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Immunization of mice withBorrelia burgdorferi decorin binding protein A (DbpA), one of two gene products of thedbpBA locus, has been shown recently to confer protection against challenge. Hyperimmune DbpA antiserum killed a large number ofB. burgdorferi sensu lato isolates of diverse phylogeny and origin, suggesting conservation of the protective epitope(s). In order to evaluate the heterogeneity of DbpA and DbpB and to facilitate defining the conserved epitope(s) of these antigens, the sequences of thedbpA genes from 29B. burgdorferi sensu lato isolates and of thedbpB genes from 15B. burgdorferi sensu lato isolates were determined. The predicted DbpA sequences were fairly heterogeneous among the isolates (58.3 to 100% similarity), but DbpA sequences with the highest similarity tended to group into species previously defined by well-characterized chromosomal markers. In contrast, the predicted DbpB sequences were highly conserved (96.3 to 100% similarity). Substantial diversity in DbpA sequence was seen among isolates previously shown to be killed by antiserum against a single DbpA, suggesting that one or more conserved protective epitopes are composed of noncontiguous amino acids. The observation of individualdbpA alleles with sequence elements characteristic of more than oneB. burgdorferi sensu lato species was consistent with a role for genetic recombination in the generation ofdbpA diversity.

Molecular Analysis of Sequence Heterogeneity among Genes Encoding Decorin Binding Proteins A and B of Borrelia burgdorferi Sensu Lato