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)

The gram-negative organism causing abortion in dogs was examined in parallel with cultures representative of the Brucella species and with Bordetella bronchiseptica. The organism fits into the genus Brucella and most closely resembles B. suis on the basis of its growth characteristics. It is of rough colonial morphology and is agglutinated by antisera prepared against rough Brucella. In mouse toxicity tests, no endotoxic activity could be demonstrated. In contrast to most Brucella cultures, it does not utilize erythritol. Electron microscopy showed a cell wall structure similar to that of other gram-negative organisms. The question of whether the organism should be designated Brucella canis, as proposed by Carmichael and Bruner, or Brucella suis biotype 5 is discussed. The authors favor the designation Brucella canis because the organism lacks the lipopolysaccharide antigen associated with the smooth agglutinogen and endotoxin, and it does not utilize erythritol.
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PMID:Taxonomic position in the genus Brucella of the causative agent of canine abortion. 568 22

The tetrasaccharide beta-D-glucopyranosyl-(1,3)-beta-D-glucopyranuronyl-(1, 2)-L-glycero-alpha-D-manno-heptopyranosyl-(1,5)-3-deoxy-D-manno-2- octulosonic acid was isolated after treatment of polysaccharide 1 of Bordetella pertussis endotoxin with nitrous acid. Taking into account previously identified di- and trisaccharide fragments and analytical data obtained for the intact polysaccharide 1, we present the structure of a heptasaccharide that is thought to represent the region immediately adjacent to the hydrophobic (lipid A) moiety of lipopolysaccharide 1 of the B. pertussis endotoxin. This heptasaccharide represents 50 to 60% of the complete polysaccharide structure.
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PMID:Structure of the terminal reducing heptasaccharide of polysaccharide 1 isolated from the Bordetella pertussis endotoxin. 608 79

Bordetella pertussis bacterial cells, bacterial extracts, and concentrated culture supernatant fluid were comparatively examined for histamine sensitizing and leucocytosis promoting activities, toxicity (mouse weight gain test), immunoprotective potency and lipopolysaccharide bioassay. The activity of histamine sensitizing factor always paralleled that of leucocytosis promoting factor. In contrast, important differences were demonstrated regarding the toxicity and protective activity of the three preparations. Culture supernatant was more toxic and less protective than either bacterial cells or cell extract. Although the latter had lower protective potency than whole cells, its lower toxicity might lead to its consideration as a possible potential vaccine.
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PMID:Comparative toxicity, protective, histamine sensitizing and leucocytosis promoting activities in mice of Bordetella pertussis culture fluid, bacterial cells and cell extracts. 609 86

Monoclonal antibodies to Bordetella pertussis were produced by fusion of mouse myeloma cells and spleen cells of immunized mice. Cell lines were examined for specific antibody production against several crude antigen preparations and lipopolysaccharide. Cross reactivity of monoclonal antibodies was assessed by enzyme immunoassay using cell lysates prepared from Bordetella spp. and several other bacteria. Reactivity of monoclonal antibodies to cell surface components was determined by immunofluorescence microscopy. Monoclonal antibodies represent useful probes to study the antigenic profile and distribution of antigens among various species of Bordetella, as well as specific tools to study the structure and function of B. pertussis virulence factors.
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PMID:Isolation and characterization of monoclonal antibodies to Bordetella pertussis. 609 81

The content of 3 antigens--filamentous haemagglutinin, lymphocytosis-promoting factor, and serotype-specific agglutinogens (fimbriae)--was determined in the current UK whole-cell whooping cough vaccine. Antibodies to these antigens and to outer membrane proteins and lipopolysaccharide of Bordetella pertussis were measured in the serum of unvaccinated children and children who had received 1, 2, or 3 doses of the vaccine. Children who had received one dose of vaccine had varied low antibody titres. Children who had received two or three doses had significantly higher antibody titres to all the antigens tested, as did some unvaccinated children with no history of whooping cough. This study shows that filamentous haemagglutinin, lymphocytosis promoting factor, and outer membrane proteins are immunogenic constituents of the whole-cell vaccine. Their inclusion in a subcellular vaccine would not involve novel antigens.
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PMID:Antigens in whooping cough vaccine and antibody levels induced by vaccination of children. 613 97

