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Localization of a conserved epitope and an azurin‐like domain in the H.8 protein of pathogenic Neisseria
Author(s) -
Kawula T. H.,
Spinota S. M.,
Klapper D. G.,
Can J. G.
Publication year - 1987
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.1987.tb00510.x
Subject(s) - biology , epitope , neisseria , neisseria meningitidis , peptide sequence , amino acid , homology (biology) , conserved sequence , alanine , neisseria gonorrhoeae , microbiology and biotechnology , biochemistry , gene , genetics , bacteria , antibody
Summary 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.