Table 1 Dissociation constants of antibody Fabs and fold-changes in apparent affinity obtained from ITC.

From: Structural and biophysical correlation of anti-NANP antibodies with in vivo protection against P. falciparum

mAb

Kd to NPNA2 (nM)

Kd to NPNA4 (nM)

Kd to NPNA6 (nM)

Mean Kd fold-change NPNA2 vs NPNA6

239

641 ± 38

20 ± 2

10 ± 1

64

311

152 ± 11

14 ± 5

19 ± 4

8

337

1523 ± 11

71 ± 1

59 ± 14

26

356

8272 ± 1284

82 ± 18

30 ± 6

276

364

47 ± 2

28 ± 2

27 ± 3

2

395

6152 ± 196

1423 ± 404

999 ± 231

6

mAb

Kd to NPNA2 (nM)

Kd to NPNA4 (nM)

Kd to NPNA6 (nM)

Mean Kd fold-change NPNA4 vs. NPNA6a

224

14245 ± 4507

126 ± 14

141 ± 8

1

366

1348 ± 110

1770 ± 82

479 ± 17

4

397

2743 ± 156

255 ± 10

92 ± 8

3

399

13345 ± 2017

5922 ± 1122

94 ± 30

63

317

132 ± 62

70 ± 12

111 ± 23

1

  1. aThe fold-change calculation for these two sets of antibodies is between NPNA4 and NPNA6 as it was shown by the crystal structures that their minimal epitopes are NPNA3. Thus, the comparison between NPNA2 and NPNA6 would not be appropriate here.
Back to article page