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Bacteroides intermedius binds fibrinogen.

M S Lantz, L M Switalski, K S Kornman

    Journal of Bacteriology
    |August 1, 1985
    PubMed
    Summary
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    Bacteroides intermedius bacteria bind human fibrinogen specifically and with high affinity. This binding, along with fibrinogen degradation by the bacteria, may facilitate tissue adherence.

    Area of Science:

    • Microbiology
    • Biochemistry
    • Molecular Biology

    Background:

    • Bacteroides intermedius is a bacterium found in the human oral cavity.
    • Fibrinogen is a key protein in blood clotting and wound healing.

    Purpose of the Study:

    • To characterize the binding of Bacteroides intermedius to human fibrinogen.
    • To investigate the fibrinogenolytic activity of Bacteroides intermedius.
    • To explore the role of fibrinogen binding in bacterial adherence.

    Main Methods:

    • Characterization of binding kinetics (time dependence, reversibility, saturation, specificity).
    • Quantification of fibrinogen binding per bacterial cell and determination of dissociation constant.
    • Assay of fibrinogenolytic activity and its inhibition by protease inhibitors.

    Related Experiment Videos

  • Use of 125I-labeled fibrinogen to study degradation at the cell surface.

    • Main Results:

    • Bacteroides intermedius exhibits time-dependent, partially reversible, saturable, and specific binding to human fibrinogen.
    • Maximum binding is approximately 3,500 fibrinogen molecules per cell with a dissociation constant of 1.7 x 10(-11) M.
    • Bacteria possess fibrinogenolytic activity, partially inhibited by protease inhibitors, with enhanced degradation of cell-associated fibrinogen.

    Conclusions:

    • Bacteroides intermedius binds human fibrinogen with high affinity.
    • The bacteria degrade fibrinogen, likely at the cell surface.
    • Fibrinogen binding may serve as a mechanism for bacterial tissue adherence.