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Fig. 3 | Journal of Translational Medicine

Fig. 3

From: Application of Nanotrap technology for high sensitivity measurement of urinary outer surface protein A carboxyl-terminus domain in early stage Lyme borreliosis

Fig. 3

Narrow OspA236-239 region is conserved across different Borrelia species and binds to mAb clone 0551. a Crystallography structure of OspA (Protein Data Bank PDB ID# 1FJ1): the epitope of the mAb is highlighted in red. b BLAST search against different Borrelia strains and species shows that the mAb clone 0551 epitope is highly conserved whereas the flanking regions are variable. c Synthetic peptides mimicking the OspA236-239 region interact with the mAb in a dose dependent manner (dot blot analysis, 1, 2, 3 = Bb Lyme antigen 0.5, 5, and 10 ng, respectively; 4, 5, and 6 = OspA219-253 0.5, 1, and 2 μg, respectively; 7, 8, and 9 = OspA219-235 0.5, 1, and 2 μg, respectively; 10, 11, and 12 = OspA240-253 0.5, 1, and 2 μg, respectively). Negative control peptides (OspA219-235 and OspA240-253) containing flanking regions but lacking the OspA236-239 sequence were devoid of immunoreactivity with the mAb clone 0551

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