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

T. H. Kawula, Stanley Spinola, D. G. Klapper, J. G. Cannon

Research output: Contribution to journalArticle

26 Citations (Scopus)

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 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.

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

Fingerprint

Azurin
Neisseria
Epitopes
Amino Acid Sequence
Monoclonal Antibodies
Neisseria meningitidis
Neisseria gonorrhoeae
Consensus Sequence
Protein Sorting Signals
Proline
Alanine
Lipoproteins
Glutamic Acid
Membrane Proteins
Proteins
Bacteria
Amino Acids
Genes

ASJC Scopus subject areas

  • Molecular Biology
  • Microbiology

Cite this

Localization of a conserved epitope and an azurin-like domain in the H.8 protein of pathogenic Neisseria. / Kawula, T. H.; Spinola, Stanley; Klapper, D. G.; Cannon, J. G.

In: Molecular Microbiology, Vol. 1, No. 2, 09.1987, p. 179-185.

Research output: Contribution to journalArticle

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