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)

Phase I cells of Bordetella pertussis but not those of B. parapertussis, B. bronchiseptica or B. avium were agglutinated by Limulus polyphemus lectin. Most strains of B. pertussis but not those of the other species were also agglutinated by Helix pomatia lectin. In precipitation reactions between lectins and purified Bordetella lipopolysaccharide (LPS) preparations a similar pattern occurred. Lectin agglutination provides a rapid presumptive method for the differentiation of B. pertussis from B. parapertussis and other Bordetella species.
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PMID:Agglutination of Bordetella species by lectins. 155 59

The present study was designed to delineate changes in serum lipid levels following various kinds of tissue injury or inflammation such as contact sensitivity to picryl chloride, thermal burn, carrageenin-induced edema, the administration of turpentine oil, Freund's complete adjuvant (FCA), killed Bordetella pertussis (BP) or lipopolysaccharide (LPS). A uniform change in the serum lipid metabolism was observed in mice that received these inflammatory stimuli; that is, increases in total cholesterol, free cholesterol and phospholipid levels, a decrease in the ester ratio and a decline in lecithin: cholesterol acyltransferase activity as well as a decrease in albumin levels, which is an index of the acute-phase response. However, serum triglyceride levels were increased by treatment with the bacterial stimuli (FCA, BP and LPS) but decreased by treatment with the other stimuli. The serum free cholesterol and phospholipid levels were significantly correlated with the intensity of contact sensitivity, which was modified by treatment with cyclophosphamide. Indomethacin or dexamethasone suppressed carrageenin-induced edema and inhibited some of the alterations in lipid metabolism that developed during inflammation because each affected a part of the lipid metabolism. These findings suggest that, like the appearance of acute-phase proteins, the uniform change in serum lipid metabolism may be another sensitive index of the acute inflammatory response.
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PMID:A uniform alteration in serum lipid metabolism occurring during inflammation in mice. 164 Jun 61

Development of antibody titres in non-vaccinated children with whooping cough of different duration (all confirmed by positive culture) were investigated by ELISA using lymphocytosis promoting factor (LPF, pertussis toxin), filamentous haemagglutinin (FHA), 69 kDa protein and lipopolysaccharide (LPS) as antigens. The antibody responses occur in three different patterns: Firstly, the LPF antibody response develops very quickly starting with the first day of clinical cough with all three classes, IgG, IgM and IgA appearing simultaneously; LPF antibody appears to be a dominant feature. Secondly, FHA and 69 kDa antibodies appear, starting as IgM with the shift to IgG and IgA later. The third pattern is represented by LPS antibody, the IgA appearing early, but with IgM predominant. Higher titres of IgG reacting with LPS were observed in vaccinated children. Transplacental transfer of antibody was also studied. All antibody titres determined in maternal blood and cord blood were proportional except for anti-LPS antibody which was retarded. Most IgG antibody was IgG1 subclass; surprisingly the 69 kDa antibody consisted of a mixture of approx. 90% IgG1 and 10% IgG4.
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PMID:Analysis of antibody profiles in children with whooping cough. 177 18

Adjuvant activities of isogenic Salmonella enterica, serovar Typhimurium, O-6,7 and O-4,5,12 lipopolysaccharide (LPS), lipid A and Bordetella pertussis LPS were compared by immunizing groups of mice subcutaneously with diphtheria and tetanus toxoid vaccine alone or mixed with one of the LPS derivatives. Five weeks later the mice were bled and the tetanus and diphtheria antibodies in the sera were measured. All the LPS derivatives efficiently increased the antibody responses when compared to the vaccine alone, but the mannose-rich O-6,7 LPS and lipid A were significantly more potent than O-4,5,12 LPS and B. pertussis LPS. We conclude that the quality of the O antigen influences the adjuvant activity of LPS.
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PMID:The role of the O antigen in adjuvant activity of lipopolysaccharide. 177 21