Endotoxin prepared from several Bordetella pertussis strains in both immunological phases I and IV gave two lipopolysaccharide peaks (LPS-I and LPS-II) when analyzed on hydroxylapatite columns in a phosphate buffer containing 0.1% sodium dodecyl sulfate; these lipopolysaccharides, present in the ratio of 2:3, are true endotoxins by both chemical and biological criteria. Endotoxins isolated from Escherichia coli, Salmonella typhimurium, and Shigella flexneri gave single lipopolysaccharide peaks when analyzed by the same procedure. Upon hydrolysis with acetic acid (pH 3.4) at 100 degrees C for 1 h, LPS-I released a polysaccharide (PS-I); the linkage broken was that of the glycosidic bond of a non-phosphorylated 3-deoxy-oct-2-ulosonic acid. Treatment with 0.25 M mineral acid at 100 degrees C for 30 min was required to free the polysaccharide moiety (PS-II) of LPS-II, the linkage broken being the glycosidic bond of a phosphorylated 3-deoxy-oct-2-ulosonic acid. Chemical and physical differences of the polysaccharide moieties PS-I and PS-II present in LPS-I and LPS-II have been described previously (25). By using the technique of 125I labeling, it was shown that the totality of labeled proteins present in the endotoxin extracted from Bordetella pertussis by the phenol-water procedure could be separated from the lipopolysaccharide by column chromatography on hydroxylapatite; it follows that these proteins are not linked by covalent bonds to the lipopolysaccharide.
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PMID:Isolation of two protein-free and chemically different lipopolysaccharides from Bordetella pertussis phenol-extracted endotoxin. 624 93

Lipopolysaccharide extracted from Bordetella pertussis was mitogenic for spleen cells of endotoxin-resistant C3H/HeJ mice. Although endotoxic lipid A was inactive, mitogenic activity of lipopolysaccharide was exhibited by purified preparations of polysaccharides I and II, which constitute the carbohydrate moiety of the macromolecule. These low-molecular-weight (2,800 and 3,600) polysaccharides, containing carboxyl groups, were not mitogenic for thymocytes and splenic T-cells of C3H/HeJ mice, but did show mitogenic activity for splenic B-cells of C3H/HeJ mice and for spleen cells of C57BL/6 athymic nude mice. The mitogenic activities of polysaccharides I and II were also compared with those of other polyanionic polysaccharides, and the results indicate that high molecular weight is not necessary, and negative charges are not sufficient, for mitogenicity.
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PMID:Mitogenic response of C3H/HeJ mouse lymphocytes to polyanionic polysaccharides obtained from Bordetella pertussis endotoxin and from other bacterial species. 626 Jun 59

Effects of Bordetella pertussis organisms, such as adjuvanticity, induction of hypersplenia, and leukocytosis as well as modification of nonspecific resistance to infection and typical morphological response of lymphatic organs, were studied in the lipopolysaccharide-resistant C3H/HeJ mouse strain. It was shown that B. pertussis exerted all of these effects in C3H/HeJ mice, although the morphological response, hypersplenia, and modification of resistance to infection with Listeria monocytogenes in such animals were less pronounced than those in lipopolysaccharide-sensitive mouse strains. This indicated that the biological activity of B. pertussis as determined in the present studies, is due partly to structural components other than lipopolysaccharide.
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PMID:Biological activity of Bordetella pertussis in lipopolysaccharide-resistant mice. 626 65

Endotoxin activity in suspensions of Bordetella pertussis, Escherichia coli, Haemophilus influenzae, and Pseudomonas aeruginosa was often markedly decreased by polymyxin B. Polymyxin B treatment may be a means to reduce inflammatory reactivity of lipopolysaccharide in vaccines of gram-negative bacteria.
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PMID:Polymyxin B inactivation of lipopolysaccharide in vaccines of Gram-negative bacteria. 626 67

Two Bordetella pertussis antigen preparations, outer membrane protein (OMP) and filamentous haemagglutinin (FHA), and a standard vaccine were used to immunize rabbits, and the effects on nasopharyngeal colonization by the organism were determined. Antibodies were measured in serum and in nasal washes by ELISA before and after challenge of the rabbits with 10(6) bacteria of strain M2. Recoveries of B. pertussis in nasal washes were used to assess colonization, which in controls persisted for at least 65 days. Some rabbits of all the immunized groups showed enhanced clearance, but there was no correlation between the elimination of B. pertussis and serum antibodies to OMP, FHA, lipopolysaccharide, lymphocytosis-promoting factor or agglutinogen 3. In contrast, nasal IgA antibody to FHA showed significant inverse correlation with bacterial persistence. Such antibody was induced by the OMP preparation as well as by FHA, but to different extents depending on the immunization schedule and adjuvant used.
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PMID:Rabbit nasopharyngeal colonization by Bordetella pertussis: the effects of immunization on clearance and on serum and nasal antibody levels. 628 59


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