Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold |
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Authors: | Adam Norek Lubomír Janda |
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Institution: | 1. CEITEC – Central European Institute of Technology, Masaryk University, Brno, Czech Republic;2. Department of Animal Physiology and Immunology, Institute of Experimental Biology, Faculty of Science, Masaryk University, Brno, Czech Republic |
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Abstract: | 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. |
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Keywords: | epitope mapping monoclonal antibody outer surface protein C OspC Borrelia burgdorferi protein alignment immunoprecipitation |
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