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

T. H. Kawula, S. M. Spinota, D. G. Klapper, J. G. Cannon

Research output: Contribution to journalArticle

27 Scopus citations

Abstract

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 prollne 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.

Original languageEnglish (US)
Pages (from-to)179-185
Number of pages7
JournalMolecular Microbiology
Volume1
Issue number2
DOIs
StatePublished - Sep 1987
Externally publishedYes

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology

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