In response to the progressive nature of Lyme disease, direct diagnostic testing of Borrelia burgdorferi surface proteins was proposed as a quicker and more sensitive alternative to the current indirect detection methods. To determine the ability of novel monoclonal antibodies to detect the surface lipoproteins BmpA and OspC, recombinant fragments of these proteins were created. These fragments were tested against the putative diagnostic antibodies via western blotting as a means to map the epitope of each of the proteins that the respective antibodies recognize. All BmpA fragments with deletions on the N-terminal end exhibited reactivity, indicating that the epitope is within the 100 amino acids of the C-terminus of the protein. While the region requires further refinement, the known high conservation of BmpA across Lyme disease-causing Borrelia isolates and the proximity of the epitope to the C-terminal end suggest that anti-BmpA monoclonal antibodies may be an effective tool for direct diagnostics. Comparatively, the OspC fragments featured deletions from both the N-terminal and C-terminal end of the protein, with a loss of reactivity occurring when the C-terminal end was deleted. Further analysis of the suspected region of antibody recognition determined the epitope to be in 25 amino acids within the C-terminus of the protein. The amino acid sequence of OspC across Lyme disease-causing Borrelia is known to have significant variability. Multiple alignment analysis of the 21 known OspC type variants (type A-U) focused on the 25 amino acid region of the putative epitope of the anti-OspC monoclonal antibody demonstrated significant variability on the N-terminal end of the epitope region and high conservation on the C-terminus. Mapping of the region of antibody reactivity onto the 3D structure of OspC suggested that the epitope region is likely accessible for antibody binding when OspC is expressed on the surface of B. burgdorferi in its native form. Although further investigation into the epitope is needed, the accessibility and possible conservation of the area indicate that anti-OspC monoclonal antibodies have potential as an effective direct diagnostic tool.