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. 2014 Aug;82(8):3186–3198. doi: 10.1128/IAI.02036-14

TABLE 4.

Kinetic data and dissociation constants for the interaction of rDbpA proteins with decorin or dermatan sulfate determined by SPR and quantitative ELISA

Protein Ligand Kd (μM)a Kd (μM)b kon (104 s−1 M−1)b koff (s−1)b
rDbpA Decorin 0.32 ± 0.05 0.29 ± 0.06 35.05 ± 6.15 0.099 ± 0.003
Dermatan sulfate 0.47 ± 0.05 0.46 ± 0.08 5.21 ± 0.16 0.024 ± 0.004
rDbpAK51A Decorin 0.74 ± 0.05 0.79 ± 0.03 12.6 ± 1.70 0.099 ± 0.018
Dermatan sulfate 1.45 ± 0.37 1.17 ± 0.28 2.57 ± 0.32 0.030 ± 0.003
rDbpAK82A Decorin NBc NB NB NB
Dermatan sulfate NB NB NB NB
rDbpAK124A Decorin 0.28 ± 0.04 0.28 ± 0.14 29.25 ± 7.50 0.084 ± 0.01
Dermatan sulfate 0.47 ± 0.02 0.54 ± 0.11 5.92 ± 0.53 0.032 ± 0.009
rDbpAK163A Decorin NB NB NB NB
Dermatan sulfate NB NB NB NB
rDbpAK170A Decorin NB NB NB NB
Dermatan sulfate NB NB NB NB
rDbpAK177A Decorin 0.30 ± 0.03 0.20 ± 0.06 35.70 ± 1.10 0.071 ± 0.004
Dermatan sulfate 0.48 ± 0.04 0.53 ± 0.09 3.34 ± 0.18 0.018 ± 0.004
a

Calculated from the ELISA experiments shown in Fig. S1 in the supplemental material. The Kd values are the means ± standard deviations (SD) from three independent experiments.

b

Calculated from the SPR experiments shown in Fig. S2 in the supplemental material. kon, association rate constant; koff, dissociation rate constant. The Kd, kon, and koff values are the means ± SD from three independent experiments.

c

NB, no binding. rDbpAK82A, rDbpAK163A, and rDbpAK170A bound decorin and dermatan sulfate so poorly that curve-fitting software could not accurately calculate the Kd, kon, and koff values. Since these values were not available, it was not possible to do a statistical analysis of decorin or dermatan sulfate binding between these mutants and WT DbpA.