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Berlin Brandenburg

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  • 1
    Language: English
    In: The Journal of Infectious Diseases, 1 February 1990, Vol.161(2), pp.336-339
    Description: The development of vaccines to prevent Neisseria infections has been impeded by antigenic diversity of most Neisseria surface components. The lipid-modified azurin (Laz), one of two distinct surface proteins recognized by the H.8 monoclonal antibody, is present in all pathogenic Neisseria. The mature protein has two domains; one contains an H.8 epitope and the other has extensive homology to azurins, a class of bacterial copper-binding proteins. The cellular location of Laz and the serum immune response to Laz were examined in patients with disseminated Neisseria infections. The data demonstrated that Laz is probably contained in the Neisseria outer membrane, although unlike most outer membrane proteins it is Sarkosyl soluble. By probing recombinant bacteriophages encoding the H.8 and azurin domains of Laz, results showed that whereas the H.8 epitope is immunogenic in patients with disseminated Neisseria infections, the azurin domain of Laz plays little role in eliciting an antibody response in these patients.
    Keywords: Biological sciences -- Biology -- Microbiology -- Epitopes ; Physical sciences -- Chemistry -- Chemical compounds -- Polyclonal antibodies ; Health sciences -- Medical conditions -- Infections -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Physical sciences -- Astronomy -- Astronomical cosmology -- Monoclonal antibodies ; Physical sciences -- Chemistry -- Chemical compounds -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies ; Health sciences -- Medical sciences -- Immunology -- Monoclonal antibodies
    ISSN: 00221899
    E-ISSN: 15376613
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  • 2
    Language: English
    In: The Journal of Infectious Diseases, 1 February 1990, Vol.161(2), pp.336-339
    Description: The development of vaccines to prevent Neisseria infections has been impeded by antigenic diversity of most Neisseria surface components. The lipid-modified azurin (Laz), one of two distinct surface proteins recognized by the H.8 monoclonal antibody, is present in all pathogenic Neisseria. The mature protein has two domains; one contains an H.8 epitope and the other has extensive homology to azurins, a class of bacterial copper-binding proteins. The cellular location of Laz and the serum immune response to Laz were examined in patients with disseminated Neisseria infections. The data demonstrated that Laz is probably contained in the Neisseria outer membrane, although unlike most outer membrane proteins it is Sarkosyl soluble. By probing recombinant bacteriophages encoding the H.8 and azurin domains of Laz, results showed that whereas the H.8 epitope is immunogenic in patients with disseminated Neisseria infections, the azurin domain of Laz plays little role in eliciting an antibody response in these patients.
    ISSN: 00221899
    Source: Archival Journals (JSTOR)
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  • 3
    Language: English
    In: Microbial Pathogenesis, 1990, Vol.9(6), pp.417-426
    Description: Twelve strains of Haemophilus ducreyi isolated primarily from chancroid outbreaks in North America were examined for the presence of pili by transmission electron microscopy. We identified piliated cells in 10 of the 12 strains. Pilin extracts were prepared from the mechanically sheared cells of the 12 H. ducreyi strains as well as the stably piliated H. influenzae strain R890 and its non-piliated parent R906. Pili were present in 12 out of 12 H. ducreyi extracts and in the R890 extract but not in the R906 preparation. Pili were purified by cycles of differential pH solubilization and crystalization. In SDS-PAGE, the preparation consisted predominantly of a protein whose apparent relative molecular mass was 24000 (24 k), and an electron micrograph showed that the preparation contained pili. Three H. ducreyi strains were passed 52 times on agar plates, and extracts prepared from these strains contained pili. There was no evidence of binding of erythrocytes obtained from nine mammalian and avian species to colonies of one of the stably piliated H. ducreyi strains. We conclude that H. ducreyi expressed pili, that the relative molecular mass of the pilin monomer was 24 k, that pilus expression was not readily lost in passage and that H. ducreyi pili may not bind to an erythrocyte receptor.
    Keywords: Haemophilus Ducreyi ; Pili ; Fimbriae ; Biology ; Chemistry
    ISSN: 0882-4010
    E-ISSN: 1096-1208
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  • 4
    Language: English
    In: Microbial Pathogenesis, 1990, Vol.8(5), pp.353-362
    Description: The non-enteric Gram-negative human pathogens, B. catarrhalis, H. ducreyi , H. influenzae , N. gonorrhoeae and N. meningitidis , do not have repeating O-antigens as part of their principle surface glycolipid, the lipooligosaccharide (LOS). Because they have similar LOS structures, we studied the conservation of LOS oligosaccharide epitopes among these organisms. Twentyone monoclonal antibodies (mAbs) generated by immunizing mice with H. influenzae, N. gonorrhoeae and N. meningitidis were studied for cross reactivity. Five mAbs generated against non-typable H. influenzae were the only strain-specific antibodies. Ten mAbs reacted to LOS epitope(s) common to a genera or species, and six mAbs bound to epitope(s) on the LOS of strains from different genera. Some cross reactive mAbs bound to LOS bands of similar molecular weights, while others bound to bands of varying molecular weights. mAb 3F11, whose epitope mimics a human blood-group antigen, bound to a 4.8 kDa LOS band in N. gonorrhoeae and H. ducreyi , two pathogens that infect genital epithelium. mAb 3D9, whose epitope consists of 2-keto-3-deoxyoctulosonic acid (KDO), reacted with different LOS bands in N. gonorrhoeae , H. influenzae and some R mutants of S. minnesota . A 14 kb restriction fragment containing lipooligosaccharide synthesis genes responsible for the assembly of the 3D9 epitope in H. influenzae hybridized to all H. influenzae strains tested but did not hybridize to gonococcal and S. minnesota strains that expressed this epitope. These studies demonstrate that conserved LOS epitope(s) exist among different species and genera of non-enteric human pathogens and that different genetic mechanisms may have evolved in these pathogens to assemble some of these conserved epitopes.
    Keywords: Lipooligosaccharides ; Epitopes ; Haemophilus ; Neisseria ; Branhamella ; Biology ; Chemistry
    ISSN: 0882-4010
    E-ISSN: 1096-1208
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