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Characterization of the interaction between fibronectin andTreponema pallidum

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Abstract

The interaction betweenTreponema pallidum and rabbit plasma fibronectin was characterized. Fibronectin was isolated from rabbit plasma and radioiodinated by the lactoperoxidase method. Fibronectin bound to the surface ofT. pallidum, reaching saturation at approximately 54 μg/ml. The association affinity constant was 2.85×107 M −1, much lower than that ofStaphylococcus aureus (5.6×109 M −1) Fibronectin binding plateaued within 15 min at 20° and 37°C, with some reelution at 37°C by 30 min. Little fibronectin, bound toT. pallidum at 4°C. The greatest amount of fibronectin was bound at the lowest pH tested (pH 6.0); the poorest binding was at pH 7.5. Approximately 90% of the binding was reversible in the presence of excess unlabeled fibronectin. The data indicate a more dynamic and weaker interaction betweenT. pallidum and fibronectin than that seen withS. aureus.

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  1. University of Texas Health Science Center at Houston, Department of Pathology and Laboratory Medicine, Houston, Texas, USA

    Bret M. Steiner & Stewart Sell

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  1. Bret M. Steiner
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Steiner, B.M., Sell, S. Characterization of the interaction between fibronectin andTreponema pallidum . Current Microbiology 12, 157–161 (1985). https://doi.org/10.1007/BF01567669

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