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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Strains of Haemophilus influenzae (n = 161) were isolated from inpatients with symptoms of pulmonary infection. Conventional tests showed that 144 strains were non-serotypable and all belonged to one of eight biotypes. The common biotypes were 2 (41%), 3 (27.1%), 1 (13.2%) and 5 (10.4%). The outer membrane protein (OMP) profiles of 59 non-serotypable strains were examined by sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE). A comparison of OMP profiles suggested a possible association between several strains belonging to biotype 2. Although no clear correlation was established between biotype or OMP profile cluster groups and the age or clinical state of the patients from whom the strains were isolated, SDS-PAGE analysis was a useful technique for the epidemiological study of non-serotypable H influenzae.
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PMID:Outer membrane protein and biotype analysis of non-serotypable strains of Haemophilus influenzae. 278 34

Haemophilus influenzae biogroup aegyptius (H. aegyptius) has been identified as the etiologic agent of the recently described disease Brazilian purpuric fever (BPF). Although there is heterogeneity among the strains associated with conjunctivitis, isolates from patients with BPF appear to be derived from a single clone. The clinical presentation of BPF suggests that bacterial lipopolysaccharides (LPS) are involved in its pathogenesis. We prepared LPS from H. influenzae biogroup aegyptius and found them to be similar to H. influenzae type b LPS in apparent size (by sodium dodecyl sulfate-polyacrylamide gel electrophoresis), biological activities, and fatty acid composition. We compared LPS from BPF clone isolates with LPS from non-BPF clone isolates in tests of Limulus lysate activation, spleen cell mitogenesis, promotion of neutrophil adherence to LPS-treated endothelial cells, and the dermal Shwartzman reaction. In none of these activities were LPS from the BPF clone isolates more potent. Because LPS shed from growing bacteria may be involved in the pathogenesis of purpura, we also measured the rate at which LPS were released into culture medium during bacterial growth and found no significant difference between BPF clone and non-BPF clone isolates.
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PMID:Comparison of lipopolysaccharides from Brazilian purpuric fever isolates and conjunctivitis isolates of Haemophilus influenzae biogroup aegyptius. Brazilian Purpuric Fever Study Group. 278 2

Isolates of Haemophilus influenzae type b (Hib) can be divided into three antigenic groups based on their reactivities with a set of two monoclonal antibodies (MAbs) directed against epitopes in the oligosaccharide region of Hib lipooligosaccharide (LOS) (P. A. Gulig, C. C. Patrick, L. Hermanstorfer, G. H. McCracken, Jr., and E. J. Hansen, Infect. Immun. 55:513-520, 1987). Approximately 24% of Hib strains react with both of these LOS-specific MAbs. Immunoprecipitation experiments involving several of these strains indicated that the epitopes recognized by these MAbs resided in two different LOS molecules, both of which were synthesized by these particular Hib strains. In addition, Western blot (immunoblot) analysis of proteinase K-treated cell extracts of these strains that had been subjected to sodium dodecyl sulfate-polyacrylamide gradient gel electrophoresis revealed two different LOS staining patterns when they were probed independently with the two MAbs. Colony blot radioimmunoassay of hundreds of colonies of one of these Hib strains showed that each colony bound both MAbs. Immune electron microscopy confirmed that individual cells of this same Hib strain expressed both types of LOS molecule at the same time. An antibody accessibility radioimmunoassay was used to show that different Hib strains of this type varied in the relative amounts of each of the two MAbs that they could bind to their cell surfaces. These findings indicate that some Hib strains can synthesize two antigenically distinct LOS molecules simultaneously.
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PMID:Antigenic evidence for simultaneous expression of two different lipooligosaccharides by some strains of Haemophilus influenzae type b. 278 4

One major outer membrane protein (P1) of Haemophilus influenzae type b (Hib), with an apparent molecular weight of 34,000 (34K) as determined by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE), has been shown to be heat modifiable. After heating at 100 degrees C for 5 min in 2% SDS, the P1 protein exhibits an apparent molecular weight of 49,000 (49K) in SDS-PAGE. Monoclonal antibodies (MAbs) reactive with P1 bound to the surface of Hib, and one of these MAbs had a protective effect against the development of Hib bacteremia in an animal model for invasive Hib disease. A 6-kilobase Hib DNA insert containing the gene encoding this P1 protein was cloned into Escherichia coli by using the gamma gt11 expression vector. Recombinant phage expressing P1 were identified by screening phage plaques with a MAb directed against the P1 protein. Expression of the P1 protein by an E. coli lysogen carrying the recombinant phage was independent of both vegetative phage growth and induction of lacZ gene-directed transcription of the Hib DNA insert. The Hib DNA insert encoding the P1 protein was subcloned into the plasmid vector pBR322, and a transformant containing the recombinant plasmid pFRG100 was identified with the P1 protein-directed MAb in a colony blot-radioimmunoassay. Western blot (immunoblot) analysis determined that the recombinant P1 protein possessed heat-modifiability characteristics identical to those of the native Hib protein. The P1 protein was expressed on the surface of both the E. coli lysogen containing the recombinant phage and the E. coli transformant containing pFRG100. Western blot analysis of acute- and convalescent-phase sera from infants with Hib meningitis showed that antibodies in the convalescent-phase sera recognized the P1 protein expressed by the E. coli transformant containing pFRG100. The availability of this cloned Hib DNA insert encoding the Hib P1 protein and the expression of this protein on the surface of recombinant E. coli should facilitate the investigation of P1 for both its vaccinogenic potential and its functional role in the outer membrane of Hib.
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PMID:Cloning and expression in Escherichia coli of the gene encoding the heat-modifiable major outer membrane protein of Haemophilus influenzae type b. 282 80

