Lyme disease, caused by the bacterium Borrelia burgdorferi (B. burgdorferi), is a significant public health concern in North America, with approximately 500 000 cases reported annually in the United States. The dissemination of B. burgdorferi from the initial tick bite site to various tissues is facilitated by surface adhesins that bind to extracellular matrix proteins such as fibronectin (Fn). This study investigates the binding dynamics of B. burgdorferi surface proteins RevA, BBK32, BmpA, OspA, FlaB, and OspC to Fn using atomic force microscopy-based single-molecule force spectroscopy. Our results demonstrate that RevA and BBK32 form strong, stable bonds with Fn, highlighting their roles as key mediators of host-cell attachment. By quantifying the rupture forces and kinetic parameters of these interactions, we provide a deeper understanding of B. burgdorferi adhesion mechanics and offer insights into potential therapeutic strategies targeting early bacterial attachment.
Hewage et al. (Thu,) studied this question.
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