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. Author manuscript; available in PMC: 2020 Mar 15.
Published in final edited form as: Curr Opin Virol. 2019 Mar 15;34:140–148. doi: 10.1016/j.coviro.2019.01.003

Figure 3.

Figure 3.

Cryptic epitopes engaged by ADI-15946, ADI-15878, and CA45. (a) The N-terminal pocket (red) is shown on the surface of EBOV GP (PDB: 5JQ3 [60]) with the N-terminal tail removed. (b) The N-terminal tail engages the highly conserved N-terminal pocket directly through I504 and D506, likely impeding recognition by the immune system. (c) ADI-15878 engages the N-terminal pocket through heavy chain CDRs 1–3, most importantly with W103. (d) The 310-pocket (blue) is shown with the β17–β18 loop removed. (e) The β17–β18 loop engages the 310-pocket primarily through two hydrophobic-aromatic residues (F290 and W291). (f) ADI-15946 engages this pocket through CDR-H3, with three hydrophobic residues (W110, L111, and L112) localized in the binding pocket. (g) The DFF cavity targeted by CA45 is shown in cyan. This pocket is bound by the cathepsin cleavage loop (h) in apo-GP. CDR H3 of CA45 binds into this pocket (i) with F100a appearing to bind similarly to F194 of the cathepsin cleavage loop.