Abstract

The diverse antigenic structure of Borrelia burgdorferi sensu lato (s.l.) and the low degree of protein sequence conservation between genospecies causes many limitations in serodiagnosis of Lyme disease (LD). Using expression systems based on Escherichia coli, five monovalent B. burgdorferi s.l. recombinant proteins were produced. i.e., BB0108, BB0126, BB0298, BB0323, BB0689 (each in three variants derived from Borrelia afzelii, Borrelia burgdorferi sensu stricto, Borrelia garinii) and four multivalent chimeric proteins containing fragments of BmpA, BBK32 and BBA64 antigens. Data obtained from bioinformatic analysis of the amino acid sequence and linear epitope mapping with polypeptide array were used to design chimeric proteins. Subsequently, Western blot (WB) and ELISA determined the reactivity of the obtained antigens with specific anti-B. burgdorferi s.l. antibodies contained in human sera. The results indicate that BB0108 and BB0323 show moderate reactivity with specific IgG and IgM in WB and ELISA, regardless of the antigen variant used. At the same time, the obtained chimeric proteins showed high reactivity with IgG in WB. In addition, it has been shown that epitope mapping can be useful in the design of chimeric proteins that exhibit reactivity with a specific antibody isotype to increase the effectiveness of Lyme disease serodiagnosis.

Author (1)