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Query: UMLS:C0043167 (pertussis)
 19,595 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

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 suspension of B. pertussis cells in 0.15 M NaC1 solution, used for the preparation of corpuscular pertussis vaccine contains components loosely bound to microbial cells and producing pronounced mitogenic effect on mouse splenocytes at a concentration of 10 micrograms/ml. The mitogenic activity of B. pertussis is due to complex substances (lipopolysaccharide, protein, nucleic acids) with a wide range of molecular weights (70,000 to greater than 400,000). The mitogenic factor showing no leukocyte-stimulating and protective activity has been isolated by sedimentation with ammonium sulfate and gel filtration on Sephadex G-200. The mitogenic activity of B. pertussis lipopolysaccharide in the blast transformation test has been confirmed.
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PMID:[Mitogenic action of the liquid phase of a microbial suspension of Bordetella pertussis]. 289 Feb 49

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

Analysis of the lipopolysaccharide (LPS, endotoxin) in cell sonicates of four Danish vaccine strains of Bordetella pertussis (3803, 3825, 3843 and 3860) and of purified strain 3803 LPS in sodium dodecyl sulphate-polyacrylamide gel electrophoresis by silver staining, showed identical profiles. The LPS profile revealed a dominant, brownish LPS II band and a minor, faster-migrating, black-stained LPS I band. However, the ratio of LPS I to LPS II in the preparation of purified LPS differed slightly from the cell sonicates. Using marker LPS, the molecular weights of LPS I and LPS II were estimated at 5.4 and 6.0 kD, respectively. Seven different lots of whole cell pertussis vaccine were assayed for LPS in the Limulus Amoebocyte Lysate test and were found to contain 0.9-2.8 micrograms LPS/ml. No significant difference in the content of LPS in similar dilutions of the individual strains was observed. In addition, the distribution of free and cell-bound LPS in four pertussis vaccines was investigated. Most of the LPS was found to exist as free LPS. During several months, the course of both LPS and pertussis toxin (Pt) release in freshly killed B. pertussis preparations was followed. In the first few weeks, 35-50% of the LPS was released and after 5-6 months of storage 60-80% had been released. In contrast, less than 10% of the biologically active pertussis toxin was released during the experimental period. The possibility of producing a safer whole cell pertussis vaccine by reducing the amount of free LPS without reducing the protective value correspondingly is discussed.
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PMID:Lipopolysaccharides in a traditional pertussis vaccine. 290 42


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