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. Author manuscript; available in PMC: 2021 May 13.
Published in final edited form as: Cell Host Microbe. 2020 May 13;27(5):710–724.e7. doi: 10.1016/j.chom.2020.04.007

Figure 2. DENV3/1 recombinant EDI loss-of-function chimeras reveal previously unidentified DENV3 hmAb characteristics.

Figure 2.

Chimeric DENV3 viruses encoding progressively larger blocks of DENV1 E glycoprotein sequence were used to interrogate the role of these transplanted regions in loss of DENV3 antibody function.

A) Four DENV3/1 chimeric viruses with increasing portions of DENV1 residues in a DENV3 backbone. DENV3/1 chimera PyMOL representations of DENV1 residues (orange) transplanted into DENV3 backbone (grey). Number of amino acids changed is in parenthesis.

B) Amino acid alignment of changed residues in DENV3/1 chimeras. DENV3 residues are shown in blue. DENV1 residues are shown in orange. A tissue culture adaptation in DENV3/1 A is shown in yellow. Blank spaces in DENV3 indicate residues not present in DENV1.

C) DENV3/1 chimeras contain DENV1-specific, DENV3-specific and cross-reactive epitopes. EC50 values of Vero-81 cell FRNT of DENV3-specific hmAb 5J7, cross-reactive hmAb EDEI C8 and DENV1-specific hmAbs 1F4 and 14c10.

D) Panel of 15 hmAbs were sorted into 3 groups by EC50 values of Vero-81 cell FRNT against chimeric DENV3/1 viruses. Group 1: Ten hmAbs do not neutralize any members of the chimeric dengue 3/1 panel. Group 2: hmAbs DENV-115, DENV-290 and −419 neutralize all chimeric DENV3/1 viruses (red circles). Group 3: hmAbs DENV-66 and −144 neutralize only DENV3/1 EDI-A and-B (blue arrows).