Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

The outer membrane (OM) component(s) from Bordetella pertussis which potentiated the antigenicity of purified Haemophilus influenzae type b capsular polysaccharide, polyribosyl ribitol phosphate (PRP), has been isolated and partially characterized. The OM was isolated from spheroplasting medium by precipitating at pH 5.0; fractionation was carried out by dissolving the crude OM in Triton X-100 followed by selective precipitation of OM in 50% ethanol. Further purification of OM was accomplished by DEAE-Sepharose 6BCL and Sephacryl S-300 chromatography. The biochemical composition and protein profiles on sodium dodecyl sulfate-polyacrylamide gel electrophoresis of various OM preparations have been examined. Combined vaccines consisting of OM components and PRP were given to young Sprague-Dawley rats, and the serum antibody to PRP was measured by an [3H]PRP binding assay. The purified OM containing mainly a 30,000-dalton protein, but not purified lipopolysaccharide or leukocytosis-promoting toxin, exhibited strong enhancement of PRP immunogenicity.
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PMID:Isolation of the outer membrane components of Bordetella pertussis which enhance the immunogenicity of Haemophilus influenzae type b capsular polysaccharide polyribosyl ribitol phosphate. 286 92

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

Haemophilus influenzae are small, gram-negative, rod-shaped bacteria. Because of their special growth requirements, they do not grow on usual blood agar media, but flourish on the mucosal membranes of the human respiratory tract where they adhere to the epithelial cells by fimbriae (a potential vaccine component). Nasopharyngeal carriage of Haemophilus influenzae is very common, and in healthy carriers the bacteria are usually unencapsulated. The outer membrane of Haemophilus influenzae contains lipopolysaccharide (of so called R form, without O antigen) and major outer membrane proteins. The lipopolysaccharide is a virulence determinant. An extracellular enzyme, IgA protease, is another potential virulence determinant. The outer membrane of Haemophilus influenzae is a rather ineffective barrier towards antibiotics, and thus the major determinants of antibacterial resistance in Haemophilus influenzae are plasmid-coded enzymes that inactivate the antibiotic, and changes in the target molecules.
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PMID:Unencapsulated Haemophilus influenzae--what kind of pathogen? 290 69

Outer membranes of Haemophilus influenzae type b were fractionated to yield Triton X-100-insoluble material and lipopolysaccharide and phospholipids. Liposomes reconstituted from lipopolysaccharide and phospholipids were impermeable to sucrose (Mr, 342) and to a high-molecular-weight dextran (average Mr, 6,600). When the Triton X-100-insoluble material was introduced into the reconstituted liposomes, the vesicles became permeable to sucrose, raffinose (Mr, 504), and stachyose (Mr, 666) and fully retained dextrans of Mr greater than 1,500. Inulin (average Mr, 1,400) was tested for its efflux from the reconstituted outer membrane vesicles; 62% of the added inulin was trapped. The molecular weight exclusion limit for the outer membrane of H. influenzae type b was therefore estimated at approximately 1,400. A protein responsible for the transmembrane diffusion of solutes was purified from H. influenzae type b by extraction of whole cells with cetyl trimethyl ammonium bromide. When this extract was passed over DEAE-Sepharose, three protein-containing peaks (I, II, and III) were eluted. Peaks I and II contained mixtures of proteins as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; when tested for their pore-forming properties, these proteins were unable to render liposomes of lipopolysaccharide and phospholipid permeable to sucrose. Peak III contained only one molecular species of protein of molecular weight 40,000; this protein acted as a porin in reconstituted vesicles. The molecular weight exclusion limit for 40,000-molecular-weight protein matched the estimate of approximately 1,400 which was determined for outer membranes. A series of homologous saccharides of increasing degree of polymerization was prepared from agarose by hydrolysis with beta-agarase and fractionation on gel filtration chromatography. These oligosaccharides of Mr, 936, 1,242, 1,548, and 1,854 were assayed for retention by the complete vesicles containing 40-kilodalton protein and lipopolysaccharide and phospholipids. All of these oligosaccharides were lost by efflux through the porin. Since the molecular conformation of the largest oligosaccharide is an elongated semirigid helix, it is suggested that the pore formed by the 40-kilodalton protein does not act as a barrier to the diffusion of this compound.
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PMID:Transmembrane permeability channels across the outer membrane of Haemophilus influenzae type b. 298 94

By phenol-water extraction an aqueous-phase soluble cellular lipopolysaccharide was isolated from Haemophilus pleuro-pneumoniae serotype 1. It was shown by sodium dodecyl sulfate-polyacrylamide gel electrophoresis, hydrolysis, methylation, and both one- and two-dimensional 1H and 13C nuclear magnetic resonance studies to be an S-type lipopolysaccharide, which could be cleaved to yield a lipid A and an O-chain polysaccharide identified as a high molecular weight branched polymer of a tetrasaccharide repeating unit having the structure: (Formula: see text).
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PMID:Structure of the O-chain of the lipopolysaccharide of Haemophilus pleuropneumoniae serotype 1. 303 18