The molecular mechanisms surrounding the toxicity and high mortality rate that accompany the release of bacterial lipopolysaccharide (LPS) are unclear, although its potent activity suggests that an amplification system is involved. Because previous studies suggest that a guanine-nucleotide-binding protein (G-protein) may participate in LPS action, we have evaluated the effects of LPS on GTPase activity in membranes isolated from macrophage (RAW 264.7) and fibroblast (B82L) cell lines. LPS induced substantial GTPase activation (200-300% above basal), and kinetic analyses indicated that the maximal LPS-stimulated increase in velocity is observed within 15 min, that it is a low-Km (for GTP) activity, that it can be enhanced by ammonium sulphate, and that it appears to be pertussis toxin-insensitive. Moreover, the LPS-enhanced GTPase activity was not antagonized by phosphatase/ATPase inhibitors such as p-nitrophenyl phosphate, ouabain, bafilomycin or N-ethylmaleimide, and in fact was potentiated by the addition of ATP or ADP. Conversely, the LPS precursor, lipid X, which can decrease the lethal effects of LPS, was found to dose-dependently inhibit the LPS-mediated stimulation of GTPase activity. Half-maximal inhibition was seen at the same lipid X/LPS ratio known to be effective in vivo, i.e. 1:1(w/w). These effects appear to be specific because other phospholipids, detergents and glycosides neither stimulated basal, nor inhibited LPS-induced, GTPase activity. These data suggest the involvement of a GTPase in LPS action, and indicate that lipid X may act to directly antagonize LPS at this level.
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PMID:Bacterial lipopolysaccharide-stimulated GTPase activity in RAW 264.7 macrophage membranes. 185 66

Knowledge of rapid events in cell signaling initiated by lipid A, the core moiety of bacterial lipopolysaccharide, is limited. In the present study we have demonstrated that cis-parinaric acid (cis-PnA) rapidly labels 1,2-sn-diacylglycerol (DAG) subsequent to labeling of phosphatidic acid (PA). Stimulation of microsomal membranes with lipid A decreased the level of PA labeled with cis-PnA within 5 s and increased the proportion of fluorescent label in DAG. Lipid A stimulation of DAG synthesis at 5-15 s was inhibited by incubation of mesangial cells with pertussis toxin prior to isolation of microsomal membranes. Inhibition of DAG formation was accompanied by an accumulation of the mass and fluorescent label in the cis-PnA-labeled phosphatidic acid pool. GTP gamma S caused a decrease in labeled PA and an increase in labeled 1,2-DAG. We conclude that the PA pool was enlarged via the lipid A sensitive lyso-PA acyl transferase (lyso-PA-AT) and was decreased by a phosphatidate phosphohydrolase to form DAG. The phosphatidate phosphohydrolase was at least partly regulated by a pertussis-sensitive G-protein. Lipid A or 1,2-dilinoleyl-PA, a product of lyso-PA-AT, induced cell activation as monitored by actin reorganization and cellular shape changes. Pretreatment of cells with pertussis toxin prevented the morphological changes normally induced by lipid A or 1,2-dilinoleyl-PA. In contrast, 1-oleoyl-2-acetylglycerol induced rapid actin reorganization and shape change, presumably bypassing the pertussis blockade. We propose that specific pools of PA and PA-derived DAG are key elements in rapid signaling in mesangial cells and are independent of the PI cycle and phospholipase C.
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PMID:Rapid activation of phosphatidate phosphohydrolase in mesangial cells by lipid A. 190 69

Pertussis toxin (PT) subunit S1 was produced in Bacillus subtilis as a secretory protein designated BacS1. BacS1 was partially purified and used to immunize mice. The sera were tested for PT-neutralizing antibodies and for protective capacity in a mouse model. Unlike previous findings with recombinant S1 from Escherichia coli, the recombinant BacS1 protein induced antibodies that were both neutralizing and protective. An adjuvant was necessary for efficient immunization with BacS1 but not with PT. Of the four adjuvants tested, aluminium phosphate gel was insufficient whereas Freund's incomplete adjuvant, Klebsiella lipopolysaccharide and Ribi's monophosphoryl lipid A-trehalose dimycolate emulsion all resulted in protective antibody production in NIH mice.
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PMID:Immunogenicity and protective efficacy of pertussis toxin subunit S1 produced by Bacillus subtilis. 190 67

