Fig. 6: Epitope conservation and mAb cross-reactivity.

a Structural and sequence analysis of the WRAIR-5021 and WRAIR-5001 footprints across sarbecoviruses. (Right) The epitope residues are numbered according to the Wuhan reference sequence; the strength of the interaction between the mAb and the RBD is indicated by the height and color of the histogram bars above the sequence alignment. Sequences are ordered based on their phylogenetic relationships based on a maximum likelihood phylogenetic tree derived from the RBD protein sequences. (Left) The RBD structure is shown in surface representation and depicts mutations between SARS-CoV-1 and SARS-CoV-2 in red; the WRAIR-5021 and WRAIR-5001 epitopes are outlined and labeled. (Right) Sequence alignment of mAb epitopes across sarbecoviruses. b The binding of mAbs was measured with a set of sarbecovirus RBDs using BLI to assess cross-reactivity. Heat-map represents the relative binding strengths for WRAIR-mAbs. Coloring legend indicating the relative binding strength is shown on the right. c ACE2 blocking activity of WRAIR RBD mAbs in a BLI-based assay. mAbs were assessed for their ability to block human ACE2 binding to selected sarbecovirus clade 1b or 1a RBDs. Source data are provided as a Source Data file.