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Conservation of peptide structure of outer membrane protein-macromolecular complex from Neisseria gonorrhoeae

M V Hansen, C E Wilde

    Infection and Immunity
    |March 1, 1984
    PubMed

    Insights

    Outer membrane protein-macromolecular complex (OMP-MC) from Neisseria gonorrhoeae shows high structural conservation across strains. This complex is a homopolymer of identical subunits, indicating conserved structure essential for gonococcal outer membrane function.

    Area of Science:

    • Microbiology
    • Structural Biology
    • Biochemistry

    Background:

    • Neisseria gonorrhoeae possesses an outer membrane protein complex (OMP-MC) crucial for its structure and function.
    • Understanding the structural conservation of OMP-MC is vital for comprehending gonococcal biology and potential therapeutic targets.

    Purpose of the Study:

    • To investigate the structural conservation of the outer membrane protein-macromolecular complex (OMP-MC) in Neisseria gonorrhoeae.
    • To determine if OMP-MC exhibits conserved structural features across different strains of N. gonorrhoeae.

    Main Methods:

    • Isoelectric point determination and amino-terminal amino acid sequencing of OMP-MC.
    • High-performance liquid chromatography (HPLC) for comparative tryptic peptide mapping.
    • Dansyl chloride labeling and dual-label peptide mapping techniques.

    Main Results:

    • OMP-MC subunits (76,000 daltons) from six N. gonorrhoeae strains showed restricted heterogeneity with an approximate pI of 7.6.
    • All investigated strains shared glycine as the amino-terminal amino acid, with no differences in the first 11 residues.
    • Peptide mapping revealed an extremely high degree of structural conservation within the OMP-MC complex.

    Conclusions:

    • OMP-MCs isolated from various N. gonorrhoeae strains exhibit significant structural homology.
    • The 800,000-dalton OMP-MC complex is a homopolymer, likely composed of 10 to 12 identical 76,000-dalton subunits.

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