The mechanism(s) by which the lipopolysaccharide (LPS) of Haemophilus influenzae type b may contribute to the virulence of this organism is unclear. Purified LPS of Haemophilus influenzae type b or phosphate buffered saline was administered intranasally to infant rats prior to the intranasal instillation of approximately 2-20 x 10(6) cfu of Hib two or three times per day for three consecutive days. The preadministration of 2.0 micrograms Hib LPS resulted in a significantly greater incidence of bacteremia (P = 0.0006) than PBS 30 min after the completion of the intranasal inoculation. Four days following completion of intranasal Hib inoculation the incidence of bacteremia was greater (P = 0.017) in the animals pretreated with LPS at 2.0 micrograms compared to the PBS pretreated animals. Preadministration of 0.2 micrograms LPS had no effect on the incidence of bacteremia or meningitis. There were no differences in the histology of the nasal cavities or turbinates of infant rats inoculated intranasally only with LPS or PBS. There were no differences in the frequency or density of bacteremia following intranasal administration of LPS from either Hib or E. coli. Although the mechanism is unknown, our findings suggest that the LPS of Hib may contribute to the ability of H. influenzae type b to invade the nasal mucosa in this infant rat model.
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PMID:Contribution of Haemophilus influenzae type b lipopolysaccharide to pathogenesis of infection. 307 63

Approximately 6% of 50 tested human sera possessed precipitating antibody against lipopolysaccharide from Haemophilus actinomycetemcomitans (Actinobacillus actinomycetemcomitans).
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PMID:Precipitating antibody against lipopolysaccharide of Haemophilus actinomycetemcomitans in human serum. 309 72

Serotyping of Haemophilus pleuropneumoniae and serologic assays for detection of serotype-specific antibody are problematic due to the potential cross-reactivity of the crude antigens used for raising immune serum or for serology. The capsular polymer (CP) of H. pleuropneumoniae serotype 5 was investigated for serotype-specific activity with antiserum to whole cells or with antiserum made monospecific to CP by adsorption with a capsule-deficient mutant. When antiserum to whole cells or monospecific antiserum to CP was tested against purified CP from serotypes 1 to 7 by immunodiffusion or enzyme-linked immunosorbent assay, only capsules of serotype 5 were reactive. In addition, only encapsulated serotype 5 cells reacted with serum monospecific to CP in an indirect immunofluorescent-antibody assay. Serotype-specific antibody was completely inhibited in each assay by preincubation of purified CP with the serum. Antiserum to whole cells of H. pleuropneumoniae serotype 5 contained antibodies to proteins and lipopolysaccharide; these antibodies cross-reacted with antigens of heterologous serotypes by dot-blot enzyme-linked immunosorbent assay and immunoblotting. The antigenic activity of CP was stable after heating for at least 30 min at 100 degrees C. High titers of antibody to CP were present in the sera of rabbits immunized intravenously with whole log-phase cells or in the convalescent sera of pigs experimentally infected with H. pleuropneumoniae serotype 5. However, the purified CP was poorly immunogenic in rabbits and swine. Our results indicate that the capsule is the serotype-specific antigen of H. pleuropneumoniae and that a monospecific antiserum to capsule or purified capsule should be used for serotyping or serologic assays, respectively.
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PMID:Serotype specificity and immunogenicity of the capsular polymer of Haemophilus pleuropneumoniae serotype 5. 311 66

Three immunoglobulin preparations for intravenous infusion were compared in vivo to determine their relative protective capacity against several gram-negative and gram-positive pathogens. Polyglobin N is a conventional IgG concentrate. Psomaglobin N is identical in formulation to Polyglobin N but is prepared from the plasma of donors who have naturally high levels of antibody to lipopolysaccharide antigens of Pseudomonas aeruginosa. IgGMA is a conventional IgG concentrate containing 12% IgG and 16% IgA. In a murine model of burn wound sepsis the three IgG preparations were similarly protective against three or ten strains of P. aeruginosa. Psomaglobin N and Polyglobin N were significantly (p less than or equal to 0.015) more protective than IgGMA against six of ten and three of ten strains of P. aeruginosa, respectively. In a murine model of Streptococcus pneumoniae type 3 pneumonia, the three Ig preparations were similarly protective. IgGMA was significantly more protective (p less than or equal to 0.025) than Psomaglobin N and Polyglobin N against Salmonella typhimurium in murine peritonitis. However, the mean protective dose (PD50) of the two later preparations was less than or equal to 20 mg/kg body weight. In models of peritonitis both Psomaglobin N and Polyglobin N were more protective than IgGMA (p less than or equal to 0.004) against Haemophilus influenzae b, Klebsiella pneumoniae, Serratia marcescens 06:H3 and group B Streptococcus types 1b and 1c. Psomaglobin N and ciprofloxacin were employed to treat established polymicrobial murine burn wound sepsis resulting from contamination of the burn site with mixtures of P. aeruginosa and Staphylococcus aureus.(ABSTRACT TRUNCATED AT 250 WORDS)
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PMID:[Prevention of gram-negative and gram-positive infections with 3 intravenous immunoglobulin preparations and therapy of experimental polymicrobial burn infection with intravenous Pseudomonas immunoglobulin G and ciprofloxacin in an animal model]. 311 21

The influence of detergents on the immunogenic activity of the major outer membrane protein of Neisseria gonorrhoeae was investigated. Most detergents tested were found to enhance the immune response. This effect was synergistic with the adjuvant activity of AlPO4. The combination of detergent and AlPO4 showed a stronger adjuvant activity than Freund's complete adjuvant. The adjuvant effect was only observed with protein preparations with very low lipopolysaccharide content. The immunostimulating effect of detergents was also observed with meningococcal group C polysaccharide conjugated to a Haemophilus influenzae type b outer membrane protein and with the fusion protein of measles virus. The influence of some detergent parameters (critical micelle concentration, hydrophile-lipophile balance, charge) was investigated.
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PMID:Synergistic effect of detergents and aluminium phosphate on the humoral immune response to bacterial and viral membrane proteins. 312 65


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