1. Pentamer–8I21 Fab and Pentamer–9I6 Fab interactions and structural superpositions.
Pentamer–8I21 Fab and Pentamer–9I6 Fab interactions and structural superpositions. (A) Structure of the Pentamer–8I21 Fab complex, with 8I21 HC (H) and LC (L) colored in red and teal, respectively. The boxed region on the complex is shown on the right as an “open-book” view, revealing details of the Pentamer–8I21 Fab interface. Oligomannose residues linked to Asn85 and Asn118 of UL130 are shown as sticks. (B) Details of Pentamer–8I21 Fab interactions. Residues involved in direct H-bond interactions are shown with sticks, and direct bonds are depicted with blue dashes. (C) Structure of the Pentamer–9I6 Fab complex, with Pentamer depicted as cartoon and colored as in Fig. 1 and (A), and 9I6 HC and LC depicted as brown and light blue surfaces, respectively. A top view of the 9I6 epitope on Pentamer (boxed region) is shown as surface on the right and colored according to subunits (UL128, magenta; UL131A, blue), with residues contacting the HC and LC of 9I6 colored in brown and light blue, respectively. (D) gH-based superposition of the 4.0 Å–resolution (violet) and 3.0 Å–resolution (cyan) Pentamer–8I21 Fab and of the 9I6 (gold) and the 3.0 Å–resolution 8I21 (cyan) complexes viewed from the side and from the top. A UL130/ UL131A-based superposition of the 9I6 (gold) and the 3.0 Å–resolution 8I21 (cyan) Fab complexes is also shown in the upper right panel. Blue semitransparent arrows in (D) show the movements of secondary structure elements.
Sumana Chandramouli et al. Sci. Immunol. 2017;2:eaan1457
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