Table 3.
Effect of DOC on the binding affinity between engineered IpaD π-helix mutants and IpaB28–226
| IpaD Mutant | Kd (μM ± SD) a,b
|
|
|---|---|---|
| − DOC | + DOC | |
| Wild-type IpaD | - | 2.0 ± 0.7 |
| D144A | - | 0.4 ± 0.2* |
| N146A | - | 1.4 ± 0.3* |
| Y149A | - | 0.5 ± 0.3* |
| D144A/N146A | - | 0.6 ± 0.2* |
| D144A/Y149A | - | 0.3 ± 0.2* |
| N146A/Y149A | - | 2.1 ± 0.6 |
| D144A/N146A/Y149A | 7.4 ± 2.4 | 2.2 ± 0.8 |
a
Apparent dissociation constants between IpaD and IpaB28–226 are reported as the mean ± standard deviation resulting from at least three independent analyses.
b
Kd values are only reported for conditions resulting in fits with R2 values ≥ 0.95.
*
Indicates statistical difference from the wild-type IpaD complement strain (one-way ANOVA followed by a Dunnett’s post test, p ≤ 0.01)).