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. 2020 Apr 1;5(2):e00195-20. doi: 10.1128/mSphere.00195-20

FIG 7.

FIG 7

T. pallidum interacts with LamR (aa 263–282) on brain endothelial cell surfaces. (A) Schematic illustration of characterized interaction regions of LamR (51, 71, 72, 74, 75). Elements include the predicted surface-exposed region (aa 101–295), C-terminal repeats (light blue box, aa 230–295), binding sites for laminin and the prion protein, including the peptide G region (yellow box; aa 161–180) and direct binding region (orange box; aa 205–229) and the neuroinvasive bacterial pathogen binding site (green box; aa 263–282). (B) T. pallidum attachment to brain endothelial cells (hCMEC/d3) was evaluated using immunofluorescence detection of adherent treponemes (FlaA; red) and hCMEC/d3 nuclei (DAPI; blue) at ×200 magnification from five FOV in duplicate from two independent experiments. Inhibition of T. pallidum attachment to hCMEC/d3 cells by antibodies was quantified as a percentage of the untreated no-antibody control (set at 100%). Results are presented as means ± SEM, and statistical analysis was performed by two-way ANOVA comparing T. pallidum binding to endothelial cells following hCMEC/d3 preincubation with anti-GAPDH (α-GAPDH) versus anti-LamR (aa 263–282) where P = 0.0037.