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Gonococcal pili. Primary structure and receptor binding domain.

G K Schoolnik, R Fernandez, J Y Tai

    The Journal of Experimental Medicine
    |May 1, 1984
    PubMed
    Summary
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    Structural analysis of gonococcal pilin reveals key regions for cell adherence and immune evasion. Understanding pilin structure aids in developing strategies against Neisseria gonorrhoeae.

    Area of Science:

    • Microbiology
    • Structural Biology
    • Immunology

    Background:

    • Neisseria gonorrhoeae uses pili for host cell attachment and immune system evasion.
    • Pilin, the major subunit of gonococcal pili, exhibits significant antigenic diversity.

    Purpose of the Study:

    • To determine the complete amino acid sequence of gonococcal pilin.
    • To elucidate the structural basis of pilin's adherence function, antigenic diversity, and polymeric structure.

    Main Methods:

    • Amino acid sequencing of pilin from gonococcal strains MS11 and R10.
    • Preparation of a soluble monomeric pilus peptide (TC-2) via arginine-specific digestion.
    • Analysis of conserved and variable regions, including homology with eukaryotic actins.

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    Main Results:

    • The MS11 pilin sequence comprises 159 amino acids with disulfide-linked cysteines and phosphoserine residues.
    • The TC-2 peptide (residues 31-111) binds to human endocervical cells, indicating its role in receptor binding.
    • Variable regions (CNBr-3) contribute to antigenic diversity, featuring charged residue changes in hydrophilic segments and beta-turns.
    • Significant homology (50%) was found between gonococcal pilin residues 2-21 and eukaryotic actin residues 202-221, forming a hydrophobic face on helical wheels.
    • The N-terminal region (TC-1, residues 1-30) shows aggregation properties, suggesting its involvement in stabilizing pilus structure.

    Conclusions:

    • The study identifies specific pilin regions responsible for cell adherence, antigenic variation, and pilus assembly.
    • Structural insights into pilin provide a foundation for understanding gonococcal pathogenesis and developing targeted interventions.