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Collagen binding to Staphylococcus aureus.

D Holderbaum, G S Hall, L A Ehrhart

    Infection and Immunity
    |November 1, 1986
    PubMed
    Summary
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    Live Staphylococcus aureus (S. aureus) exhibits significantly higher collagen-binding affinity than killed bacteria. This high-affinity binding, mediated by a protein component, may facilitate bacterial adhesion and invasion in host tissues.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Immunology

    Background:

    • Staphylococcus aureus (S. aureus) exhibits variable collagen binding among different strains.
    • Previous studies focused on heat-killed, formaldehyde-fixed S. aureus.

    Purpose of the Study:

    • To investigate collagen binding affinity in live and differently killed S. aureus strains.
    • To characterize the nature and specificity of the collagen binding site.

    Main Methods:

    • Compared collagen binding affinity of live, gamma-irradiated, and heat-killed S. aureus (Cowan 1 strain).
    • Assessed binding reversibility, kinetics, and inhibition by other proteins.
    • Examined collagen binding across four different S. aureus strains.

    Main Results:

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    • Live S. aureus (Cowan 1) demonstrated over 100-fold greater collagen-binding affinity (Kd = 9.7 x 10(-11) M) than heat-killed bacteria (Kd = 4.3 x 10(-8) M).
    • Gamma-irradiated S. aureus showed binding indistinguishable from live organisms, suggesting minimal alteration of binding moieties.
    • Binding was rapid, reversible, protein-dependent (eliminated by trypsin), and not inhibited by fibronectin, fibrinogen, C1q, or IgG.
    • Two strains (Cowan 1, ATCC 25923) exhibited specific, saturable binding, while two others (Woods, S4) showed no binding.

    Conclusions:

    • Certain S. aureus strains possess high-affinity collagen-binding sites.
    • This binding mechanism may contribute to bacterial adhesion and invasion of host tissues.
    • The binding site appears to be a surface protein distinct from known receptors for fibronectin, fibrinogen, C1q, and IgG.