidermis through inhibition of keratinocyte cytokine release. This investigation examined the direct effect of cyclosporin on the production of GM-CSF by murine keratinocytes and the keratinocyte cell line PAM 212. GM-CSF bioactivity increased in cell supernatants from keratinocytes exposed in vitro to 1 microgram/ml cyclosporin for up to 24 h. GM-CSF and IL-1 mRNA levels in keratinocytes cultured under similar conditions or in the presence of lipopolysaccharide also increased. The lack of inhibition of GM-CSF expression following cyclosporin treatment is consistent with recent observations in T cells and is opposite to the effect of cyclosporin on interleukin 2.
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PMID:Cyclosporin increases granulocyte/macrophage colony-stimulating factor (GM-CSF) activity and gene expression in murine keratinocytes. 154 36

An IgG3 murine monoclonal antibody (designated MO8) specific for the serogroup C2 Salmonella lipopolysaccharide (LPS) was generated by fusing mouse myeloma cells NS1 with spleen cells of BALB/c mice immunised with heat-killed S. manhattan. MO8 reacted with purified LPS prepared from serogroup C2 Salmonella but did not react with that prepared from other O serogroups, and its reactivity was also specifically absorbed by serogroup C2 Salmonella only. Polyacrylamide gel electrophoresis of the serogroup C2 LPS and subsequent immunoblotting with MO8 yielded multiple reactive bands giving a characteristic ladder pattern. The specificity of MO8 was further demonstrated in the slide agglutination test with 223 bacteria, of which only 25 belonging to serogroup C2 Salmonella reacted with the MO8 ascitic fluid. The specificity of MO8 makes it useful not only for the serological identification of Salmonella but also for the epitope analysis of the serogroup C2 LPS.
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PMID:Characterisation and application of a murine monoclonal antibody specific for the serogroup C2 Salmonella. 245 55

Ciprofloxacin accumulation in Pseudomonas aeruginosa was measured by a bioassay. Drug accumulation in strain PAO2 was compared with that of three spontaneous ciprofloxacin-resistant mutants selected with 0.5 micrograms of ciprofloxacin per ml. PAO4701 cfxA2 contains a mutation in the gyrA gene, PAO4742 cfxB5 may represent a permeability mutant based on pleiotropic drug resistance, and PAO4700 cfxA1 cfxB1 contains both types of mutations. In all strains, drug accumulation was similar, reaching steady state during the first minute of exposure. Drug accumulation was unsaturable over a range of 5 to 80 micrograms/ml, suggesting that ciprofloxacin accumulates by diffusion in P. aeruginosa. Although all four strains accumulated two- to sevenfold more ciprofloxacin in the presence of the inhibitor carbonyl cyanide m-chlorophenylhydrazone, the cfxB mutants accumulated two- to fourfold less drug than either PAO2 or the cfxA2 mutant. Polyacrylamide gel analysis revealed a protein common to cfxB mutants only, while all strains had similar lipopolysaccharide profiles. The results suggest that ciprofloxacin accumulation in P. aeruginosa is a complex phenomenon that may be affected by both an energy-dependent drug efflux process and outer envelope composition.
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PMID:Factors influencing the accumulation of ciprofloxacin in Pseudomonas aeruginosa. 251 23

The lipopolysaccharide (LPS) structure of Campylobacter spp. can be visualized with polyacrylamide gel electrophoresis by examining proteinase K-treated whole cell lysates. Polyacrylamide gel electrophoresis LPS profiles of C. jejuni strains are rough type with low concentrations of low-molecular-weight polysaccharide side chains, serum-resistant C. fetus strains have smooth-type LPS, and serum-sensitive C. fetus strains have rough-type LPS. We electroblotted the proteinase K-treated whole cell lysates of 17 C. jejuni and 9 C. fetus strains from polyacrylamide gel electrophoresis to nitrocellulose paper to examine antigenicity to immune rabbit sera. There was virtually no antigenic cross-reactivity of C. jejuni and C. fetus LPS. Among C. jejuni strains, core LPS structures were cross-reactive, but the O-polysaccharide side chains were best recognized by homologous antisera. Antisera to several serum-resistant C. fetus strains recognized only the polysaccharide side-chain regions of serum-resistant strains and no part of the LPS from the sensitive strain. Antiserum raised against a serum-sensitive C. fetus strain but not homologous antisera recognized the core region of the LPS of the serum-resistant C. fetus strains. These findings suggest that core LPS antigens are widely shared within C. fetus subsp. fetus strains but that in the serum-resistant strains this core region is not surface exposed and therefore not immunogenic to rabbits infected with whole cells.
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PMID:Antigenic heterogeneity of lipopolysaccharides from Campylobacter jejuni and Campylobacter fetus. 258 Jul 93

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

Outer membranes (OMs) of Salmonella enteritidis, S. anatum, S. typhimurium, and S. infantis were extracted and cross-linked with glutaraldehyde to form a large macromolecular antigen. The antigen consisted of OM proteins and lipopolysaccharide and was designated 4-OMP-LPS. Polyacrylamide gel electrophoresis of extracted OMs from each serotype revealed differences in protein profiles. S. enteritidis and S. infantis possessed a greater variety of proteins than did S. anatum and S. typhimurium. Immunizations with 4-OMP-LPS in phosphate-buffered saline (4-OMP-LPS-C) and 4-OMP-LPS emulsified with muramyl dipeptide in the oil phase of a hexadecane-water emulsion (4-OMP-LPS-MDP) revealed that BALB/c mice were capable of eliciting specific primary and secondary immunoglobulin M (IgM) and IgG responses. Both antigen preparations were capable of eliciting IgM and IgG specific for the cell surfaces of each live Salmonella serotype. Also, 4-OMP-LPS-MDP and 4-OMP-LPS-C were capable of evoking a substantial anamnestic response. Adsorption studies revealed that the combined serotypes had the antigenic capacity to adsorb up to 94% of the antibodies, but 4-OMP-LPS-MDP antibodies were more effectively adsorbed than were 4-OMP-LPS-C antibodies. Adsorption of pooled antiserum with heterologous bacteria yielded a variety of adsorption profiles.
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PMID:Immunoglobulin M and immunoglobulin G responses in BALB/c mice to conjugated outer membrane extracts of four Salmonella serotypes. 403 94


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