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Fibronectin binding to Staphylococcus aureus.

R A Proctor, D F Mosher, P J Olbrantz

    The Journal of Biological Chemistry
    |December 25, 1982
    PubMed
    Summary
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    This study shows that Staphylococcus aureus binds fibronectin, a key protein in immune responses. Optimal binding occurs at pH 7.4 or higher, revealing insights into bacterial interactions with host tissues.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Immunology

    Background:

    • Bacteria interact with macromolecules like fibronectin, which can act as opsonins or tissue-adherence factors.
    • Soluble fibronectin is crucial for phagocytic removal of bacteria, while insoluble fibronectin bridges bacteria and host tissues.

    Purpose of the Study:

    • To characterize the binding of soluble plasma fibronectin to Staphylococcus aureus.
    • To understand the interactions between fibronectin and S. aureus as a foundation for further research.

    Main Methods:

    • Studied the binding of radio-labeled fibronectin (125I-fibronectin) to clinical and laboratory strains of S. aureus.
    • Separated bound fibronectin from free fibronectin using centrifugation.
    • Determined specific binding by subtracting binding in the presence of excess fibronectin from total binding.

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    Main Results:

    • Fibronectin bound saturably, irreversibly, and non-covalently to S. aureus at pH 7.4 or greater.
    • Optimal S. aureus harvesting conditions for maximum fibronectin binding sites were identified (logarithmic phase, pH 8.4, brain-heart infusion media).
    • Several substances including dextrans, fibrinogen, and protein A did not affect fibronectin binding; non-saturable binding occurred below pH 7.0, peaking at pH 5.8.
    • Significant strain-dependent variations in fibronectin binding capacity were observed, with S. aureus ATCC 25923 showing 7500 binding sites/organism at pH 7.4.

    Conclusions:

    • Fibronectin binding to S. aureus is pH-dependent and saturable under specific conditions.
    • The study provides quantitative data on fibronectin-S. aureus interactions, including binding sites and association constants.
    • Understanding these interactions is vital for developing strategies against S. aureus infections.