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Fibronectin binding to a Streptococcus pyogenes strain.

P Speziale, M Höök, L M Switalski

    Journal of Bacteriology
    |February 1, 1984
    PubMed
    Summary
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    Staphylococcus aureus and Streptococcus pyogenes bind to fibronectin using specific protein receptors. These receptors, located on the bacterial surface, interact with distinct regions of fibronectin, aiding bacterial attachment and potentially opsonization.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Immunology

    Background:

    • Staphylococcus aureus is known to bind fibronectin, a process potentially crucial for bacterial attachment and opsonization.
    • Recent findings indicate that some Streptococcus strains (serological groups A, C, and G) also bind fibronectin.

    Purpose of the Study:

    • To characterize the fibronectin-binding interaction in Streptococcus pyogenes.
    • To identify and analyze the nature of fibronectin receptors on streptococci and staphylococci.

    Main Methods:

    • Radiolabeled fibronectin ([125I]fibronectin) binding assays to bacterial cells.
    • Protease and trypsin digestion of bacterial cells to release and characterize fibronectin receptors.
    • Affinity chromatography using fibronectin-Sepharose and Sepharose 4B for receptor purification.

    Related Experiment Videos

  • Enzymatic digestion (papain) and antibody-based assays to determine receptor composition.
  • Analysis of isolated fibronectin fragments for bacterial binding specificity.

    • Main Results:

    • Streptococcus pyogenes exhibits time-dependent, functionally irreversible, and specific fibronectin binding.
    • Protease treatment of bacteria significantly reduces fibronectin binding; trypsin digestion releases active fibronectin receptors.
    • Purified fibronectin receptors inhibit [125I]fibronectin binding to bacteria.
    • Receptors are proteinaceous, as indicated by inactivation with papain and lack of binding to anti-lipoteichoic acid antibodies.
    • Both S. aureus and S. pyogenes preferentially bind an N-terminal fibronectin fragment (approx. 25,000 Mr); S. pyogenes also binds a slightly smaller fragment (approx. 23,000 Mr).

    Conclusions:

    • Streptococcus pyogenes possesses specific protein receptors for fibronectin, similar to Staphylococcus aureus.
    • These bacterial fibronectin receptors interact with specific domains of the fibronectin molecule.
    • The identified binding mechanism is relevant to bacterial adhesion and host-pathogen interactions.