FIG. 6.

Receptor-binding residues modeled on CatL-cleaved EBOV GP trimer structure. (A) Surface representation of the ZEBOV-GP trimer structure (as reported in reference 10) depicting N-glycan sites in the head region (red) (side view; left panel) and residues important for virus entry (blue) (top view; right panel). GP1 is shown in shades of orange and GP2 in shades of green. (B) The surface-modeled CatL-cleaved EBOV-GP trimer structure (based on reference 10) reveals the complete removal of all N-linked glycans (red) from the head region surface (side view; left panel) and exposes the conserved core of the RBD and critical residues for virus entry (blue) (top view; right panel). The approximately 20-Å by 15-Å footprint reported by Lee et al., which contains residues important for virus entry, is indicated in the black circled regions of the top view (right panel). (C) Using a ribbon diagram and transparent surface rendering, the model of CatL-cleaved ZEBOV-GP complexed to the heavy (blue) and light (purple) chains of KZ52 depicts unobstructed binding of KZ52 to the processed EBOV GP and supports the surface plasmon resonance binding data. The color scheme of EBOV GP is the same as in Fig. 5. All graphic representations were produced with PyMOL.