Figure 5
From: Exploring host-pathogen interactions through genome wide protein microarray analysis
Biophysical characterization of the NadA/LOX-1 interaction.
(a) Blank subtracted sensograms of NadA (500 - 7.8 nM) tested on covalently immobilized LOX-1 and (b) of LOX-1 (250 - 7.8 nM) tested on biotinylated NadA immobilized on SA biosensors. Association and dissociation curves were fitted in a 1:1 model. (c) Schematic representation of the NadA constructs used to determine NadA binding site on LOX-1. NadA gene, NadA (green), NadA24–170 (blue) and NadA91–342 (yellow) structure are shown. NadA24–89 head construct is represented only as a cartoon (rectangles) since it is not trimeric and not folded. Signal peptide (light blue) and membrane anchor (orange) are shown in the cartoon. (d) Blank subtracted sensograms of LOX-1 (200 nM) on biotinylated NadA (blue), NadA24–170 (green), NadA91–342 (yellow) and NadA24–89 (red). (e) Binding competition between LOX-1 and anti-NadA mAbs. Binding between NadA and LOX-1 is shown (blue). mAb 9F11 mapping NadA stalk does not inhibit the binding with NadA (red). mAb 3C11/H7 (violet) and mAb 1C9/A9 (green) mapping on NadA head abrogated NadA binding on LOX-1.