Outer membrane protein P1 from Haemophilus influenzae type b MinnA was purified and partially characterized. Antiserum was generated against the purified protein and was used to immunologically screen a lamba EMBL3 genomic library prepared from strain MinnA DNA. A 4.2-kilobase-pair EcoRI-BamHI fragment containing the P1 gene was subcloned into pBR322. The recombinant protein was synthesized by Escherichia coli K-12, in which it localized to the outer membrane. The N-terminal sequence of the purified protein was determined and found to correspond to residues 23 through 36. The 22-amino-acid leader peptide had a typical structure, with two lysine residues near the amino terminus, a stretch of hydrophobic residues, and alanine residues at positions 20 and 22. The Mr of the processed protein was 47,752, which is in good agreement with the estimate of 50,000 from sodium dodecyl sulfate-polyacrylamide gel electrophoresis. Putative -35 and -10 promoter sequences were identified upstream from the translational start site. Codon usage was examined and determined to be substantially different than the codon preference in E. coli.
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PMID:Purification, cloning, and sequence of outer membrane protein P1 of Haemophilus influenzae type b. 284 61

One hundred fifty-eight patients, 21 years of age or less, presenting with culture-positive (Haemophilus influenzae or Streptococcus pneumoniae) conjunctivitis were treated with trimethoprim-polymyxin B (TP), gentamicin sulfate (GS) or sodium sulfacetamide (SS) ophthalmic solution for 10 days. Clinical response at 3 to 6 days after start of therapy was similar for all test agents: 26 of 55 (47%) patients cured, 25 of 55 (45%) improved for TP; 28 of 57 (49%) cured, 26 of 57 (46%) improved for GS; and 19 of 46 (41%) cured, 22 of 46 (48%) improved for SS. Clinical response at 2 to 7 days after completion of therapy was also similar: 46 of 55 (84%) patients cured, 5 of 55 (9%) improved for TP; 50 of 57 (88%) cured, 5 of 57 (9%) improved for GS; and 41 of 46 (89%) cured, 2 of 46 (4%) improved for SS. Bacteriologic response at 2 to 7 days after completion of therapy was similar for all antimicrobials: 44 of 55 (83%) patients for TP; 39 of 57 (68%) for GS; and 33 of 46 (72%) for SS.
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PMID:Comparison of three topical antimicrobials for acute bacterial conjunctivitis. 284 48

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

The structural and serological relatedness of the pilus proteins of several isolates of Haemophilus influenzae type b cultured from patients with invasive disease and from different anatomic sites within the same patient was examined. Epithelial cell-adherent variants of 25 nonadherent parent isolates were obtained by selection for organisms that adhered to human erythrocytes. Outer membrane protein analysis by sodium dodecyl sulfate-polyacrylamide gel electrophoresis revealed the presence of an additional 24- to 24.5-kilodalton protein among all adherent variants but absent from all nonadherent parent isolates. Polyclonal rabbit antiserum against the intact native pilus protein of H. influenzae M43 cross-reacted with 20 of 25 adherent H. influenzae in both immunodot and slide-agglutination assays. No differences in reactivity among isolates cultured from more than one anatomic site in the same patient were noted. Anti-M43 pilus antiserum had bactericidal activity against both the homologous strain and a heterologous strain that demonstrated serologic identity in the immunodot and slide agglutination assays. The adherence of these strains to human epithelial cells in vitro was inhibited by Fab fragments purified from the antipilus antiserum. These data indicate that a remarkable degree of homogeneity in pilin subunit size exists among the pili of H. influenzae type b and that major antigenic determinants are shared among most of these pili. Also, antibodies directed against H. influenzae pilus proteins may be able to contribute to host defenses through serum bactericidal activity and by blocking the adherence of this bacterium to host epithelial cells.
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PMID:Structural and serological relatedness of Haemophilus influenzae type b pili. 289 39

Hybrid cell lines producing monoclonal antibodies against Bordetella pertussis filamentous hemagglutinin (FHA) were established. The specificity of the antibodies was ascertained by enzyme-linked immunosorbent assay (ELISA), sandwich ELISA, and sodium dodecyl sulfate-polyacrylamide gel electrophoresis followed by electroblotting. The monoclonal antibody-based sandwich ELISA was developed for detection of B. pertussis FHA. The assay had a detection limit of B. pertussis FHA in concentrations ranging from 7 to 15 ng/ml. The assay was also able to detect whole B. pertussis, Bordetella parapertussis, and Bordetella bronchiseptica bacteria. No cross-reactions were observed with strains of Branhamella catarrhalis, Neisseria meningitidis, Haemophilus influenzae, Klebsiella pneumoniae, Legionella pneumophila, Streptococcus miteor, or Streptococcus pneumoniae. 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 FHA.
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PMID:Monoclonal antibody-based sandwich enzyme-linked immunosorbent assay for detection of Bordetella pertussis filamentous hemagglutinin. 290 74

The soluble whole-cell protein profiles of 15 isolates of Haemophilus paragallinarum were examined using standardized sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The patterns were reproducible and the isolates were similar overall. Despite this similarity, two protein profile types were recognized.
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PMID:Whole-cell protein profiles of Haemophilus paragallinarum as detected by polyacrylamide gel electrophoresis. 293 Mar 98


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