Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria

• Published in: Molecular microbiology Vol. 1; no. 2; p. 179
• Main Authors: Kawula, T H, Spinola, S M, Klapper, D G, Cannon, J G
• Format: Journal Article
• Language: English
• Published: England 01-09-1987
• Subjects: Amino Acid Sequence; Azurin - genetics; Azurin - immunology; Bacterial Outer Membrane Proteins - genetics; Bacterial Outer Membrane Proteins - immunology; Bacterial Proteins - genetics; Base Sequence; Cloning, Molecular; Enzyme-Linked Immunosorbent Assay; Epitopes - genetics; Molecular Sequence Data; Neisseria gonorrhoeae - genetics; Neisseria meningitidis - genetics; Repetitive Sequences, Nucleic Acid
• ISSN: 0950-382X
• DOI: 10.1111/j.1365-2958.1987.tb00510.x

The pathogenic neisseriae, Neisseria gonorrhoeae and Neisseria meningitidis, possess an outer membrane protein, H.8, which contains a conserved monoclonal antibody (MAb)-binding epitope in all strains tested. We have cloned and sequenced a meningococcal H.8 gene, and determined the characteristics of the predicted protein. The predicted signal peptide has features characteristic of a prokaryotic lipoprotein. The region at the N-terminal end of the mature protein (39 amino acids) is primarily composed of alanine, glutamate and proline residues arranged in imperfect repeats with the consensus sequence AAEAP. The epitope for H.8 MAb-binding was localized to a 20-amino-acid sequence within this region. The remainder of the predicted amino acid sequence shows extensive homology to azurins, which are small blue copper-binding proteins found in a limited number of species of pathogenic bacteria.