Table 2. Relative affinities of LigB proteins for fibronectin and fibrinogen.
Fibronectin | Fibrinogen | ||||
LigB | Kd a | %b | Kd a | %b | Category |
7′-12 | 23±8 | 100 | 34±11 | 100 | full binding |
7′-11 | 27±14c | 100 | see below | - | |
8-12 | 26±3 | 100 | n.d. | - | |
9-12 | 22±3 | 100 | 37±13 | 100 | |
9-11 | 31±14d | 100 | 27±9d | 100 | |
7′-11 | see above | - | 63 (28) | 54 | moderate/low |
7′-10 | 77±47c, e | 30 | 207 (165) | 16 | |
9-10 | 252±30d, e | 9 | 169±40d | 20 | |
7′-9 | weak | - | weak | - | weak |
10-12 | weak | - | weak | - | |
10-11 | inactive | - | n.d. | - | inactive |
11-12 | inactive | - | inactive | - |
Apparent dissociation constant estimated by ELISA. Mean and standard deviation from at least three separate experiments is shown, except where the mean from two experiments is shown with the range in parentheses; n.d., not determined.
Relative affinity compared to LigB7′-12; where 100% is shown, the affinities are statistically equivalent.
Significant 2.9-fold enhancement by repeat 11 (P<0.01).
Significant 8.1-fold enhancement by repeat 11 for fibronectin binding (P<0.001), and 6.3-fold stimulation for fibrinogen binding (P<0.001).
Some dependence on repeats 7′ and 8 in the absence of repeat 11, giving a 3.3-fold effect (P<0.001).