Table 1.
Apparent dissociation constants (KD) of HlgA and HlgC for chemokine receptors as determined by Surface Plasmon Resonance analyses.
| Protein | Receptor | Affinities (nM) | |
|---|---|---|---|
| KD | SD | ||
| HlgA | CXCR1 | 5.69 | ± 1.94 |
| CXCR2 | 27.20 | ± 5.54 | |
| CCR2 | 3.51 | ± 0.29 | |
| C5aR | NI | ||
| HlgC | CXCR1 | NI | |
| CXCR2 | NI | ||
| CCR2 | NI | ||
| C5aR | 5.64 | ± 1.53 | |
Results of three experimental replicates are shown. No interaction observed (NI) indicates that no binding was observed within the limits of detection. Average capture levels are as follows: CXCR1 683 RU ± 67; CXCR2 696 RU ± 58; CCR2 1056 RU ± 136; C5aR 713 RU ± 88. Average Rmax (maximum response units at saturation) for interactions between HlgA and chemokine receptors are as follows: CXCR1 15.1 RU ± 1.9; CXCR2 20.5 ± 3.3; CCR2 21.4 RU ± 1.4. Average Rmax for interaction between HlgC and C5aR is 16.3 RU ± 0.7.