To verify the specificity of the identified motifs, nine representative clones were selected (Table 1) and assessed for their ability to bind D29 Fab-IgG by direct ELISA. No crossreaction by these peptide-phage clones with control antibodies was observed, confirming that the binding to D29 Fab-IgG was specific (Fig. 4B) . The peptide-phage clones were then tested for their ability to inhibit D29 Fab-IgG's binding to immobilized DENV2. Although most of the selected peptide-phage clones only weakly inhibited D29 Fab-IgG's binding to DENV2, clone P3 (Cluster 1) and P9 (Cluster 2) significantly competed by 30% and 70%, respectively (Fig. 4C ). Significant inhibition of binding to both prM and E was also observed on Western blot for P9, however no noticeable inhibition was observed for P3 (Fig. 4D) . Alignment of P3 and P9 peptide sequences to their respective clusters revealed 9 and 11 aa match, respectively (Fig. 5 ). This may explain the difference in the ability of the two peptide phage clones to inhibit binding of D29 Fab-IgG.