Localization of and immune response to the lipid-modified azurin of the pathogenic Neisseria

J Infect Dis. 1990 Feb;161(2):336-9. doi: 10.1093/infdis/161.2.336.


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 Lax 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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Antibodies, Bacterial / biosynthesis*
  • Antibodies, Monoclonal / immunology
  • Antigens, Bacterial / analysis
  • Antigens, Bacterial / immunology
  • Azurin / analysis*
  • Azurin / immunology
  • Bacterial Proteins / analysis*
  • Bacteriophages / genetics
  • Blotting, Western
  • Cell Membrane / immunology
  • Epitopes / immunology
  • Gonorrhea / immunology
  • Humans
  • Meningococcal Infections / immunology
  • Neisseria gonorrhoeae / immunology*
  • Neisseria gonorrhoeae / ultrastructure
  • Neisseria meningitidis / immunology*
  • Neisseria meningitidis / ultrastructure


  • Antibodies, Bacterial
  • Antibodies, Monoclonal
  • Antigens, Bacterial
  • Bacterial Proteins
  • Epitopes
  • Azurin