Presentation: 2025 ND EPSCoR Annual conference
October 21, 2025, NDSU Memorial Union, Fargo, North Dakota
Interaction Dynamics of Borrelia Surface Proteins with Fibronectin
Kavindi
Madduma Hewage
Doctoral Student
University of North Dakota
Co-authors: Carlos Munoz, Doctaral Student, University of North Dakota, Mehmet Ozdogan, Nanofoundary Specialist, University of North Dakota, Catherine A. Brissette, Professor, University of North Dakota, Nuri Oncel, Professor, University of North Dakota, Grand Forks
Session
Poster number: 158
Nueta Room
Lyme disease, caused by the bacterium Borrelia 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 (ECM) proteins such as fibronectin (Fn). This study investigates the binding dynamics of B. burgdorferi surface proteins RevA, BBK32, BmpA, OspA, and OspC to Fn using atomic force microscopy-based single-molecule force spectroscopy (AFM-SMFS). 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. Lyme disease, B. burgdorferi, Adhesin Proteins, AFM, DFS.