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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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