Fig. 2

YG8–1, YG8–2, and YG8–3 bound to the same region of HlgB. (a) The binding affinities of YG8–1, YG8–2, and YG8–3 to HlgB were determined by ELISA. HlgB was coated onto 96-well plates in the presence of serial dilutions of YG8–1, YG8–2, and YG8–3. Bound IgG was detected using horseradish peroxidase (HRP)-conjugated goat anti-human IgG. (b–d) YG8–1, YG8–2, and YG8–3 competed with each other in a concentration-dependent manner. YG8–1 was coated onto 96-well plates, and YG8–2 (b) or YG8–3 (c) was added at various concentrations after pre-incubated with GST-HlgB. YG8–2 was coated onto 96-well plates, and YG8–3 (d) was added at various concentrations after pre-incubation with GST-HlgB. Bound GST-HlgB was detected using an anti-GST antibody. Data are representative of three independent experiments and shown as the mean ± SD