This paper describes the development of a murine bank of monoclonal antibodies against Bordetella pertussis toxin, filamentous hemagglutinin (FHA), pili, lipopolysaccharide (LPS), or outer membrane proteins (OMPs). Subunits S1, S2, S3 of pertussis toxin (PT) bound immunoglobulins and glycoproteins such as fetuin and haptoglobin in an unspecific manner. The specificity of monoclonal antibodies towards subunits S1, S2, S3 or S4 of PT could be demonstrated by using purified immunoglobulins or their Fab2 fragments. A set of FHA-specific monoclonal antibodies could be differentiated on the basis of their binding to the various breakdown products present in FHA preparations. Pili-specific monoclonal antibodies reacted with either native pili or denatured pilin, and both demonstrated serotype specificity. Monoclonal antibodies to Bordetella pertussis OMPs were directed to either the virulent phase-regulated trypsin-sensitive, detergent-extractable OMPs 92 kDa, 32 kDa, and 30 kDa or the non-virulent phase-expressed, not-trypsin sensitive OMPs 38 kDa, 33kDa, and 18 kDa.
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PMID:Description of a hybridoma bank towards Bordetella pertussis toxin and surface antigens. 198

An assay has been developed for Bordetella pertussis heat-labile toxin (HLT) based on morphological alterations in certain human embryonic lung (HEL) cell lines. Eighteen cell lines from human and other sources were tested but only two, MRC-5 and HELu2, were responsive to HLT. Confluent monolayers of the cells contracted within 24 h of exposure to the toxin, but without loss of viability during incubation for a further 3 days. The effect of HLT was quantitated by scoring the extent of morphological change, and by the decrease in Giemsa staining of the cell monolayers, as measured on an ELISA plate reader. This cell culture assay for HLT was more sensitive than lethality titration in mice but the dose-response curve had a lower slope. The specificity of the response was established by comparing unheated HLT with HLT heated at 56 degrees C, and with extracts from transposon-insertion mutants of B. pertussis which were deficient in HLT. Purified preparations of pertussis toxin and B. pertussis lipopolysaccharide gave no morphological response even at high doses.
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PMID:Assay of Bordetella pertussis heat-labile toxin with human embryonic lung cells. 199 Jan 37

The viability of four strains of Bordetella bronchiseptica, two strains of B. pertussis and one strain of B. parapertussis exposed to hyperimmune and pre-colostrum porcine serum was examined. Viable cell numbers (cfu/ml) of the B. pertussis strains and a rough strain of B. bronchiseptica (CSU-P-1) decreased by 99% and 99.99%, respectively, after exposure for 1 h to porcine hyperimmune serum. In contrast, smooth B. bronchiseptica strains and the B. parapertussis strain showed no significant decrease in viable cell numbers after the same treatment. B. bronchiseptica strain CSU-P-1 also showed a 99% decrease in viable cell numbers after exposure to pre-colostrum porcine serum for 1 h whereas the other strains tested showed no decrease in viable numbers under the same conditions. Heating the hyperimmune and pre-colostrum serum at 56 degrees C for 30 min resulted in the loss of bactericidal activity suggesting the involvement of complement in both systems. Analysis of silver-stained SDS-PAGE profiles of lipopolysaccharide (LPS) extracted from the bacterial cells indicated that the smooth strains of B. bronchiseptica and the B. parapertussis strain possessed high mol. wt O-side chain-like material, whereas the B. pertussis strains and B. bronchiseptica strain CSU-P-1 did not. Gel filtration of acid-hydrolysed LPS samples indicated two distinct carbohydrate peaks for the strains with high mol. wt O-side chain-like material, whereas the other strains each yielded one distinct peak. Western-blot analysis indicated a positive reaction for anti-B. bronchiseptica antibodies to the high mol. wt O-side chain-like material of all serum-resistant strains used in this study.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:Serum sensitivity and lipopolysaccharide characteristics in Bordetella bronchiseptica, B. pertussis and B. parapertussis. 201 Sep 7


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