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. 2010 Oct 11;78(12):5314–5323. doi: 10.1128/IAI.00681-10

FIG. 4.

FIG. 4.

N. lactamica PorB binding to TLR2. (A) Dose-dependent binding of fluorescent N. lactamica PorB to the surface of BEAS-2B cells (106/ml, 100 μl) measured by flow cytometry (closed squares) is inhibited by coincubation with an excess amount of unlabeled N. lactamica PorB (100 μg/ml, open squares) ***, P = 0.0002 and *, P = 0.05 by unpaired t test. Binding of N. lactamica PorB is not inhibited by excess amount of N. meningitidis PorB (open triangles). Binding affinities (Kd) of N. lactamica PorB (B) and PamCSK4 (C) for TLR2 in vitro measured by modified ELISA. Plated N. lactamica PorB (0.6 up to 50 μg/ml) and Pam3CSK4 (0.12 up to 10 μg/ml) were incubated with 2 μg/ml of soluble TLR2:Fc chimera. Specific binding is detected via the Fc tag using horseradish peroxidase (HRP)-conjugated anti-mouse IgG in duplicate wells from triplicate experiments and is expressed as average A450 ± SD. BMAX and Kd are calculated according to the law of mass action.