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. Author manuscript; available in PMC: 2019 Apr 17.
Published in final edited form as: Immunity. 2018 Apr 17;48(4):799–811.e9. doi: 10.1016/j.immuni.2018.03.026

Figure 3. AMMO1 targets a unique discontinuous epitope on gH/gL.

Figure 3

(A) CryoEM reconstruction of gH/gL-gp42-AMMO1 complex at 4.8 Å resolution. (B) 90° rotation from A: AMMO1 heavy chain is shown in dark purple, AMMO1 light chain in light purple, gL in light blue, gH D-I in dark blue, gH D-II in wheat, gH D-III in green, gH D-IV in yellow and gp42 in cherry. (C–D) Ribbon diagram of the gH/gL/gp42-AMMO1 atomic model rendered with the same colors as panels A and B. (E) Zoomed-in view of the AMMO1 epitope with regions of interest labeled. (F) AMMO1 footprint on the gH/gL-gp42 complex. Only the AMMO1 CDR loops are shown interacting with gH/gL-gp42 rendered in surface representation. Residues that have been identified as being important for AMMO1 binding (K73 and Y76) are shown in dark red. (G) The gH N60 glycan is shown in stick representation in the corresponding region of cryoEM density to highlight the putative contacts made with AMMO1. The star shows the position of the gH KGD motif. See Figures S4 and S5.