Fig. 3
Structural basis for broad ebolavirus neutralization by antibody CA45. a Surface representation of CA45-bound EBOV GPΔMuc trimer (left) colored by Shannon sequence entropy on a scale of increasing entropy from white to green (GP1) and white to orange (GP2), with border of CA45 footprint colored raspberry. Close-up view rotated by 60° (right), with bound CA45 heavy and light chains shown in purple and gray, respectively. b Comparison of mean entropies of CA45 epitope with those of other neutralizing antibodies and inhibitors that target the GP1–GP2 interface, by mean entropy per GP-binding site residue (left) or normalized by individual residue buried surface area (right). c Surface representation of CA45-bound EBOV GPΔMuc trimer (left), colored by subunit and subdomain, with CA45 epitope residues conserved in > 99.5% of ebolavirus isolates colored white and variable residues colored dark gray. Close-up and rotated view of CA45 epitope with bound antibody shown as colored in a. d Sequence alignment of CA45 epitope residues across representative ebolavirus sequences. Residues are listed in order of increasing sequence entropy, with entropy values listed and graphed above. Sequence logo reflects sequence variation across representative ebolavirus sequences from previous outbreaks38, with residues colored by amino acid type. CA45-specific alanine sensitive mutations and escape mutation are boxed in red and yellow, respectively. Residues unique in RESTV and TAFV colored teal and violet, respectively. e “Open-book” view of right panel in c with surface representation of antibody shown rotated by 180° relative to view in c. Alanine sensitive mutations and escape mutation mapped onto surface of GP in red and yellow respectively (left), with corresponding interface residues on antibody colored similarly (right). f “Open-book” view of right panel in c, with residue positions unique to RESTV and TAFV mapped onto surface of GP in teal and violet, respectively, with corresponding interface residues on antibody colored similarly (right)
