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. Author manuscript; available in PMC: 2019 Sep 5.
Published in final edited form as: Nat Microbiol. 2018 Nov 5;4(1):124–133. doi: 10.1038/s41564-018-0275-7

Fig. 5 |. The cryoEM structure of EV-D68 in complex with 15C5 and 11G1.

Fig. 5 |

a, Iso-contoured views of the cryoEM map (radially coloured) of the immune complex EV-D68-M:15C5:11G1. The EV-D68 capsid is bound with 60 copies of Fab 15C5 at three-fold axes and 60 copies of Fab 11G1 at five-fold axes, respectively, b, A quarter of the central section of the cryoEM map in a; the radii are marked by the arcs, c, Surface representation shows the interaction interface of Fab 11G1. Each Fab 11G1 (heavy chain: magenta; light chain: orange) binds across two neighbouring VP1s (light blue and blue) of the capsid. Footprints of the VH and VL of the Fab on the capsid are coloured with magenta and orange, d, A close-up view (wire diagram) of the interaction interface between 11G1 and the capsid shows the conformational changes (indicated with black arrows) of the VP1 BC loop and HI loop before (grey) and after (coloured) binding with 11G1. e,f, Close-up views of the interaction interfaces between the capsid and the light (e) or heavy chain (f) of Fab 11G1. Potential hydrogen bonds are marked by yellow dashed lines.