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)

Endotoxin protein represents a group of immunobiologically active p polypeptides which are associated with the lipopolysaccharide endotoxin in the outer membrane of Gram-negative bacteria. To study the adjuvant effect of endotoxin protein, CF-1 mice were immunized intraperitoneally with graded doses of glutaraldehyde-inactivated cholera toxoid with and without endotoxin protein prepared from Bordetella pertussis, Salmonella typhi or Vibrio cholerae. Immune responsiveness was assessed by measuring resistance to intravenous challenge with cholera enterotoxin and by serum antitoxin responses. The results showed that endotoxin protein from S. typhi can enhance the 50% protective dose (PD50) of cholera toxoid five to 12-fold, the endotoxin protein from V. cholerae enhances the PD50 six to seven fold at most, but the endotoxin protein from B. pertussis can enhance the PD50 some 27-fold. Furthermore, within the variability of both the mouse protection test and the rabbit intracutaneous assay of toxin induced vascular permeability, mouse serum neutralizing antitoxin levels correlated with the greater degree of resistance of the mice to the toxin challenge. The adjuvant effect also has been demonstrated by measuring the appearance of antitoxin specific plaque forming cells derived from mouse lymphocyte cultures. After seven days of culture in the presence of endotoxin protein and cholera toxoid, the number of plaque forming cells to cholera toxin coated sheep erythrocytes was enhanced some 28 times as compared to the cultures exposed to the cholera toxoid alone.
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PMID:The adjuvant effect of pertussis endotoxin protein in modulating the immune response to cholera toxoid in mice. 287 8

The serum antibody responses of vaccinated children and whooping cough patients to the highly purified Bordetella pertussis antigens, leukocytosis-promoting factor (LPF), lipopolysaccharide (LPS), a protein binding to complement-fixing antibodies induced during whooping cough (PBCA) and to a partly purified filamentous hemagglutinin fraction (FHA) were analysed in enzyme-linked immunosorbent assay. Of the IgG antibodies, those to FHA and LPS were often persistent both after infection and vaccination. The mean titers were about six to ten times higher after disease than after vaccination in corresponding age groups. IgG antibodies to LPF were frequently detected in high titers in patients (mean arbitrary units = 1723), but seldom in low titers (mean units = 20), after vaccination. IgG antibodies to PBCA disappeared some years after vaccination. IgM antibodies to PBCA, FHA and LPS were present in almost 100% after vaccination and disease. IgM antibodies to LPF were detected in 23% of the vaccinated and in 83% of the patients. The respective mean IgM units to PBCA, FHA, LPS and LPF were 14, 13, 16 and 134 times higher in patients than in vaccinated children. None of the vaccinated children and 20% of the patients had IgA antibodies to LPF. No pronounced differences in the percentage of the respective IgA responses to PBCA, the FHA fraction and LPS were found between the two groups. The striking differences in the immune response of vaccinated children and patients were to LPF. Since whooping cough protects better than vaccination against B. pertussis infection, the present study indicates that immunogenic LPF should be included in an acellular vaccine. Also addition of FHA, PBCA and possibly even of LPS, if it can be prepared in an immunogenic and atoxic form, might be necessary in order to prepare a highly effective acellular vaccine.
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PMID:Antibody responses after vaccination and disease against leukocytosis promoting factor, filamentous hemagglutinin, lipopolysaccharide and a protein binding to complement-fixing antibodies induced during whooping cough. 287 24

The levels of antibodies to disintegrated Bordetella pertussis and its individual fractions (protein and polysaccharide) in children immunized with different batches of adsorbed DPT vaccine have been determined with the use of EIA techniques. The background level of antibodies in the control groups has been determined, and in immunized children the levels of antibodies to disintegrated B. pertussis and its protein fraction have been shown to considerably exceed the levels of antibodies to lipopolysaccharide.
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PMID:[Antipertussis immunity studied by immunoenzyme analysis]. 287 81

