To confirm the residue assignation of the predicted epitopes for D29 on prM and E, clusters of 2-3 residue mutants were made on a prM-E construct that Puttikhunt and co-workers had previously shown to fold correctly when expressed in HEK293 [24] For the P3 (prM-E) epitope, two mutants, M1 (P56L-A, P58Q-G, P59N-G) and M2 (E246K-A, E247K-A) were generated (Fig. 6A ). Their reactivity with D29 Fab-IgG was tested by Western blot analysis, using h4G2 and m2H2 as control antibodies. All antibodies reacted with their respective protein targets for the non-mutated prM-E protein; however, binding of m2H2 and D29 Fab-IgG to the prM protein was almost completely abolished by mutation at the prM residues in M1 (Fig. 6B) . Mutation at the E residues within the P3 sequence (M2) on the other hand, did not have significant impact on the reactivity with D29 Fab-IgG (Fig. 6B) . Detection of both M1 and M2 by h4G2 verified the expression of both mutants. To verify the P9 (E) epitope, eight mutants were generated: