A combination of potently neutralizing monoclonal antibodies isolated from an Indian convalescent donor protects against the SARS-CoV-2 Delta variant
Fig 5
X-ray crystallography of THSC20.HVTR04 and THSC20.HVTR26 complexed with SARS-CoV-2 RBD.
A. Schematic of THSC20.HVTR26 Fab (PDB 7Z0X, shown in dark and light green for heavy and light chains respectively) and THSC20.HVTR04 Fab (PBD 7Z0Y, shown in dark and light blue), bound to SARS-CoV-2 spike RBD (shown in purple/pink respectively). Structures were aligned by RBD. B. Surface view of SARS-CoV-2 RBD from PDB 7Z0X (top) or 7Z0Y (bottom), viewed from the angle of ACE2 approach, with the ACE2 binding site colored gold. Complementarity determining regions are shown in cartoon view, labelled, and colored as in A. C. Surface view of THSC20.HVTR26 Fab variable domains (colored as in A). RBD residues 475–489 and F456 are shown in purple cartoon and stick view. Key amino acids E484, T478, F486, and N487 are labelled. D. Surface view of THSC20.HVTR04 Fab variable domains (colored as in A). RBD residues 439–450 and 498–502 are shown in purple cartoon and stick view. Key amino acids V445, K444, P499, N439, and N440 are labelled. E. Primary sequence of SARS-CoV-2 RBD positions 410 to 510 (purple), and mutations associated with the Beta (cyan), Delta+ (lime), or Omicron (salmon) variants. The percentage of accessible surface for each amino acid that was bound by THSC20.HVTR04 or THSC20.HVTR26 was calculated (% buried surface area) and plotted using blue or green dots respectively, where each dot represents ~10% of the total solvent accessible surface area.