Epitope mapping of Borrelia burgdorferi OspC protein in homodimeric fold

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Authors

NOREK Adam JANDA Lubomír

Year of publication 2017
Type Article in Periodical
Magazine / Source Protein Science
MU Faculty or unit

Central European Institute of Technology

Citation
Web http://onlinelibrary.wiley.com/doi/10.1002/pro.3125/abstract
Doi http://dx.doi.org/10.1002/pro.3125
Field Biochemistry
Keywords epitope mapping; monoclonal antibody; outer surface protein C; OspC; Borrelia burgdorferi; protein alignment; immunoprecipitation
Description 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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