Figure 2: m336 precisely targets the DPP4-binding site on MERS-CoV RBD. | Nature Communications

Figure 2: m336 precisely targets the DPP4-binding site on MERS-CoV RBD.

From: Junctional and allele-specific residues are critical for MERS-CoV neutralization by an exceptionally potent germline-like antibody

Figure 2

(a) Mapping of the m336 epitope and DPP4-binding site on MERS-CoV RBD sequence. Residues interacting with DPP4 and m336 are marked with purple and green dots, respectively. MERS-CoV residue numbers are labelled above the sequence. (b) Plot of buried surface areas of MERS-CoV RBD residues that interact with both m336 and DPP4. Residue numbers of MERS-CoV RBD residues are labelled for each data point. (c) Epitope of m336 (green) overlaps with DPP4-binding site (purple) on the MERS-CoV RBD (orange). (d) Comparison of the electrostatic potential surfaces of the MERS-CoV RBD-contacting regions on m336 and DPP4. Molecular surfaces are coloured red for acidic areas and blue for basic areas with the RBD footprints highlighted in orange and olive boundary lines. (e) When superposed on MERS-CoV RBD, the volume of m336 overlaps with that of RBD-bound DPP4 indicating antibody m336 exploits similar angle of approach as receptor DPP4 to engage the MERS-CoV and achieves neutralization by blocking DPP4 binding to MERS-CoV.

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