The surface proteins of several Bordetella strains and their modulated derivatives were examined by surface radioiodination, cell fractionation, and Western blotting. A surface protein with a high Mr, missing in a mutant lacking the filamentous hemagglutinin, was identified in virulent Bordetella pertussis and Bordetella parapertussis cells and was absent in avirulent B. pertussis strains. The electrophoretic profiles of lipopolysaccharide and the 40,000-Mr anion-selective porin were not determinants which correlated with phase variation or phenotypic modulation. At least three envelope proteins (91,000, 32,000, and 30,000 molecular weight) were found only in virulent B. pertussis strains and were absent or diminished in the avirulent phase and most phenotypically modulated strains. Two transposon-induced mutants unable to produce hemolysin, dermonecrotic toxin, pertussis toxin, and filamentous hemagglutinin also lacked these three envelope proteins, confirming that virulence-associated envelope proteins were genetically regulated with other virulence-associated traits.
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PMID:Surface proteins of Bordetella pertussis: comparison of virulent and avirulent strains and effects of phenotypic modulation. 287 57

Free lipid A of Bordetella pertussis, Neisseria meningitidis, and Escherichia coli lipopolysaccharide (LPS) was prepared by hydrolysis in acetate buffer (pH 4.5); in addition, lipid A from B. pertussis and E. coli was prepared by hydrolysis in mineral acid (HCl). The precipitates obtained were purified by extraction methods in toluene-methanol and are referred to as crude lipid A. Purified lipid A from N. meningitidis and B. pertussis was obtained by extraction in a mixture of chloroform-methanol-water-triethylamine. The different preparations were tested for their pyrogenicity (endogenous pyrogen; EP) and their capacity to trigger the release of interleukin-1 (IL-1; previously known as lymphocyte-activating factor; LAF) by human monocytes. Crude lipid A from E. coli and N. meningitidis were both IL-1 inducers. Crude B. pertussis lipid A (acetate buffer; pH 4.5), which contains a beta-1-6-linked D-glucosamine disaccharide, two phosphoryl groups, and five fatty acids, was pyrogenic and an IL-1 inducer (EP+/LAF+); but crude B. pertussis lipid A (0.25 N HCl), which lacked the glycosidic phosphoryl group, was 1,000-fold less pyrogenic than the diphosphorylated lipid A, yet it retained its IL-1-inducing capacity (EP-/LAF+). Purified N. meningitidis lipid A was not an inducer of IL-1 release and purified B. pertussis lipid A exhibited identical pyrogenicity as the parent LPS but was devoid of any IL-1-release inducing capacity (EP+/LAF-). These results demonstrate that for some endotoxins, purified lipid A is unable to induce IL-1 release by human monocytes; however, it is pyrogenic, supporting the hypothesis that IL-1 and EP are induced by different determinants on the LPS molecule.
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PMID:Inability of pyrogenic, purified Bordetella pertussis lipid A to induce interleukin-1 release by human monocytes. 287 60

The content of antibodies to B. pertussis disintegrated cells, protein fraction and lipopolysaccharide in the blood of patients and convalescents has been studied. The study has revealed that in the blood sera of whooping cough patients the titers of antibodies to lipopolysaccharide considerably exceed the titers of antibodies to other antigenic fractions. The titers of IgM to lipopolysaccharide have been shown to exceed the titers of IgM to other fractions 1.5-2 times.
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PMID:[Immune response to various antigenic preparations of Bordetella pertussis in whooping cough patients and convalescents studied by immunoenzyme analysis]. 287 3

The sera of children and adults with a history of pertussis, as well as the sera of children immunized in three injections, have been studied in the enzyme immunoassay. The levels of antibodies to Bordetella pertussis protein and lipopolysaccharide, and to disintegrated B. pertussis cells have been determined; a serum titer of 1:1,600 and higher is considered as a criterion for the serological diagnosis of pertussis.
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PMID:[Possible serodiagnosis of pertussis infection by an immunoenzyme method]. 289 Dec 32

