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

The development of vaccines to prevent Neisseria infections hasbeen impeded byantigenic diversity of most Neisseria surface components. The lipid-modified azurin (Laz), one of two distinct sur-face 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 mem-brane, although unlike most outer membrane proteins it is Sarkosyl soluble. By probing recom-binant 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. The cell surfaces of the pathogenic Neisseria are marked by antigenic diversity, a feature that has impeded the devel-opment of vaccines to prevent Neisseria infections [1]. Only a few surface components are shared by the pathogenic Neis