Schematic drawing of prM/E proteins after synthesis and summary of the effect of C-terminal E domains on the recognition of E protein by mAbs.

<p>(A) Schematic drawing of prM/E proteins on ER membrane after synthesis. The topology of the stem (MH, EH1, EH2) and anchor (MT1, MT2, ET1, ET2) regions on membrane were based on a cryo-EM study of DENV virions at high resolution <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052600#pone.0052600-Zhang1" target="_blank">[18]</a>. The ectodomains of prM and E proteins were drawn disproportionately. SS: signal sequence. The numbers of E residues between domains were shown. (B) Summary of the effect of C-terminal E domains on the recognition of E protein by mAbs based on dot blot assay and capture ELISA. Epitope residues were determined by binding assays involving a panel of 67 alanine mutants of predicted surface-exposed E residues as described previously <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0052600#pone.0052600-Lin1" target="_blank">[33]</a>. ↓ indicates reduced binding (R.I.<0.4 in dot blot assay or <i>P</i><0.05 in capture ELISA) to mutant E proteins (prMEd421, prMEd395, Ed421); →indicates binding was not reduced. ND, not done.