Hybrid cell lines producing monoclonal antibodies against Bordetella pertussis lipopolysaccharide (LPS) were established. The specificity of the antibodies was ascertained by enzyme-linked immunosorbent assay (ELISA) and ELISA-inhibition experiments with LPS and delipidated polysaccharide fragments (PS-1 and PS-2) prepared from B. pertussis LPS. Monoclonal antibody 9-1-H5 reacted with B. pertussis LPS only, whereas monoclonal antibodies 6-4-H6 and 9-2-A8 reacted with PS-1 and PS-2 as well as B. pertussis LPS. The antibodies did not react with LPS prepared from B. parapertussis and B. bronchiseptica in an LPS-specific ELISA. A monoclonal antibody-based sandwich ELISA was developed for detection of B. pertussis LPS. This assay had a detection limit of B. pertussis LPS in concentrations ranging from 0.16 to 0.32 microgram/ml. The assay was also shown to be specific for the detection of whole B. pertussis bacteria. No cross-reactions were observed with strains of Branhamella catarrhalis, Neisseria meningitidis, Streptococcus miteor, Haemophilus influenzae, or Legionella pneumophila. The monoclonal antibodies might be useful for the detection of soluble antigens and whole bacteria in clinical samples and for studies of the immunochemical structure of B. pertussis LPS.
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PMID:Production and characterization of monoclonal antibodies directed against Bordetella pertussis lipopolysaccharide. 289 6

The absence of subunit S3 in cell-associated pertussis toxin (PT) from a mutant of Bordetella pertussis which failed to produce cell-free toxin suggested that this subunit was involved in the release of PT into the culture medium. The addition of methylated beta-cyclodextrin (MCD) to the culture medium caused a small but consistent increase in the release of lipopolysaccharide (LPS) by four wild-type strains of B. pertussis. Since previous studies have shown that MCD also enhances the levels of PT in culture supernates, it seemed probable that the increased shedding of outer-membranes vesicles (OMV) may explain the increased levels of both cell-free PT and LPS. Release of PT was inhibited in media buffered with HEPES but was unaffected in Tris/HC1 buffer. This suggested that in addition to shedding of the outer membrane, increased permeability and greater destabilization of the outer membrane, as caused by Tris/HC1 buffer, may be important in the release of PT. Our data do not support the idea that PT is packaged into OMV because only an insignificant proportion (0.01%) of the total cell-free PT was associated with LPS. The association of PT with small micelles derived from outer-membrane amphiphiles may be more important since the LPS content of PT purified from culture supernates (containing no large OMV) was nearly 18% by weight.
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PMID:Release of pertussis toxin and its interaction with outer-membrane antigens. 289 25

The B lymphocytes and macrophages of lipopolysaccharide (LPS) nonresponder C3H/HeJ mice were found to respond to certain R types of LPS endotoxin in a fashion resembling that ordinarily seen with the cells from normal responder mice. DNA synthesis, polyclonal antibody synthesis, and interleukin-1 activity were stimulated by Bordetella pertussis LPS and Salmonella minnesota R595 LPS, although to a lesser extent than with responder cells. Mitogenesis stimulated by both LPSs was inhibited by polymyxin B; this finding provided evidence that any trace endotoxin-associated proteins were not responsible for the activity. Of particular interest was the finding that wild-type smooth LPS actually inhibited activation of the C3H/HeJ B cells not only by the LPS but also by mitogenic proteins, including purified protein derivative of tuberculin. The nonspecific nature of this inhibition and the fact that maximal inhibition occurred some 9 to 12 h into the culture period suggested that the proliferation of the B cells was affected by smooth-type LPS in a manner heretofore unrecognized. These findings permit a new approach to the study of how LPS endotoxin affects cells of the immune system.
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PMID:Inhibition of activated nonresponder C3H/HeJ lymphocytes by lipopolysaccharide endotoxin. 290 22


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