In current work, we used recombinant OspC protein derived from B. afzelii strain BRZ31 in the native homodimeric fold for mice immunization and following selection process to produce three mouse monoclonal antibodies able to bind to variable parts of up to five different OspC proteins. Applying the combination of mass spectrometry assisted epitope mapping and affinity based theoretical prediction we have localized regions responsible for antigen-antibody interactions and approximate epitopes' amino acid composition. Two mAbs (3F4 and 2A9) binds to linear epitopes located in previously described immunogenic regions in the exposed part of OspC protein. The third mAb (2D1) recognises highly conserved discontinuous epitope close to the ligand binding domain 1.

• Keywords
• Borrelia burgdorferi, OspC, epitope mapping, immunoprecipitation, monoclonal antibody, outer surface protein C, protein alignment,
• MeSH
• Antigens, Bacterial chemistry   genetics   immunology   MeSH
• Borrelia burgdorferi chemistry   genetics   immunology   MeSH
• Epitope Mapping * MeSH
• Protein Multimerization * MeSH
• Mice, Inbred BALB C MeSH
• Antibodies, Monoclonal, Murine-Derived chemistry   immunology   MeSH
• Mice MeSH
• Bacterial Outer Membrane Proteins chemistry   genetics   immunology   MeSH
• Protein Folding MeSH
• Animals MeSH
• Check Tag
• Mice MeSH
• Female MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• Antigens, Bacterial MeSH
• Antibodies, Monoclonal, Murine-Derived MeSH
• OspC protein MeSH Browser
• Bacterial Outer Membrane Proteins MeSH