Figure 2
Mapping of binding site of VTN in SE36. (a) Schematic representation of SE36. The “8” and “S” indicate octamer repeat and serine rich region, respectively. “RGD” indicates RGD motif. The number 178 denotes the position of polyserine sequence present in PfSERA5 but deleted in SE3613. SE36-1 to -4 denote truncated recombinant forms. P1 to P15 are synthetic peptides19. (b) Reactivity of VTN in NHS and HTS against each truncated SE36 recombinant. Each recombinant was adsorbed to microtiter plate and NHS and HTS were added at 1:2000 dilution. (c) Reactivity of the purified VTN against each truncated SE36 recombinant. Each recombinant was adsorbed to microtiter plate and the purified VTN was added at 2 μg/mL concentration. (d) Reactivity of VTN in NHS and HTS against each synthetic peptide. Each synthetic peptide was adsorbed to microtiter plate (0.3 μM) and NHS and HTS were added at 1:2000 dilution. (e) Reactivity of the purified VTN against each synthetic peptide. Each synthetic peptide was adsorbed to microtiter plate and the purified VTN was added at 2 μg/mL concentration. Results in (b–e) are expressed as means ± standard deviation (SD) from three independent experiments. In (b and d), statistical analyses between NHS and HTS were performed using a Mann-Whitney U test. No significant differences were found.
